Fungal strains having reduced or eliminated mycotoxin, ethanol, and / or pigment production capacity

Abstract

Disclosed herein are filamentous fungal strains having reduced or eliminated mycotoxin production capability, having enhanced glucose regulation and uptake, and / or having a high degree of desirable coloration. Methods of producing such filamentous fungal strains are also provided, as are food and textile materials comprising the same.

Description

[0001]Fungal Strains Having Reduced or Eliminated Mycotoxin, Ethanol, and / or Pigment Production Capacity CROSS REFERENCE TO RELATED APPLICATIONS This application claims the benefit of priority of U.S. provisional patent application 63 / 582,032, filed 12 September 2023, the entirety of which is hereby incorporated by reference in its entirety, for all purposes. FIELD The present disclosure relates to filamentous fungal strains which produce reduced levels of mycotoxins and methods of producing such strains. Fungal mycelium biomass, in various formats, comprising the filamentous fungal strains is also disclosed, as is the use of the same in preparing food materials in embodiments where the fungal strains are edible. BACKGROUND A mycotoxin is a low-molecular-weight metabolite produced by fungi that is toxic and capable of causing both sickness and death in humans and animals. Mycotoxins are structurally diverse and differ in their mechanisms of toxicity. They are of concern in food safety and agriculture because of their toxicity and frequent accumulation in crops used for food and feed. Examples of mycotoxins capable of causing human and animal illness include beauvericin, citrinin, fumonisins, fusarins such as fusaric acid, aflatoxins, ochratoxins, zearalenone, ergot alkaloids such as ergotamine, and others. A single fungal species may produce many different mycotoxins, and several different species of fungi may all produce the same mycotoxin. Fumonisins, are produced by a number of fungi including certain species of the genus Fusarium, including F. anthophilum, F. fujikuroi, F. nygamai, F. oxysporum, and F. proliferatum (Munkvold and Desjardins 1997). Fumonisins are structurally similar to sphinganine, a sphingolipid biosynthetic intermediate. These mycotoxins disrupt sphingolipid metabolism in plants and animals by inhibiting the enzyme sphinganine N- acyltransferase and causing the accumulation of sphingoid bases, which is thought to be responsible for the majority of fumonisin-induced toxicity. At least 28 fumonisins have been isolated from fungi, and they are classified into four groups, fumonisin A, B, C, and P series. Fumonisins B (FB), the major fumonisins produced in nature, are polyketides consisting of a linear 19- or 20-carbon backbone with hydroxyl, methyl, and tricarballylic acid moieties at various positions along the base chain. Examples include fumonisin 1 (FB1), fumonisin B2 (FB2), and fumonisin B3 (FB3) and fumonisin B4 (FB4). Further, FB6 is an isomer of FB1, having hydroxyl groups at C3, C4, and C5, instead of at C3, C5, and C10 in FB1. Beauvericin is a mycotoxin that is a depsipeptide of the enniatin antibiotic family and is produced by many fungi, including Beaveria bassiana and Fusarium spp. Beauvericin is toxic to human cells and tissues and is known to have insecticidal and antimicrobial activity, including against fungi and viruses. Beauvericin is synthesized by beauvericin synthase, an enzyme that catalyzes depsipeptide formation via a nonribosomal thiol- templated mechanism. With the increase in global demand for food, in particular nutritious food with high protein content, coupled with a growing awareness of environmental costs associated with the production of animal-based foods, the search for innovative alternatives to traditional non-animal sources of food has intensified. In recent years, edible fungi have emerged as a potential source of a non-animal based food. These include, inter alia, Fusarium venenatum (formerly classified as Fusarium graminearum), a strain of which has been formulated into food products and marketed under the brand name QUORN®. Additionally, Fusarium strain flavolapis (ATCC Accession Deposit No. PTA-10698, also referred to as F. flavolapis) has also been formulated into high quality nutritious, protein-rich food (see e.g., WO 2016 / 004380, WO 2017 / 151684, WO 2019 / 046480 and PCT / US20 / 20152). The presence of mycotoxins in these, or any other, species of edible fungi would be problematic. If measurable levels of one or more mycotoxins in an edible fungi is above commercially recognized thresholds, those levels must be reduced for any products made from such fungi (food or otherwise) to be deemed safe for use or consumption by humans and animals, including aquaculture. Additionally, the use of glucose as a carbon source in the fermentation of mycelium has many benefits. Glucose is inexpensive, the most abundantly available carbon source and, because it is the preferred carbon source for a majority of living organisms, it is utilized efficiently. However, the use of glucose as a carbon source in fermentation methods can also lead to ethanol production, which is problematic. Ethanol inhibits growth of fungi, for example by altering the permeability of the cell membranes, and in high enough doses ethanol is toxic to fungi. Because of factors like this, alternative and far more expensive carbon sources are often used for the fermentative production of fungi. Finally, fungi are useful for the production of numerous food and beverages. Fungi itself can be the primary component in fermented foods and beverages, and in the modern food industry fungi have become financially important food components, as many are highly nutritious and can be incorporated into countless food applications. Generally, fungi that are white or that have mild or neutral colors are desirable for food uses. White or neutral colored fungal biomass can be used as a “blank canvas” for the production of food items, while maintaining a product that is visually appealing to a consumer. However, many fungi are naturally non-white and / or are not naturally a neutral color. Further, some fungi are known to produce pigments during fermentation that may not be optimal for the production of food products. Such pigments, which can produce colors such as pink, purple, grey, brown, or others, can be problematic for the production of food products that consumers will purchase and enjoy. There is thus a need for edible fungal strains in which production of mycotoxins is either reduced or abolished. There is also a need for the production of edible fungal strains that can be grown on cheaper, more environmentally friendly carbon sources such as glucose. There is also a need for edible fungal strains that are white and / or neutral in color, that can be used to facilitate food production in an aesthetically pleasing manner. SUMMARY The present disclosure provides meaningful solutions to the problems associated with the prior art. In a first aspect, the present disclosure provides a filamentous fungal strain, comprising one or more reduced function mutations in one or more mycotoxin-associated genes. In embodiments, the one or more mutations comprise at least one loss of function mutation. In embodiments, the one or more mutations are selected from the group consisting of one or more knockout mutations, one or more introduced premature stop codons, one or more introduced point mutations, and combinations thereof. In embodiments, each point mutation independently produces a frameshift mutation, a nonsense mutation, or a missense mutation. In embodiments, the mycotoxin is selected from the group consisting of aflatoxins, beauvericin, fusarins, citrinin, ochratoxins, trichothecenes, zearalenone, fumonisins, mycophenolic acid, penicillic acid, patulin, cyclopiazonic acid, ergot alkaloids, cyclopiazonic acid, gliotoxin, sterigmatocystin, and combinations thereof. In embodiments, production of a mycotoxin in the strain is reduced as compared to a filamentous fungal strain of the same species without the one or more mutations in one or more mycotoxin-associated genes when grown under the same conditions. In embodiments, the mycotoxin is beauvericin or a fumonisin. In embodiments, the mycotoxin is beauvericin and the mycotoxin-associated gene is beauvericin synthase. In embodiments, the filamentous fungal strain is incapable of producing beauvericin. In embodiments, the filamentous fungal strain produces less beauvericin than a strain of the same filamentous fungi without the one or more mutations. In embodiments, the filamentous fungal strain produces a modified beauvericin demonstrating reduced or eliminated functionality, or both, as compared to a strain of the same filamentous fungi without the one or more mutations. In embodiments, the mycotoxin is a fumonisin and the mycotoxin-associated gene is selected from the group consisting of Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof. In embodiments, the mycotoxin-associated gene is Fum1, Fum6, Fum8, or combinations thereof. In embodiments, the filamentous fungal strain is incapable of producing fumonisin. In embodiments, the filamentous fungal strain produces less fumonisin than a strain of the same filamentous fungi without the one or more mutations. In embodiments, the filamentous fungal strain produces a modified fumonisin demonstrating reduced or eliminated functionality, or both, as compared to a strain of the same filamentous fungi without the one or more mutations. In embodiments, the mutant filamentous fungus further comprises one or more rco- 3 gene mutations; and / or a mutation in a pigment-associated gene. In embodiments, the pigment-associated gene is selected from the group consisting of bik1, bik2, bik3, bik4, bik5, and bik6. In embodiments, the filamentous fungal strain is selected from Rhizopus oligosporus, Ustilago esculenta, Hericulum erinaceus, Polyporous squamosus, Grifola fondosa, Hypsizygus marmoreus, Hypsizygus ulmarius, Calocybe gambosa, Pholiota nameko, Calvatia gigantea, Agaricus bisporus, Stropharia rugosoannulata, Hypholoma lateritium, Pleurotus eryngii, Pleurotus ostreatus, Pleurotus ostreatus var. columbinus, Tuber borchii, Morchella esculenta, Morchella conica, Morchella importuna, Sparassis crispa, Fusarium venenatum, Fusarium venenatum A3 / 5, Fusarium strain flavolapis (ATCC Accession Deposit No. PTA-10698), Disciotis venosa, Clonostachys rosea, Cordyceps militaris, Trametes versicolor, Ganoderma lucidum, Flammulina velutipes, Lentinula edodes, Pleurotus djamor, Pleurotus ostreatus, and Leucoagaricus spp. In embodiments, the filamentous fungal strain is Fusarium strain flavolapis (ATCC Accession Deposit No. PTA-10698). This first aspect also provides a method of making a mutant filamentous fungal strain, comprising: exposing the fungal strain to a physical mutagen or a chemical mutagen, and / or performing site-directed mutagenesis on the fungal strain; wherein the exposing or the performing introduces at least one reduction of function mutation into at least one mycotoxin-associated gene. In embodiments, the mutation comprises at least one loss of function mutation. In embodiments, the mutation comprises at least one mutation selected from the group consisting of a knockout mutation, one or more introduced premature stop codons, one or more introduced point mutations, and combinations thereof. In embodiments, each point mutation independently produces a frameshift mutation, a nonsense mutation, or a missense mutation. In embodiments, the physical mutagen is selected from gamma rays, X rays, UV light, fast neutrons, thermal neutrons, beta particles, alpha particles, and combinations thereof. In embodiments, the chemical mutagen is selected from ethyl methyl sulfate, nitrogen mustards, mitomycin, methyl methane sulfonate, diethyl sulfate, nitrosoguanidine, ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, acridine orange, ethidium bromide, proflavin, daunorubicin, and combinations thereof. In embodiments, the site-directed mutagenesis is selected from knockout mutations, oligonucleotide-directed mutagenesis, Kunkel’s method, cassette mutagenesis, PCR mutagenesis, homologous recombination, CRISPR / Cas9 mutagenesis, Delitto Perfetto, transplacement "pop-in pop-out," direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker, direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker using long homologous regions, in vivo site-directed mutagenesis with synthetic oligonucleotides, and combinations thereof. In embodiments, the method further comprises confirming the presence of the at least one reduction of function mutation in the genes. In embodiments, the method further comprises exposing the strain to adaptive laboratory evolution to develop a characteristic in the strain selected from a higher growth rate, greater cell density, diminished mycotoxin production, and combinations thereof. In embodiments, the adaptive laboratory evolution occurs by serially diluting the mutant strain under selective pressure. This first aspect also provides a mutant strain of Fusarium flavolapis having one or more reduction of function mutations introduced into its Fum1 gene or having its Fum1 gene deleted. In embodiments, the mutant strain is incapable of producing more than 10 ppb of fumonisin. In embodiments, the mutant strain is incapable of producing detectable levels of fumonisin. In embodiments, the mutant strain is incapable of producing fumonisin. In embodiments, the mutant strain produces less fumonisin than a Fusarium flavolapis strain without the mutations or deletion. In embodiments, the mutant strain produces a modified fumonisin demonstrating reduced or eliminated functionality, or both, as compared to a Fusarium flavolapis strain without the mutations or deletion. In embodiments, the mutant strain’s Fum1 gene sequence is at least about 90% identical to SEQ ID NO:1. In embodiments, the mutant strain produces a fumonisin protein that is at least 90% identical to SEQ ID NO: 3. In embodiments, the mutant strain’s Fum1 amino acid sequence comprises an amino acid change from tryptophan to a premature stop codon at position 953. In embodiments, the mutant strain produces a fumonisin protein having the amino acid sequence of SEQ ID NO: 4. This first aspect also provides a mutant strain of Fusarium flavolapis having one or more reduction of function mutations introduced into its bea1 gene, or having its bea1 gene deleted. In embodiments, the mutant strain is incapable of producing beauvericin. In embodiments, the mutant strain produces less beauvericin than a Fusarium flavolapis strain without the mutations or deletion. In embodiments, the mutant strain produces a modified beauvericin demonstrating reduced or eliminated functionality, or both, as compared to a Fusarium flavolapis strain without the mutations or deletion. In embodiments, the mutant strains’ bea1 gene sequence is at least about 90% identical to SEQ ID NO:5. In embodiments, the mutant strain produces a beauvericin protein that is at least 90% identical to SEQ ID NO: 7. In embodiments, the mutant strain’s bea1 amino acid sequence comprises an amino acid change from tryptophan to a premature stop codon at position 1135. In embodiments, the mutant strain produces a beauvericin protein having the amino acid sequence of SEQ ID NO: 8. This first aspect also provides a mutant strain of Fusarium venenatum having one or more reduction of function mutations introduced into its bea1 gene, or having its bea1 gene deleted. In embodiments, the mutant strain is incapable of producing beauvericin. In embodiments, the mutant strain produces less beauvericin than a Fusarium venenatum strain without the mutations or deletion. In embodiments, the mutant strain produces a modified beauvericin demonstrating reduced or eliminated functionality, or both, as compared to a Fusarium venenatum strain without the mutations or deletion. In a second aspect, the present disclosure provides a filamentous fungal strain, comprising one or more one or more reduced function mutations in one or more pigment- associated genes. In embodiments, the one or more mutations comprises at least one loss of function mutation. In embodiments, the one or more mutations are selected from the group consisting of a knockout mutation, one or more introduced premature stop codons, one or more introduced point mutations, and combinations thereof. In embodiments, each point mutation independently produces a frameshift mutation, a nonsense mutation, or a missense mutation. In embodiments, the strain is incapable of producing bikaverin. In embodiments, the filamentous fungal strain produces less bikaverin than a filamentous fungal strain of the same species without the mutations. In embodiments, the strain produces a modified bikaverin demonstrating reduced or eliminated functionality, or both, as compared to a filamentous fungal strain of the same species without the mutations. In embodiments, the pigment-associated gene is selected from the group consisting of bik1, bik2, bik3, bik4, bik5, and bik6. In embodiments, the pigment-associated gene is selected from the group consisting of bik1, bik2, and bik3. In embodiments, the pigment- associated gene is bik1. In embodiments, production of a pigment in the strain is reduced as compared to a filamentous fungal strain of the same species without the one or more mutations. In embodiments, the strain is grown under conditions of nitrogen limitation during submerged fermentation. In embodiments, a biomass of the filamentous fungal strain has a whiter color than a biomass of a filamentous fungal strain of the same species without the one or more mutations. In embodiments, a biomass of the filamentous fungal strain has a Whiteness Index of at least 7.5. In embodiments, a biomass of the filamentous fungal strain has a high L* value. In embodiments, a biomass of the filamentous fungal strain has an L* value of about 75 – about 100 or about 50 – about 100. In embodiments, a biomass of the filamentous fungal strain has a low a* value and a low b* value. In embodiments, an a* value and a b* value of a biomass of the filamentous fungal strain is each independently about 0 – about 30, or about 0 – about 25. In embodiments, the strain further comprises an rco-3 gene mutation, a mutation in a mycotoxin-associated gene, or both. In embodiments, the mycotoxin-associated gene is selected from the group consisting of bea1, Fum1, Fum6, and Fum8. In embodiments, the filamentous fungus is selected from the group consisting of Rhizopus oligosporus, Ustilago esculenta, Hericulum erinaceus, Polyporous squamosus, Grifola fondosa, Hypsizygus marmoreus, Hypsizygus ulmarius, Calocybe gambosa, Pholiota nameko, Calvatia gigantea, Agaricus bisporus, Stropharia rugosoannulata, Hypholoma lateritium, Pleurotus eryngii, Pleurotus ostreatus, Pleurotus ostreatus var. columbinus, Tuber borchii, Morchella esculenta, Morchella conica, Morchella importuna, Sparassis crispa, Fusarium venenatum, Fusarium venenatum A3 / 5, Fusarium strain flavolapis (ATCC Accession Deposit No. PTA-10698), Disciotis venosa, Clonostachys rosea, Cordyceps militaris, Trametes versicolor, Ganoderma lucidum, Flammulina velutipes, Lentinula edodes, Pleurotus djamor, Pleurotus ostreatus, and Leucoagaricus spp. In embodiments, the filamentous fungus is Fusarium strain flavolapis (ATCC Accession Deposit No. PTA-10698). This second aspect also provides a method of making a mutant filamentous fungal strain, comprising exposing the fungal strain to a physical mutagen or a chemical mutagen, and / or performing site-directed mutagenesis on the fungal strain; wherein the exposing or the performing introduces at least one reduction of function mutation into at least one pigment-associated gene. In embodiments, the mutation comprises at least one loss of function mutation. In embodiments, the mutation comprises at least one mutation selected from the group consisting of one or more knockout mutations, one or more introduced premature stop codons, one or more introduced point mutations, and combinations thereof. In embodiments, each point mutation independently produces a frameshift mutation, a nonsense mutation, or a missense mutation. In embodiments, the physical mutagen is selected from gamma rays, X rays, UV light, fast neutrons, thermal neutrons, beta particles, alpha particles, and combinations thereof. In embodiments, the chemical mutagen is selected from ethyl methyl sulfate, nitrogen mustards, mitomycin, methyl methane sulfonate, diethyl sulfate, nitrosoguanidine, ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, acridine orange, ethidium bromide, proflavin, daunorubicin, and combinations thereof. In some embodiments, the chemical mutagen is selected from ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, and combinations thereof. In embodiments, the site- directed mutagenesis is selected from oligonucleotide-directed mutagenesis, Kunkel’s method, cassette mutagenesis, PCR mutagenesis, homologous recombination, CRISPR / Cas9 mutagenesis, Delitto Perfetto, transplacement "pop-in pop-out," direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker, direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker using long homologous regions, in vivo site-directed mutagenesis with synthetic oligonucleotides, and combinations thereof. In embodiments, the method further comprises confirming the presence of the reduction of function mutation in the gene. In embodiments, the method further comprises exposing the strain to adaptive laboratory evolution to develop a characteristic in the strain selected from a higher growth rate, greater cell density, diminished pigment production, and combinations thereof. In embodiments, the adaptive laboratory evolution occurs by serially diluting the mutant strain under selective pressure. This second aspect also provides a mutant strain of Fusarium flavolapis having one or more premature stop codons and / or one or more point mutations introduced into its bik1 gene or having its bik1 gene deleted. In embodiments, the mutant strain is incapable of producing detectable levels of bikaverin. In embodiments, the mutant strain is incapable of producing bikaverin. In embodiments, the mutant strain produces less bikaverin than a Fusarium flavolapis strain without the stop codons or point mutations. In embodiments, the mutant strain produces a modified bikaverin demonstrating reduced or eliminated functionality, or both, as compared to a Fusarium flavolapis strain without the stop codons or point mutations. In embodiments, the bik1 gene sequence is at least about 90% identical to SEQ ID NO:18. In embodiments, the mutant strain produces a bikaverin synthase protein that is at least 90% identical to SEQ ID NO: 20. In a third aspect, the present disclosure provides a filamentous fungal strain, comprising one or more one or more reduced function mutations in one or more ethanol- associated genes. In embodiments, the one or more mutations comprise at least one loss of function mutation. In embodiments, the one or more mutations are selected from the group consisting of one or more knockout mutations, one or more introduced premature stop codons, one or more introduced point mutations, and combinations thereof. In embodiments, each point mutation independently produces a frameshift mutation, a nonsense mutation, or a missense mutation. In embodiments, production of ethanol in the strain when grown using glucose as a carbon source is reduced as compared to a filamentous fungal strain of the same species without the one or more mutations. In embodiments, the strain exhibits increased growth when grown using glucose as a carbon source as compared to a filamentous fungal strain of the same species without the one or more mutations. In embodiments, growth occurs via submerged fermentation. In embodiments, growth occurs via liquid surface fermentation. In embodiments, the filamentous fungal strain is incapable of producing ethanol. In embodiments, the filamentous fungal strain produces less ethanol than a filamentous fungal strain of the same species without the mutations. In embodiments, the filamentous fungal strain exhibits increased growth using glucose as a carbon source when compared to a filamentous fungal strain of the same species without the mutations. In embodiments, the one or more ethanol-associated genes are selected from the group consisting of rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof. In embodiments, the one or more ethanol-associated genes are selected from the group consisting of rco-3, col-26, glt-1, cre1, hgt, and combinations thereof. In embodiments, the ethanol-associated gene is rco-3. In embodiments, ethanol production in the strain when grown using glucose as a carbon source is reduced as compared to a filamentous fungal strain of the same species comprising a wild-type rco-3 gene. In embodiments, growth in the strain when grown using glucose as a carbon source is increased as compared to a filamentous fungal strain of the same species comprising a wild-type rco-3 gene. In embodiments, growth occurs via submerged fermentation. In embodiments, growth occurs via liquid surface fermentation. In embodiments, the strain further comprises a mutation in a pigment-associated gene, a mutation in a mycotoxin-associated gene, or both. In embodiments, the mycotoxin- associated gene is selected from the group consisting of bea1, Fum1, Fum6, Fum8, and combinations thereof. In embodiments, the pigment-associated gene is selected from the group consisting of bik1, bik2, bik3, bik4, bik5, bik6, and combinations thereof. In embodiments, the pigment-associated gene is selected from the group consisting of rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof. In embodiments, the filamentous fungus is selected from the group consisting of Rhizopus oligosporus, Ustilago esculenta, Hericulum erinaceus, Polyporous squamosus, Grifola fondosa, Hypsizygus marmoreus, Hypsizygus ulmarius, Calocybe gambosa, Pholiota nameko, Calvatia gigantea, Agaricus bisporus, Stropharia rugosoannulata, Hypholoma lateritium, Pleurotus eryngii, Pleurotus ostreatus, Pleurotus ostreatus var. columbinus, Tuber borchii, Morchella esculenta, Morchella conica, Morchella importuna, Sparassis crispa, Fusarium venenatum, Fusarium venenatum A3 / 5, Fusarium strain flavolapis (ATCC Accession Deposit No. PTA-10698), Disciotis venosa, Clonostachys rosea, Cordyceps militaris, Trametes versicolor, Ganoderma lucidum, Flammulina velutipes, Lentinula edodes, Pleurotus djamor, Pleurotus ostreatus, and Leucoagaricus spp. In embodiments, the filamentous fungus is Fusarium strain flavolapis (ATCC Accession Deposit No. PTA-10698). This third aspect also provides a method of making a mutant filamentous fungal strain, comprising exposing the fungal strain to a physical mutagen or a chemical mutagen, and / or performing site-directed mutagenesis on the fungal strain; wherein the exposing or the performing introduces at least one reduction of function mutation into at least one ethanol-associated gene. In embodiments, the mutation comprises at least one loss of function mutation. In embodiments, the mutation is selected from the group consisting of one or more knockout mutations, one or more introduced premature stop codons, one or more introduced point mutations, and combinations thereof. In embodiments, each point mutation independently produces a frameshift mutation, a nonsense mutation, or a missense mutation. In embodiments, the physical mutagen is selected from gamma rays, X rays, UV light, fast neutrons, thermal neutrons, beta particles, alpha particles, and combinations thereof. In embodiments, the chemical mutagen is selected from ethyl methyl sulfate, nitrogen mustards, mitomycin, methyl methane sulfonate, diethyl sulfate, nitrosoguanidine, ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, acridine orange, ethidium bromide, proflavin, daunorubicin, and combinations thereof. In some embodiments, the chemical mutagen is selected from ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, and combinations thereof. In embodiments, the site- directed mutagenesis is selected from oligonucleotide-directed mutagenesis, Kunkel’s method, cassette mutagenesis, PCR mutagenesis, homologous recombination, CRISPR / Cas9 mutagenesis, Delitto Perfetto, transplacement "pop-in pop-out," direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker, direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker using long homologous regions, in vivo site-directed mutagenesis with synthetic oligonucleotides, and combinations thereof. In embodiments, the method further comprises confirming the presence of the reduction of function mutation in the gene. In embodiments, the method further comprises exposing the strain to adaptive laboratory evolution to develop a characteristic in the strain selected from a higher growth rate, greater cell density, diminished pigment production, and combinations thereof. In embodiments, the adaptive laboratory evolution occurs by serially diluting the mutant strain under selective pressure. This third aspect also provides a mutant strain of Fusarium flavolapis having one or more reduction of function mutations introduced into its rco-3 gene, or having its rco-3 gene deleted. In embodiments, the mutant strain exhibits increased growth when grown using glucose as a carbon source as compared to a filamentous fungal strain of the same species without the mutations or deletion. In embodiments, the mutant strain is incapable of producing ethanol. In embodiments, the mutant strain produces less ethanol than a Fusarium flavolapis strain without the mutations or deletion. In embodiments, the mutant strain exhibits increased growth and reduced ethanol production when grown using glucose as a carbon source as compared to a filamentous fungal strain of the same species without the mutations or deletion. In embodiments, the rco-3 gene sequence is at least about 90% identical to SEQ ID NO:11. In embodiments, the mutant strain produces a RCO3 protein that is at least 90% identical to SEQ ID NO: 14. In a fourth aspect, the present disclosure provides a mycelial biomass and / or a cohesive mycelial biomass comprising any filamentous fungal strain provided herein. The present disclosure also provides a mycelial biomass and / or a cohesive mycelial biomass made by any of the methods provided herein. The present disclosure also provides a food product comprising a mycelial biomass provided herein, wherein the food product is selected from human food, animal feed, aquaculture feed, and pet food. In embodiments, the mycelial biomass is formulated as a liquid dispersion, a mycelial flour, or particles for the food product. In embodiments, the biomass is formulated as a liquid dispersion and the food product is a dairy analog. In embodiments, the dairy analog is selected from: hard cheese analogs, semi-hard cheese analogs, semi-soft cheese analogs, soft or soft ripened cheese analogs, cream cheese analogs, sour milk cheese analogs, blue cheese analogs, mascarpone cheese analogs, pasta filata analogs, brined cheese analogs, whey cheese analogs, fresh cheese analogs, butter analogs, whey analogs, cream analogs, sour milk analogs, yogurt analogs, milk analogs, powdered dairy analogs, ice cream analogs, and combinations thereof. In embodiments, the biomass is formulated as a mycelial flour and the food product is one or more baked goods; or the biomass is formulated as a mycelial flour and the food product is fried to create a noodle analog food product. In embodiments, the biomass is formulated as particles and the food product is selected from a meat analog, a tofu analog, and textured vegetable protein analog. The present disclosure also provides a textile product comprising any mycelial biomass provided by the present disclosure. In embodiments, the textile product comprises a fungal durable sheet material. In embodiments, the sheet material is selected from textiles, fabrics and leather analogs. DESCRIPTION OF DRAWINGS Figure 1 shows colonies of strains TR1, AL1, and F. flavolapis grown on glycerol or YPD plates at 72 hours according to Example 4. Figure 2 shows colonies of strains TR1, AL1, and F. flavolapis grown on glycerol or YPD plates at 96 hours according to Example 4. Figure 3 shows growth curves for strains TR1, AL1, and F. flavolapis grown without or with yeast extract at time points of 24, 48, 72, and 96 hours (left column to right column for each strain and condition) according to Example 6. Figure 4 shows cohesive mycelial biomasses produced by strains AL1, TR4, and F. flavolapis and their yield according to Example 7. Figure 5 shows cohesive mycelial biomasses produced by strains AL1 and F. flavolapis and their yield according to Example 8. Figure 6 shows colonies of strains AL1, TR4, and F. flavolapis grown on glycerol plates at 25, 27, or 30 degrees C according to Example 10. Figure 7A shows colonies of strains TR4, TR5, and F. flavolapis. Figure 7B shows cohesive mycelial biomasses of strains TR4, TR5, and F. flavolapis. Figure 7C shows measurements of cohesive mycelial biomass yields of colonies of strains TR4, TR5, and F. flavolapis. See Example 10. Figure 8 shows the coding sequence of the F. flavolapis bea1 gene, and its corresponding amino acid sequence, indicating the location of all possible premature stop codons identified by the instant inventors. Figure 9A shows colonies grown on glucose plates after UV exposure. Figure 9B shows selected (marked with arrows) single colonies of RD6 / UV1, UV2, and RD7 / UV3 during a second round of purification. Figure 9C shows colonies from a third round of purification. Figure 10 shows a schematic depicting the DNA amplicon for rco3KO. Figure 11A shows growth of rco3KO, RD6 and TR5 strains. Figure 11B show measured colony size following growth of rco3KO, RD6 and TR5 strains. Figure 12A shows recalculated yields from petri dish fermentation. Figure 12B shows biomats grown in glass trays. Figure 12C shows yields determined from the biomats shown in Figure 12B. Figure 13A shows yields determined after high glucose batch surface fermentation. Figure 13B shows protein content determined after high glucose batch surface fermentation. Figure 13C shows glucose conversion to biomass efficiency determined after high glucose batch surface fermentation. Figure 13D shows yields plotted against glucose conversion efficiency, both determined after high glucose batch surface fermentation. Figure 14A shows RD6 yields determined after growth in blue trays. Figure 14B shows RD6 yield rates determined after growth in blue trays. Figure 15A shows compositions of RD6 determined after growth at different glucose concentrations. Figure 15B shows compositions of RD6, including calculated carbohydrates, determined after growth at different glucose concentrations. Figure 16A shows an experimental design for rco3KO small-scale surface fermentation. Figure 16B shows yields determined after performing the experiment described in Figure 16A. Figure 16C shows biomats produced after performing the experiment described in Figure 16A. Figure 17A depicts measured cell density from seed fermenter routine sampling. Figure 17B depicts changes in seed fermentation broth metabolites over time. Figure 17C depicts measured cell density from production fermenter routine sampling. Figure 17D depicts changes in production fermenter broth metabolites over time from routine sampling. Figure 18 shows a schematic of the bik1KO gBlock (deletion cassette) design. Figure 19 shows cultures of TR5 and putative bik1KO transformants bik1KO#1, bik1KO#2, bik1KO#3, bik1KO#5, and bik1KO#10 in a nitrogen-limited medium. DETAILED DESCRIPTION Disclosed herein are filamentous fungal strains comprising one or more mutations of one or more genes responsible, in whole or in part, for the production of at least one mycotoxin (i.e., mycotoxin-associated genes). In various aspects, such mutations alter or eliminate the function of such genes, thereby reducing or, in some embodiments, completely eliminating the production of the mycotoxin by such strains. In a first aspect, the present disclosure provides methods of introducing one or more premature stop codons into at least one mycotoxin-associated gene, as well as filamentous fungal strains produced by such methods which, in some embodiments, are edible. A stop codon signals the termination of translation of a polypeptide or protein. During the process of producing a polypeptide or protein from a gene, most codons in the genetic code correspond to the addition of an amino acid to a growing polypeptide chain; stop codons signal the termination of this process by binding release factors, which cause the ribosomal subunits to disassociate, releasing the polypeptide chain. While start codons need nearby sequences or initiation factors to start translation, a stop codon alone is sufficient to terminate translation. The general concept of this first aspect, then, is to introduce one or more premature stop codons into a mycotoxin-associated gene in a filamentous fungus. The premature stop codon(s) become part of a translation termination signal in the gene and is / are thus used to terminate translation of the gene’s product prematurely, leading to a truncated and / or incomplete protein that demonstrates altered (reduced or enhanced, as may be appropriate) functionality, or a nonfunctional protein. The result is: a reduction in, or elimination of, production of the mycotoxin by the fungi; production of a modified mycotoxin demonstrating reduced, or eliminated, functionality; or both. As will be appreciated, more than one premature stop codon may be introduced into a single mycotoxin-associated gene, and premature stop codons may be inserted into two or more mycotoxin-associated genes. In a second aspect, the present disclosure provides methods of introducing one or more point mutations into at least one mycotoxin-associated gene, such that each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene, as well as filamentous fungal strains produced by such methods which, in some embodiments, are edible. A frameshift mutation occurs when an introduced point mutation causes a shift in the reading frame of the codons in the gene, leading to alteration of the sequence of amino acids during protein translation. A nonsense mutation occurs when an introduced point mutation produces a nonsense codon (which does not code for any amino acid) leading to a truncated protein product. A missense mutation occurs when an introduced point mutation results in a codon that specifies a different amino acid and thus causes the synthesis of a protein with an altered amino acid sequence during translation. The general concept of this second aspect, then, is to introduce one or more point mutations into a mycotoxin-associated gene in a filamentous fungi. The point mutations each independently alter the gene sequence in a manner that leads to a truncated and / or incomplete protein that demonstrates altered (reduced or enhanced, as may be appropriate) functionality, or a nonfunctional protein, without the introduction of any premature stop codons into the gene sequence. The result is: a reduction in, or elimination of, production of the mycotoxin by the fungi; production of a modified mycotoxin demonstrating reduced, or eliminated, functionality; or both. As will be appreciated, more than one point mutation may be introduced into a single mycotoxin-associated gene, each of which may independently result in the same or different types of mutations; for example, the introduction of two point mutations into a single gene may result in both a frameshift mutation and a nonsense mutation within that gene. Additionally, point mutations may be inserted into two or more mycotoxin-associated genes. In a third aspect, the present disclosure provides methods of introducing one or more premature stop codons and one or more point mutations into at least one mycotoxin- associated gene, such that each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene, as well as filamentous fungal strains produced by such methods which, in some embodiments, are edible. The general concept of this third aspect, then, is to introduce one or more premature stop codons and one or more point mutations into a mycotoxin-associated gene in a filamentous fungi. As above, the premature stop codon(s) become part of a translation termination signal in the gene and is / are thus used to terminate translation of the gene’s product prematurely, leading to a truncated and / or incomplete protein that demonstrates altered (reduced or enhanced, as may be appropriate) functionality, or a nonfunctional protein. Additionally, the point mutations each independently alter the gene sequence in a manner that leads to a truncated and / or incomplete protein that demonstrates altered (reduced or enhanced, as may be appropriate) functionality, or a nonfunctional protein, without the introduction of any premature stop codons into the gene sequence. The result is: a reduction in, or elimination of, production of the mycotoxin by the fungi; production of a modified mycotoxin demonstrating reduced, or eliminated, functionality; or both. As will be appreciated, more than one premature stop codon and more than one point mutation may be introduced into a single mycotoxin-associated gene, each of which may independently result in the same or different types of mutations. Additionally, premature stop codons and point mutations may be inserted into two or more mycotoxin-associated genes. In each of the above aspects, the mutations described above do not necessarily have to be the result of site-directed mutagenesis or homologous recombination. In some embodiments, the mutations described above do not result from site-directed mutagenesis or homologous recombination, although the strains may have genetic modifications of this type in other parts of their genome provided that they comprise one or more genetic modifications by introduction of one or more premature stop codons, the introduction of one or more point mutations, or both, as described herein. Filamentous fungal strains produced according to the present disclosure produce reduced levels of mycotoxins, produce mycotoxins demonstrating reduced or eliminated functionality, or both, as compared to unmodified strains of the same species, and are suitable for human and / or animal use without further processing to lower mycotoxin levels. Such strains also produce reduced mycotoxin levels, produce mycotoxins demonstrating reduced or eliminated functionality, or both, when cultured under conditions that would otherwise cause mycotoxin production in unmodified strains of the same species. By eliminating or minimizing the steps typically required to reduce or eliminate the impact of mycotoxins from fungal strains, filamentous fungal strains produced according to the present disclosure provide valuable processing and economic advantages. Also disclosed herein are filamentous fungal strains comprising one or more mutations of one or more genes responsible, in whole or in part, for the production of ethanol (i.e., ethanol-associated genes). In various aspects, such mutations alter or eliminate the function of such genes, thereby reducing or, in some embodiments, completely eliminating the production of ethanol by such strains. In a fourth aspect, the present disclosure provides methods of introducing one or more null mutations into, or knocking out, at least one ethanol-associated gene, as well as filamentous fungal strains produced by such methods which, in some embodiments, are edible. A null mutation is a genetic mutation that prevents a gene from being transcribed into RNA or translated into a functional protein product. This results in a nonfunctional gene product or no gene product at all. Examples of null mutations include mutations in coding sequences and mutations in regulatory or other non-coding sequences such as promoter, operator, and Shine-Dalgarno sequences. A knockout mutation, or a gene knockout, is a genetic engineering technique that permanently inactivates a gene in an organism by removing the gene of interest entirely, or otherwise inactivating the gene. The general concept of this fourth aspect, then, is to introduce one or more null mutations into, or to completely knockout, an ethanol-associated gene in a filamentous fungus. The null mutation(s) become part of the gene and is / are thus used to prevent translation of the gene entirely, or lead to the production of a truncated and / or incomplete protein that demonstrates altered (reduced or enhanced, as may be appropriate) functionality, or a nonfunctional protein. The gene knockout completely and permanently eliminates the production of anything from the gene, eliminating protein production. The result is: reduction or elimination of ethanol production, reduction or elimination of ethanol production in the presence of glucose, reduction or elimination of production of glucose-6- phosphate, reduction of the rate of glucose uptake, increased production of pyruvate, or combinations thereof. As will be appreciated, more than one mutation may be introduced into a single ethanol-associated gene, and mutations may be inserted into two or more ethanol-associated genes. In a fifth aspect, the present disclosure provides methods of introducing one or more point mutations into at least one ethanol-associated gene, such that each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene, as well as filamentous fungal strains produced by such methods which, in some embodiments, are edible. The general concept of this fifth aspect, then, is to introduce one or more point mutations into an ethanol-associated gene in a filamentous fungi. The result is: reduction or elimination of ethanol production, reduction or elimination of ethanol production in the presence of glucose, reduction or elimination of production of glucose-6-phosphate, reduction of the rate of glucose uptake, increased production of pyruvate, or combinations thereof. As will be appreciated, more than one point mutation may be introduced into a single ethanol-associated gene, each of which may independently result in the same or different types of mutations; for example, the introduction of two point mutations into a single gene may result in both a frameshift mutation and a nonsense mutation within that gene. Additionally, point mutations may be inserted into two or more ethanol-associated genes. In a sixth aspect, the present disclosure provides methods of introducing one or more premature stop codons and one or more point mutations into at least one ethanol-associated gene, such that each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene, as well as filamentous fungal strains produced by such methods which, in some embodiments, are edible. The general concept of this sixth aspect, then, is to introduce one or more premature stop codons and one or more point mutations into an ethanol-associated gene in a filamentous fungi. As above, the premature stop codon(s) become part of a translation termination signal in the gene and is / are thus used to terminate translation of the gene’s product prematurely, leading to a truncated and / or incomplete protein that demonstrates altered (reduced or enhanced, as may be appropriate) functionality, or a nonfunctional protein. The result is: reduction or elimination of ethanol production, reduction or elimination of ethanol production in the presence of glucose, reduction or elimination of production of glucose-6-phosphate, reduction of the rate of glucose uptake, increased production of pyruvate, or combinations thereof. As will be appreciated, more than one premature stop codon and more than one point mutation may be introduced into a single ethanol-associated gene, each of which may independently result in the same or different types of mutations. Additionally, premature stop codons and point mutations may be inserted into two or more ethanol-associated genes. In each of the above aspects, the mutations described can be the result of site-directed mutagenesis or homologous recombination. In some embodiments, the mutations described above do not result from site-directed mutagenesis or homologous recombination. In some embodiments, the strains comprise one or more genetic modifications by introduction of one or more premature stop codons, the introduction of one or more point mutations, or both, as described herein. Filamentous fungal strains produced according to the present disclosure demonstrate reduced ethanol production, reduced ethanol production in the presence of glucose, reduced production of glucose-6-phopshate, reduced glucose uptake, increased production of pyruvate, or combinations thereof, as compared to unmodified strains of the same species. Such strains also demonstrate reduced ethanol production, reduced ethanol production in the presence of glucose, reduced production of glucose-6- phopshate, reduced glucose uptake, increased production of pyruvate, or combinations thereof, when cultured under conditions that would otherwise cause ethanol production in unmodified strains of the same species. By eliminating or minimizing the steps typically required to reduce or eliminate the impact of ethanol from fungal strains, filamentous fungal strains produced according to the present disclosure provide valuable processing and economic advantages. Finally, also disclosed herein are filamentous fungal strains comprising one or more mutations of one or more genes responsible, in whole or in part, for the production of at least one pigment (i.e., pigment-associated genes). In various aspects, such mutations alter or eliminate the function of such genes, thereby reducing or, in some embodiments, completely eliminating the production of the pigment by such strains. In a seventh aspect, the present disclosure provides methods of introducing one or more null mutations into, or knocking out, at least one bikaverin-associated gene, as well as filamentous fungal strains produced by such methods which, in some embodiments, are edible. The general concept of this seventh aspect, then, is to introduce one or more null mutations into, or to completely knock out, a bikaverin-associated gene in a filamentous fungus. The result is: a reduction in, or elimination of, production of bikaverin by the fungi; production of a modified bikaverin demonstrating reduced, or eliminated, functionality; or both. As will be appreciated, more than one mutation may be introduced into a single bikaverin-associated gene, and mutations may be inserted into two or more bikaverin- associated genes. In an eighth aspect, the present disclosure provides methods of introducing one or more point mutations into at least one bikaverin-associated gene, such that each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene, as well as filamentous fungal strains produced by such methods which, in some embodiments, are edible. The general concept of this eighth aspect, then, is to introduce one or more point mutations into a bikaverin-associated gene in a filamentous fungi. The result is: a reduction in, or elimination of, production of bikaverin by the fungi; production of a modified bikaverin demonstrating reduced, or eliminated, functionality; or both. As will be appreciated, more than one point mutation may be introduced into a single bikaverin- associated gene, each of which may independently result in the same or different types of mutations; for example, the introduction of two point mutations into a single gene may result in both a frameshift mutation and a nonsense mutation within that gene. Additionally, point mutations may be inserted into two or more bikaverin-associated genes. In a ninth aspect, the present disclosure provides methods of introducing one or more premature stop codons and one or more point mutations into at least one bikaverin- associated gene, such that each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene, as well as filamentous fungal strains produced by such methods which, in some embodiments, are edible. The general concept of this ninth aspect, then, is to introduce one or more premature stop codons and one or more point mutations into a bikaverin-associated gene in a filamentous fungi. The result is: a reduction in, or elimination of, production of the bikaverin by the fungi; production of a modified bikaverin demonstrating reduced, or eliminated, functionality; or both. As will be appreciated, more than one premature stop codon and more than one point mutation may be introduced into a single bikaverin-associated gene, each of which may independently result in the same or different types of mutations. Additionally, premature stop codons and point mutations may be inserted into two or more bikaverin- associated genes. In each of the above aspects, the mutations described above can be the result of site- directed mutagenesis or homologous recombination. In some embodiments, the mutations described above do not result from site-directed mutagenesis or homologous recombination. In some embodiments, the strains comprise one or more genetic modifications by introduction of one or more premature stop codons, the introduction of one or more point mutations, or both, as described herein. Filamentous fungal strains produced according to the present disclosure demonstrate reduced levels of bikaverin, produce bikaverin demonstrating reduced or eliminated functionality, or both, as compared to unmodified strains of the same species, and are suitable for human and / or animal use without further processing to lower bikaverin levels. Such strains also demonstrate reduced bikaverin levels, produce bikaverin demonstrating reduced or eliminated functionality, or both, when cultured under conditions that would otherwise cause bikaverin production in unmodified strains of the same species. By eliminating or minimizing the steps typically required to reduce or eliminate the impact of bikaverin from fungal strains, filamentous fungal strains produced according to the present disclosure provide valuable processing and economic advantages. Definitions As used herein, the following terms shall have the following meanings unless the context clearly requires otherwise: The terms “about,” “approximately,” etc., when used in relation to numerical limitations or ranges, mean that the recited limitation or range may vary by up to 10%. For example, “about 750” can mean as little as 675 or as much as 825, or any value therebetween. When used in relation to ratios or relationships between two or more numerical limitations or ranges, the terms “about,” “approximately,” etc. mean that each of the limitations or ranges may vary by up to 10%; for example, a statement that two quantities are “approximately equal” can mean that a ratio between the two quantities is as little as 0.9:1.1 or as much as 1.1:0.9 (or any value therebetween), and a statement that a four-way ratio is “about 5:3:1:1” can mean that the first number in the ratio can be any value of at least 4.5 and no more than 5.5, the second number in the ratio can be any value of at least 2.7 and no more than 3.3, and so on. A “bikaverin-associated gene” is a gene responsible, in whole or in part, for the production of bikaverin. Such a gene encodes a polypeptide (such as an enzyme) that is required in biosynthesis of bikaverin; alteration of the gene also alters or eliminates the expression and / or activity of the polypeptide. In some embodiments, a bikaverin-associated gene is wholly responsible for the biosynthesis of bikaverin, for example a gene encoding a polyketide synthase. In other embodiments, a bikaverin-associated gene is only partly responsible for the biosynthesis of bikaverin, for example bik1, which encodes a polyketide synthase involved in the biosynthesis of bikaverin. A “bikaverin-associated gene” includes the DNA sequence of such gene as well as any and all mRNA derived from that DNA sequence (if any). The term “biomass” refers to a mass of a living or formerly living organism, including fungal, microbial, and plant biomass. Microbial biomass sources can include bacterial, fungal (including higher fungi), and microalgal biomass sources. Plant biomass sources can include any source of plant-based biopolymers such as cellulose, lignin and pectin. By way of non-limiting example, the phrase “filamentous fungal biomass” as used herein refers to a mass of a living or formerly living filamentous fungus. The term “biomat” refers to a cohesive mass of filamentous fungal tissue comprising a network of interwoven hyphae filaments. Biomats may be produced by any one or more fungal fermentation methods, for example according to methods described in WO 2020 / 176758, WO 2019 / 099474, and / or WO 2018 / 014004. An “ethanol-associated gene” is a gene responsible, in whole or in part, for the production of ethanol. Such a gene encodes a polypeptide (such as an enzyme) that is required in ethanol production; alteration of the gene also alters or eliminates the expression and / or activity of the polypeptide. In some embodiments, an ethanol-associated gene is wholly responsible for the production of ethanol, for example a gene encoding a glucose- associated gene. In other embodiments, an ethanol-associated gene is only partly responsible for the production of ethanol, for example rco-3, which encodes a glucose sensor involved in the production of ethanol. An “ethanol-associated gene” includes the DNA sequence of such gene as well as any and all mRNA derived from that DNA sequence (if any). The terms “genetic mutation,” “mutation,” and / or “genetic alteration” refer to any change in a naturally occurring (wild type) nucleotide sequence of a gene that creates a permanent change to that gene's DNA sequence. The change may be in the coding sequence of the gene, in the 5’ or 3’ untranslated regions, the promoter, the terminator, any enhancer, any other regulatory element of the gene, or combinations of any of the foregoing. Such changes include deletions, insertions, and / or substitutions of one or more nucleotides in the wildtype sequence. The change in the DNA sequence may cause a disruption of the gene such that, during transcription and / or translation, the amount of polypeptide / protein encoded by the gene is reduced, or the polypeptide / protein encoded by the gene is materially altered in sequence, structure, function, or combinations thereof. A “glucose transport-associated gene” is a gene responsible, in whole or in part, for the sensing and / or transport of glucose. Such a gene encodes a polypeptide (such as an enzyme) that is required in sensing and / or transport of glucose; alteration of the gene also alters or eliminates the expression and / or activity of the polypeptide. In some embodiments, a glucose transport-associated gene is wholly responsible for the sensing and / or transport of glucose, for example a gene encoding a glucose sensor. In other embodiments, a glucose transport-associated gene is only partly responsible for the sensing and / or transport of glucose, for example rco-3, which encodes a glucose sensor involved in the sensing and / or transport of glucose and the production of ethanol. A “glucose transport-associated gene” includes the DNA sequence of such gene as well as any and all mRNA derived from that DNA sequence (if any). The phrase “mycelial biomass” refers to a biomass of filamentous fungus in which fungal mycelium makes up about 50 wt% - about 100 wt% of the biomass. In embodiments, fungal mycelium makes up at least about 50 wt%, at least about 55 wt%, at least about 60 wt%, at least about 65 wt%, at least about 70 wt%, at least about 75 wt%, at least about 80 wt%, at least about 85 wt%, at least about 90 wt%, at least about 95 wt%, at least about 96 wt%, at least about 97 wt%, at least about 98 wt%, at least about 99 wt%, or substantially all of the biomass. The remainder (i.e., the non-mycelial portion) of the mycelial biomass may contain other fungal tissues (conidia, fruiting bodies, etc.). “Mycelial biomass” specifically includes biomass produced by any fermentation method and thus encompasses biomass produced by submerged fermentation methods and non-submerged fermentation methods. In some embodiments, a mycelial biomass is produced by any one or more submerged fermentation methods known in the art, such as, for example, those described in U.S. Patent 7,635,492 to Finnigan et al.. In other embodiments, a mycelial biomass is a “cohesive mycelial biomass” produced by a fermentation process other than a submerged fermentation process. A “cohesive mycelial biomass” has sufficient tensile strength and structural integrity to be picked up and moved by hand without disintegrating or tearing and is produced by any one or more fungal fermentation methods in which the filamentous fungus grows in such a way as to form a mass of interwoven mycelia, e.g., methods in which a fungal mycelium is grown in air or a controlled atmosphere out of a growth medium or feedstock (e.g., liquid surface fermentation, fermentation on the surface of a membrane or mesh scaffold, solid substrate fermentations in which mycelial biomass grows free of solid substrate, etc.). Examples of methods of producing a “cohesive mycelial biomass” are described in PCT Application Publications 2020 / 176758, 2019 / 099474, and 2018 / 014004. Generally speaking, mycelial biomasses recovered from submerged fermentation processes are paste-like substances with poor tensile strength and structural integrity and thus are not cohesive mycelial biomasses. A “mycotoxin-associated gene” is a gene responsible, in whole or in part, for the production of at least one mycotoxin. Such a gene encodes a polypeptide (such as an enzyme) that is required in mycotoxin biosynthesis; alteration of the gene also alters or eliminates the expression and / or activity of the polypeptide. In some embodiments, a mycotoxin-associated gene is wholly responsible for the production of a mycotoxin, for example a gene encoding a beauvericin synthase. In other embodiments, a mycotoxin- associated gene is only partly responsible for the production of a mycotoxin, for example Fum1, which encodes a polyketide synthase involved in the biosynthesis of fumonisins. A “mycotoxin-associated gene” includes the DNA sequence of such gene as well as any and all mRNA derived from that DNA sequence (if any). A “pigment-associated gene” is a gene responsible, in whole or in part, for the production of a pigment. Such a gene encodes a polypeptide (such as an enzyme) that is required in pigment production; alteration of the gene also alters or eliminates the expression and / or activity of the polypeptide. In some embodiments, a pigment-associated gene is wholly responsible for the production of a pigment, for example a gene encoding a bikaverin-associated gene. In other embodiments, a pigment-associated gene is only partly responsible for the production of a pigment, for example bik1, which encodes a polyketide synthase involved in the production of bikaverin. A “pigment-associated gene” includes the DNA sequence of such gene as well as any and all mRNA derived from that DNA sequence (if any). The term “whiteness index” is based on measurement of uniform color spaces on the CIE 1976 L*a*b* scale for any illuminant as recommended by the Commission Internationale de l'Eclairage (CIE). The CIE L*a*b* scale is a simplified cube root version of the Adams-Nickerson space produced by the quantities of CIE L*a*b* in rectangular coordinates. The relationship of the CIE L*a*b* scale and the CIE XYZ scale for any illuminant is described in the ASTM E 308 Standard Practice for Computing the Colors of Objects by Using the CIE System (ASTM International, West Conshohocken, PA, USA). Using this standard, the measurement of the quantities of CIE L*a*b* using a colorimeter can be used to determine the Whiteness Index of a substance in relationship with physical observation. According to this standard, a Whiteness Index of >7.5 calculated from the formula (L* / b*)−a* means that a sample looks white (wherein L*−=dark, L*+=white; b*−=blue, b*+=yellow, a*−=green, and a*+=red). The theoretical “perfect white” has reference values of 100% across the visible spectrum with corresponding colorimetric values of L*=100.00, a*=0.00 and b*=0.00. An item that is only near white may be darker, having a lower L* value, and possibly be slightly chromatic either in the red-green dimension (a*) or in the yellow-blue dimension (b*). Mycotoxin-Associated Genes In various aspects, the present disclosure provides filamentous fungal strains comprising one or more mutated mycotoxin-associated genes. In some embodiments, such strains are edible and suitable for the production of food products. Such strains either produce reduced levels of mycotoxin, or have had their ability to produce a mycotoxin completely eliminated, as a result of the mutated gene(s). In some embodiments, the mycotoxin-associated gene is any gene that encodes a polypeptide useful in the production of a mycotoxin. In some embodiments, the mycotoxin- associated gene is any one or more genes that encode a polypeptide useful in the production of a mycotoxin selected from: aflatoxins, beauvericin, fusarins, citrinin, ochratoxins, trichothecenes, zearalenone, fumonisins, mycophenolic acid, penicillic acid, patulin, cyclopiazonic acid, ergot alkaloids, cyclopiazonic acid, gliotoxin, sterigmatocystin, and combinations thereof. In some embodiments, the mycotoxin-associated gene is any gene that encodes a polypeptide useful in the production of an aflatoxin selected from: aflatoxin B1, aflatoxin B2, aflatoxin G1, aflatoxin G2, aflatoxin M1, aflatoxin M2, aflatoxicol, aflatoxin Q1, and combinations thereof. In some embodiments, the mycotoxin-associated gene is any gene that encodes a polypeptide useful in the production of a fusarin selected from: fusaric acid, fusarin A, fusarin C, fusarin D, and combinations thereof. In some embodiments, the mycotoxin-associated gene is any gene that encodes a polypeptide useful in the production of an ochratoxin selected from: ochratoxin A, ochratoxin B, ochratoxin C, ochratoxin TA, and combinations thereof. In some embodiments, the mycotoxin-associated gene is any gene that encodes a polypeptide useful in the production of a trichothecene selected from: deoxynivalenol^(DON^or^vomitoxin), nivalenol, T-2 / HT-2 toxins, diacetoxyscirpenol (DAS), and combinations thereof. In some embodiments, the mycotoxin-associated gene is any gene that encodes a polypeptide useful in the production of zearalenone, alpha-zearalenol,^beta-zearalenol, and / or combinations thereof. In some embodiments, the mycotoxin-associated gene is any gene that encodes a polypeptide useful in the production of a fumonisin selected from: fumonisin B1, fumonisin B2, fumonisin B3, fumonisin B4, and combinations thereof. In some embodiments, the mycotoxin-associated gene is any gene that encodes a polypeptide useful in the production of an ergot alkaloid selected from: methylergometrine, ergotamine ergotoxine, and combinations thereof. Fumonisin-Associated Genes As noted above, in some embodiments the mycotoxin-associated gene is any gene that encodes a polypeptide useful in the production of a fumonisin selected from: fumonisin B1, fumonisin B2, fumonisin B3, fumonisin B4, and combinations thereof. As set forth herein, alteration of these genes can occur via a knockout mutation, one or more null mutations, the introduction of one or more premature stop codons into the gene(s), the introduction of one or more point mutations into the gene(s), and / or the introduction of a mutation by any other means described herein. In some embodiments, the mycotoxin-associated gene is a gene encoding a fumonisin synthase, for example Fum1, which encodes a polyketide synthase involved in the biosynthesis of fumonisins. The Fum1 gene has been isolated from several fungal strains and their sequences determined. For example, the nucleotide sequence of Fum1 (also called Fum5, fumonisin PKS) isolated from Fusarium fujikuroi is available as NCBI Genbank accession no. IMI58289: HF679031. The fumonisin biosynthetic gene cluster involved in the fumonisin biosynthesis pathway was previously identified from the filamentous fungal strain Fusarium verticillioides. See e.g. Huffman et al., 2010; Visentin et al., 2011; Medina et al.; 2013, Rocha et al., 2015. These genes have been isolated from several fungal strains and their sequences determined. The fumonisin biosynthetic gene cluster comprises 16 or 17 transcriptionally coregulated genes, which include genes designated as Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20 and Fum21. Fum1 was later found to be the same as Fum5. Fum2 and Fum3 were later found to be the same as Fum12 and Fum9, respectively (Visentin et al. (2011)). Studies have demonstrated that these genes are involved in fumonisin production. Although analytical testing has indicated that a negligible amount of fumonisin was produced by F. flavolapis, analysis of its DNA sequence revealed that the F. flavolapis genome possesses a complete set of 16 genes for fumonisin biosynthesis, as in Fusarium fujikuroi. The gene Fum1 encodes a polyketide synthase, which plays a key role in the biosynthesis, as it catalyzes the synthesis of a linear polyketide that forms the backbone structure of fumonisins. Fum8 encodes an alpha-aminotransferase, which is involved in adding amine groups to the backbone. The remaining genes encode proteins that take part in further processing of the backbone. Fum13 encodes a C-3 carbonyl reductase. Fum2, Fum3, Fum6 and Fum15 encode cytochrome P450 oxygenases that catalyze oxygenation. Fum7, Fum10, Fum11, Fum14 and Fum16 are required for tricarballylic acid esterification. Fum17 and Fum18 are longevity assurance factors; and Fum19 encodes a protein highly similar to ABC multidrug transporters, which can possibly reduce cellular concentration of toxins. These have been suggested as being involved in fumonisin self-protection and sphingolipid metabolism. In some embodiments, the mycotoxin-associated gene is selected from Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof. In some embodiments, the mycotoxin-associated gene is Fum1. In some embodiments, the mycotoxin-associated gene is Fum6. In some embodiments, the mycotoxin-associated gene is Fum8. In some embodiments, the present disclosure provides a filamentous fungal strain comprising one or more mutations in a gene selected from: Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof. In some embodiments, the mutations comprise a knockout mutation, one or more null mutations, the introduction of one or more premature stop codons into the gene(s), the introduction of one or more point mutations into the gene(s), and / or the introduction of a mutation by any other means described herein. In that regard, in some embodiments the present disclosure provides a filamentous fungal strain comprising a gene selected from: Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof, wherein the gene comprises one or more of these mutations within its sequence. In other embodiments, the present disclosure provides a filamentous fungal strain comprising a Fum1 gene having one or more of these mutations within its sequence. In other embodiments, the present disclosure provides a filamentous fungal strain comprising a Fum6 gene having one or more of these mutations within its sequence. In still other embodiments, the present disclosure provides a filamentous fungal strain comprising a Fum8 gene having one or more of these mutations within its sequence. In some embodiments, the mutations comprise the introduction of one or more point mutations into the gene(s), each of which independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). In that regard, in some embodiments the present disclosure provides a filamentous fungal strain comprising a gene selected from: Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof, wherein the gene comprises one or more point mutations within its sequence. In other embodiments, the present disclosure provides a filamentous fungal strain comprising a Fum1 gene having one or more point mutations within its sequence. In other embodiments, the present disclosure provides a filamentous fungal strain comprising a Fum6 gene having one or more point mutations within its sequence. In still other embodiments, the present disclosure provides a filamentous fungal strain comprising a Fum8 gene having one or more point mutations within its sequence. In each of the foregoing embodiments, each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). In some embodiments, the mutations comprise the introduction of one or more premature stop codons and one or more point mutations into the gene(s). In that regard, in some embodiments the present disclosure provides a filamentous fungal strain comprising a gene selected from: Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof, wherein the gene comprises one or more premature stop codons and one or more point mutations within its sequence. In other embodiments, the present disclosure provides a filamentous fungal strain comprising a Fum1 gene having one or more premature stop codons and one or more point mutations within its sequence. In other embodiments, the present disclosure provides a filamentous fungal strain comprising a Fum6 gene having one or more premature stop codons and one or more point mutations within its sequence. In still other embodiments, the present disclosure provides a filamentous fungal strain comprising a Fum8 gene having one or more premature stop codons and one or more point mutations within its sequence. In each of the foregoing embodiments, each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). In some embodiments, the present disclosure provides a filamentous fungal strain comprising one or more mutations in a gene selected from Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof, wherein the strain produces less fumonisin than a strain of the same filamentous fungi that does not comprise the mutation(s). Such strains also produce reduced fumonisin levels, produce a modified fumonisin demonstrating reduced or eliminated functionality; or both, when cultured under conditions that would otherwise cause fumonisin production in unmodified strains of the same species. In other embodiments, the gene is Fum1, Fum6, or Fum8. In some embodiments, the present disclosure provides a filamentous fungal strain comprising one or more mutations in a gene selected from Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof, wherein the strain is incapable of producing fumonisin. In other embodiments, the gene is Fum1, Fum6, or Fum8. In some embodiments, the present disclosure provides a mycelial biomass, made from a filamentous fungal strain comprising one or more mutations in a gene selected from: Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof. In some embodiments, the mutations comprise a knockout mutation, one or more null mutations, the introduction of one or more premature stop codons into the gene(s), the introduction of one or more point mutations into the gene(s), and / or the introduction of a mutation by any other means described herein. In that regard, in some embodiments the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising a gene selected from: Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof, wherein the gene comprises one or more of these mutations within its sequence. In other embodiments, the gene is Fum1, Fum6, or Fum8. In some embodiments, the mutations comprise the introduction of one or more point mutations into the gene(s), each of which independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). In that regard, in some embodiments the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising a gene selected from: Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof, wherein the gene comprises one or more point mutations within its sequence. In other embodiments, the gene is Fum1, Fum6, or Fum8. In each of the foregoing embodiments, each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). In some embodiments, the mutations comprise the introduction of one or more premature stop codons and one or more point mutations into the gene(s). In that regard, in some embodiments the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising a gene selected from: Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof, wherein the gene comprises one or more premature stop codons and one or more point mutations within its sequence. In other embodiments, the gene is Fum1, Fum6, or Fum8. In each of the foregoing embodiments, each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). In some embodiments, the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising one or more mutations in a gene selected from Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof, wherein the strain produces less fumonisin than a strain of the same filamentous fungi that does not comprise the mutation(s), even when cultured under conditions that would otherwise cause fumonisin production in unmodified strains of the same species. In other embodiments, the gene is Fum1, Fum6, or Fum8. In some embodiments, the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising one or more mutations in a gene selected from Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof, wherein the strain is incapable of producing fumonisin. In other embodiments, the gene is Fum1, Fum6, or Fum8. In some embodiments, the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising one or more genetic mutations such that the strain produces less fumonisin, produces a modified fumonisin demonstrating reduced or eliminated functionality, or both, as compared to a strain of the same filamentous fungi that does not comprise the mutation(s), even when cultured under conditions that would otherwise cause fumonisin production in unmodified strains of the same species. In some embodiments, the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising one or more genetic mutations and is incapable of producing fumonisin. In these embodiments, the genetic mutations are in one or more genes selected from Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof. In other embodiments, the genetic mutations are in the Fum1, Fum6, or Fum8 genes. Beauvericin-Associated Genes As noted above, in some embodiments the mycotoxin-associated gene is any gene that encodes for a polypeptide useful in the production of beauvericin. As set forth herein, alteration of these genes can occur via any one or more of the methods of genetic mutation disclosed herein. In some embodiments, the mycotoxin-associated gene is a gene encoding a beauvericin synthase. Biosynthesis of beauvericin is governed by beauvericin synthase, a non-ribosomal peptide synthase that appears to present considerable divergence among different fungal species (Urbaniak M, et al., J Fungi (Basel). 2020 Nov 15;6(4):288. doi: 10.3390 / jof6040288. PMID: 33203083; PMCID: PMC7712144.). The first description of a beauvericin synthase, having a molecular mass of approximately 250 kDa, was by Peeters et al. (J. Antibiot. 1988;41:352–359. doi: 10.7164 / antibiotics.41.352.) in Beauveria bassiana. The beauvericin gene cluster (also from B. bassiana), including a 9570 bp gene encoding a putative cyclooligomer depsipeptide synthase was reported by Xu et al. (Chem. Biol. 2008;15:898–907. doi: 10.1016 / j.chembiol.2008.07.011). A Fusarium beauvericin synthase gene of 9413 bp was cloned and characterized for the first time by Zhang et al. (Sci. China Life Sci. 2013;56:628–637. doi: 10.1007 / s11427-013-4505-1) Fusarium proliferatum. The beauvericin synthase gene has thus been isolated from more than one fungal strain and the sequences of each gene have been determined. In some embodiments, the present disclosure provides a filamentous fungal strain comprising one or more mutations in a beauvericin synthase gene. In some embodiments, the mutations comprise a knockout mutation, one or more null mutations, the introduction of one or more premature stop codons into the gene(s), the introduction of one or more point mutations into the gene(s), and / or the introduction of a mutation by any other means described herein. In that regard, in some embodiments the present disclosure provides a filamentous fungal strain comprising a beauvericin synthase gene having one or more of these mutations within its sequence. In some embodiments, the mutations comprise the introduction of one or more point mutations into the beauvericin synthase gene, each of which independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene. In that regard, in some embodiments the present disclosure provides a filamentous fungal strain comprising a beauvericin synthase gene having one or more point mutations within its sequence. In this embodiment, each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene. In some embodiments, the mutations comprise the introduction of one or more premature stop codons and one or more point mutations into the beauvericin synthase gene. In that regard, in some embodiments the present disclosure provides a filamentous fungal strain comprising a beauvericin synthase gene having one or more premature stop codons and one or more point mutations within its sequence. In this embodiment, each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene. In some embodiments, the present disclosure provides a filamentous fungal strain comprising one or more mutations in a beauvericin synthase gene, wherein the strain produces less beauvericin, produces a modified beauvericin demonstrating reduced or eliminated functionality, or both, as compared to a strain of the same filamentous fungi that does not comprise the mutation(s). Such strains also do so when cultured under conditions that would otherwise cause beauvericin production in unmodified strains of the same species. In some embodiments, the present disclosure provides a filamentous fungal strain comprising one or more mutations in a beauvericin synthase gene, wherein the strain is incapable of producing beauvericin. In some embodiments, the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising one or more mutations in a beauvericin synthase gene. In some embodiments, the mutations comprise a knockout mutation, one or more null mutations, the introduction of one or more premature stop codons into the gene(s), the introduction of one or more point mutations into the gene(s), and / or the introduction of a mutation by any other means described herein. In that regard, in some embodiments the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising a beauvericin synthase gene having one or more such mutations within its sequence. In some embodiments, the mutations comprise the introduction of one or more point mutations into the beauvericin synthase gene, each of which independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene. In that regard, in some embodiments the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising a beauvericin synthase gene having one or more point mutations within its sequence. In this embodiment, each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene. In some embodiments, the mutations comprise the introduction of one or more premature stop codons and one or more point mutations into the beauvericin synthase gene. In that regard, in some embodiments the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising a beauvericin synthase gene having one or more premature stop codons and one or more point mutations within its sequence. In this embodiment, each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene. In some embodiments, the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising one or more mutations in a beauvericin synthase gene, wherein the strain produces less beauvericin, produces a modified beauvericin demonstrating reduced or eliminated functionality, or both, as compared to a strain of the same filamentous fungi that does not comprise the mutation(s), even when cultured under conditions that would otherwise cause beauvericin production in unmodified strains of the same species. In some embodiments, the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising one or more mutations in a beauvericin synthase gene, wherein the strain is incapable of producing beauvericin. In some embodiments, the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising one or more genetic mutations such that the strain produces less beauvericin, produces a modified beauvericin demonstrating reduced or eliminated functionality, or both, as compared to a strain of the same filamentous fungi that does not comprise the mutation(s), even when cultured under conditions that would otherwise cause beauvericin production in unmodified strains of the same species. In some embodiments, the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising one or more genetic mutations and is incapable of producing beauvericin. In these embodiments, the genetic mutations are in a beauvericin synthase gene. As provided herein, genetic mutation of one or more mycotoxin-associated genes can result in a filamentous fungal strain that is incapable of producing a mycotoxin, can result in the strain producing less mycotoxin than the unaltered or naturally occurring strain that does not have the same genetic mutation, and / or can result in the strain producing a modified mycotoxin demonstrating reduced or eliminated functionality as compared to the unaltered or naturally occurring strain that does not have the same genetic mutation, when the two strains are grown under substantially the same growth conditions. With respect to production of less mycotoxin, in some embodiments the filamentous fungal strain produces about 10% - about 100% less, in some embodiments about 20% - about 100% less, in some embodiments about 30% - about 100% less, in some embodiments about 40% - about 100% less, in some embodiments about 50% - about 100% less, in some embodiments about 60% - about 100% less, in some embodiments about 70% - about 100% less, in some embodiments about 80% - about 100% less, in some embodiments about 90% - about 100% less, and in some embodiments about 100% less mycotoxin than the naturally occurring strain. In some embodiments the filamentous fungal strain produces about 10%, about 15%, about 20%, about 25%, about 30%, about 35%, about 40%, about 45%, about 50%, about 55%, about 60%, about 65%, about 70%, about 75%, about 80%, about 85%, about 90%, about 95%, about 96%, about 97%, about 98%, about 99% or about 100% less mycotoxin than the naturally occurring strain. In some embodiments the filamentous fungal strain produces, on a dry weight basis, less than about 10 ppb mycotoxin as compared to the naturally occurring strain. In some embodiments the filamentous fungal strain produces less than about 9 ppb, less than about 8 ppb, less than about 7 ppb, less than about 6ppb, less than about 5 ppb, less than about 4.5 ppb, less than about 4 ppb, less than about 3.5 ppb, less than about 3 ppb, less than about 2.5 ppb, less than about 2 ppb, less than about 1.5 ppb, or less than about 1 ppb mycotoxin as compared to the naturally occurring strain. Pigment-Associated Genes In various aspects, the present disclosure provides filamentous fungal strains comprising one or more mutated pigment-associated genes. In some embodiments, such strains are edible and suitable for the production of food products. Such strains either produce reduced levels of a pigment, or have had their ability to produce a pigment completely eliminated, as a result of the mutated gene(s). As stated herein, the mutation(s) can occur via a knockout, or via the introduction of one or more null mutations, premature stop codons, and / or point mutations into the genes, each point mutation independently resulting in either a frameshift mutation, a nonsense mutation, or a missense mutation within the genes. In some embodiments, the pigment-associated gene is any one or more genes selected from: 2,7–dimethoxy–6–(acetoxyethyl)juglone, 3–O–(α–D–ribofuranosyl)– questin, 4–O–methyl erythrostominone, 8–O–methybostrycoidin, 2–(4–((3E,5E)–14– aminotetradeca–3,5–dienyloxy) butyl)–1,2,3,4–tetrahydroisoquinolin–4–ol (ATDBTHIQN), Altenuene, Alternarienoic acid, Alternariol, Alternariol-5-methyl ether, Alterperylenol, Ankaflavin, Anthraquinone derivative, Anthraquinones, Arpink red™, Asperflavin, Aurofusarin, Azaphilones, Bassianin, Bikaverin, Black Perithecial Pigment, Bostrycoidin, Carotenoids, Catenarin, Chaetoglobin A–B, Chaetomugilins A–F, Chaetoviridins A–D, Chromanone, Chrysophanol, Citrinin, Cochliodinol, Culmorin, Cynodontin, Deoxyerythrostominol, Deoxyerythrostominone, Emodin, Epicoccarines A–B, Epicocconone, Epierythrostominol, Epipyridone, Erythroglaucin, Erythrostominone, Eurorubrin, Flavipin, Fusarubin, Guestin, Helminthosporin, Isobenzofuran, Lycopene, Melanin, Mitorubrin, Mitorubrinol, Monapurone A–C, Monarubrin, Monascin, Monascin, Monascorubramine, Monascorubrin, Monasphilone A and B, Monopilol A–D, N– glucosylmonascorubramine, N–glucosylrubropunctamine, Naphthaquinones, Naphthoquinones, Nectriafurone, Neurosporaxanthin, Neurosporen,N orbikaverin, Norjavanicin, O–demethylanhydrofusarubin, O–methyl–6– hydroxynorjavanicin, O– methylanhydrofusarubin, O–methylfusarubin, O–methylsolaniol, Oosporein, Orevactaene, Pachybasin, Phytoene, Purpurogenone, Pyridomacrolidin, Pyridovericin, Rubrocristin, Rubrofusarin, Rubropunctamine, Rubropunctatin, Rubropunctin, Secalonic acid D, Spirilloxanthin, Stemphyperylenol, Tenellin, Tenuazoic acid, Torulene, Tritisporin, Viomellein, Xanthomegnin, β–carotene, γ–carotene, and combinations thereof. Bikaverin-Associated Genes In some embodiments the pigment-associated gene is any gene that encodes a polypeptide useful in the production of bikaverin. Bikaverin is a reddish pigment that can contribute to the inclusion of off-colors in food products that comprise fungal mycelial biomass. Alteration of these genes can occur via any method disclosed herein, or combinations of two or more methods. In some embodiments, the bikaverin-associated gene is a gene encoding a bikaverin synthase, for example bik1, which encodes a polyketide synthase involved in the biosynthesis of bikaverin. The bik1 gene has been isolated from several fungal strains and their sequences determined. The bikaverin biosynthetic gene cluster involved in the bikaverin biosynthesis pathway was previously identified from the filamentous fungal strain Fusarium fujikuroi (Wiemann, P., et al., (2009) Molecular Microbiology, 72: 931-946). Evidence indicates the bikaverin biosynthetic gene cluster comprises six genes, which include genes designated as bik1, bik2, bik3, bik4, bik5, and bik6. Studies have demonstrated that these genes are involved in bikaverin production. Analysis of the F. flavolapis DNA sequence revealed that the F. flavolapis genome possesses a complete set of six genes for bikaverin biosynthesis, as in Fusarium fujikuroi. The gene bik1 encodes a polyketide synthase, which plays a key role in the biosynthesis of bikaverin, as it catalyzes the synthesis of pre-bikaverin (3,8,10,11- tetrahydroxy-1-methyl-12H-benzo[b]xanthen-12-one). bik2 encodes a putative FAD- dependent monooxygenase. Bik3 encodes an O-methyltransferase. The Bik2 and Bik3 proteins convert prebikaverin to Nor-bikaverin. The Bik3 protein converts Nor-bikaverin to bikaverin. bik4 encodes a putative NmrA-like transcriptional regulator. bik5 encodes a Zn(II)2Cys6fungal type transcription factor. bik6 encodes an MFS-type transporter, which may be involved in transport of bikaverin. In some embodiments, the pigment-associated gene is selected from bik1, bik2, bik3, bik4, bik5, bik6, and combinations thereof. In some embodiments, the pigment-associated gene is bik1. In some embodiments, the pigment-associated gene is bik2. In some embodiments, the pigment-associated gene is bik3. In some embodiments, the present disclosure provides a filamentous fungal strain comprising one or more mutations in a gene selected from: bik1, bik2, bik3, bik4, bik5, bik6, and combinations thereof. In some embodiments, the mutations comprise a knockout mutation, one or more null mutations, the introduction of one or more premature stop codons into the gene(s), the introduction of one or more point mutations into the gene(s), and / or the introduction of a mutation by any other means described herein. In that regard, in some embodiments the present disclosure provides a filamentous fungal strain comprising a gene selected from: bik1, bik2, bik3, bik4, bik5, bik6, and combinations thereof, wherein the gene comprises one or more of these mutations within its sequence. In other embodiments, the present disclosure provides a filamentous fungal strain comprising a bik1 gene having one or more of these mutations within its sequence. In other embodiments, the present disclosure provides a filamentous fungal strain comprising a bik2 gene having one or more of these mutations within its sequence. In still other embodiments, the present disclosure provides a filamentous fungal strain comprising a bik3 gene having one or more of these mutations within its sequence. In some embodiments, the mutations comprise the introduction of one or more point mutations into the gene(s), each of which independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). In that regard, in some embodiments the present disclosure provides a filamentous fungal strain comprising a gene selected from: bik1, bik2, bik3, bik4, bik5, bik6, and combinations thereof, wherein the gene comprises one or more point mutations within its sequence. In other embodiments, the present disclosure provides a filamentous fungal strain comprising a bik1 gene having one or more point mutations within its sequence. In other embodiments, the present disclosure provides a filamentous fungal strain comprising a bik2 gene having one or more point mutations within its sequence. In still other embodiments, the present disclosure provides a filamentous fungal strain comprising a bik3 gene having one or more point mutations within its sequence. In each of the foregoing embodiments, each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). In some embodiments, the present disclosure provides a filamentous fungal strain comprising one or more mutations in a gene selected from bik1, bik2, bik3, bik4, bik5, bik6, and combinations thereof, wherein the strain produces less bikaverin than a strain of the same filamentous fungi that does not comprise the mutation(s). Such strains also produce reduced bikaverin levels, produce a modified bikaverin demonstrating reduced or eliminated functionality; or both, when cultured under conditions that would otherwise cause bikaverin production in unmodified strains of the same species. In other embodiments, the gene is bik1, bik2, or bik3. In some embodiments, the present disclosure provides a filamentous fungal strain comprising one or more mutations in a gene selected from bik1, bik2, bik3, bik4, bik5, bik6, and combinations thereof, wherein the strain is incapable of producing bikaverin. In other embodiments, the gene is bik1, bik2, or bik3. In some embodiments, the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising one or more mutations in a gene selected from bik1, bik2, bik3, bik4, bik5, bik6, and combinations thereof, wherein the strain produces less bikaverin than a strain of the same filamentous fungi that does not comprise the mutation(s), even when cultured under conditions that would otherwise cause bikaverin production in unmodified strains of the same species. In other embodiments, the gene is bik1, bik2, or bik3. In some embodiments, the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising one or more mutations in a gene selected from bik1, bik2, bik3, bik4, bik5, bik6, and combinations thereof, wherein the strain is incapable of producing bikaverin. In other embodiments, the gene is bik1, bik2, or bik3. In some embodiments, the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising one or more genetic mutations such that the strain produces less bikaverin, produces a modified bikaverin demonstrating reduced or eliminated functionality, or both, as compared to a strain of the same filamentous fungi that does not comprise the mutation(s), even when cultured under conditions that would otherwise cause bikaverin production in unmodified strains of the same species. In some embodiments, the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising one or more genetic mutations and is incapable of producing bikaverin. In these embodiments, the genetic mutations are in one or more genes selected from bik1, bik2, bik3, bik4, bik5, bik6, and combinations thereof. In other embodiments, the genetic mutations are in the bik1, bik2, or bik3 genes. As provided herein, genetic mutation of one or more pigment-associated genes can result in a filamentous fungal strain that is incapable of producing a pigment, can result in the strain producing less pigment than the unaltered or naturally occurring strain that does not have the same genetic mutation, and / or can result in the strain producing a modified pigment demonstrating reduced or eliminated functionality as compared to the unaltered or naturally occurring strain that does not have the same genetic mutation, when the two strains are grown under substantially the same growth conditions. With respect to production of less pigment, in some embodiments the filamentous fungal strain produces about 10% - about 100% less, in some embodiments about 20% - about 100% less, in some embodiments about 30% - about 100% less, in some embodiments about 40% - about 100% less, in some embodiments about 50% - about 100% less, in some embodiments about 60% - about 100% less, in some embodiments about 70% - about 100% less, in some embodiments about 80% - about 100% less, in some embodiments about 90% - about 100% less, and in some embodiments about 100% less pigment than the naturally occurring strain. In some embodiments the filamentous fungal strain produces about 10%, about 15%, about 20%, about 25%, about 30%, about 35%, about 40%, about 45%, about 50%, about 55%, about 60%, about 65%, about 70%, about 75%, about 80%, about 85%, about 90%, about 95%, about 96%, about 97%, about 98%, about 99% or about 100% less pigment than the naturally occurring strain. Ethanol-Associated Genes In various aspects, the present disclosure provides filamentous fungal strains comprising one or more mutated ethanol-associated genes. In some embodiments, such strains are edible and suitable for the production of food products. Such strains either produce reduced levels of ethanol, or have had their ability to produce ethanol completely eliminated, as a result of the mutated gene(s). Some ethanol-associated genes are glucose- associated genes. In some embodiments, the ethanol-associated gene is any gene that encodes a polypeptide useful in the production of ethanol. In some embodiments, the ethanol- associated gene is any one or more genes that encode a polypeptide useful in the production of ethanol selected from: rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof. In some embodiments, the ethanol-associated gene is any gene that encodes a polypeptide useful in the production of ethanol selected from: rco-3, col-26, glt-1, cre1, hgt, and combinations thereof. In some embodiments, the ethanol-associated gene is any gene that encodes a polypeptide useful in the production of ethanol selected from: rco-3, col-26, hgt, and combinations thereof. In some embodiments, the ethanol-associated gene is any gene that encodes a polypeptide useful in the production of ethanol selected from: rco-3, col-26, and a combination thereof. In some embodiments, the ethanol-associated gene is any gene that encodes a polypeptide useful in the production of ethanol selected from: hgt, hxt, and a combination thereof. In some embodiments, the ethanol-associated gene is rco-3. In some embodiments, the ethanol-associated gene is col-26. In some embodiments, the ethanol- associated gene is hgt. Glucose Transport-Associated Genes As noted above, in some embodiments the ethanol-associated gene is any gene that encodes a polypeptide useful in the production of ethanol selected from: rco-3, col-26, glt- 1, cre1, hgt, hxt, and combinations thereof. Evidence indicates each of rco-3, col-26, glt-1, cre1, hgt, and hxt, is involved in glucose transport. As set forth herein, alteration of these genes can occur via a knockout mutation, one or more null mutations, the introduction of one or more premature stop codons into the gene(s), the introduction of one or more point mutations into the gene(s), and / or the introduction of a mutation by any other means described herein. In some embodiments, the ethanol-associated gene is a gene encoding a glucose sensor, for example rco-3, which encodes a glucose sensor involved in the biosynthesis of ethanol. The rco-3 gene has been isolated from several fungal strains and their sequences determined. The low-affinity and high-affinity glucose uptake systems in filamentous fungi involved in the ethanol biosynthesis pathway was previously identified from the filamentous fungal strain Neurospora crassa (Schneider RP, Wiley WR.1971. Kinetic Characteristics of the Two Glucose Transport Systems in Neurospora crassa. J Bacteriol 106). The genes involved in the glucose uptake systems have been isolated and their sequences determined. A glucose transport system in filamentous fungi comprises rco-3, col-26, glt-1, cre1, and hgt, and hxt is also involved in glucose transport. Studies have demonstrated that these genes are involved in ethanol production. Analysis of the F. flavolapis DNA sequence revealed that the F. flavolapis genome possesses a rco-3 gene, as in Neurospora crassa. The gene rco-3 encodes a glucose sensor, which plays a key role in the biosynthesis of ethanol. col-26 encodes a transcription factor, which is involved in regulation of hgt and glt-1 expression. glt-1 encodes a glucose transporter. cre1 encodes a transcription factor, which is involved in regulation of hgt expression. hgt encodes a glucose transporter. hxt encodes a glucose transporter. In some embodiments, the ethanol-associated gene is selected from rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof. In some embodiments, the ethanol-associated gene is rco-3. In some embodiments, the ethanol-associated gene is col-26. In some embodiments, the ethanol-associated gene is glt-1. In some embodiments, the ethanol- associated gene is cre1. In some embodiments, the ethanol-associated gene is hgt. In some embodiments, the ethanol-associated gene is hxt. In some embodiments, the present disclosure provides a filamentous fungal strain comprising one or more mutations in a gene selected from: rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof. In some embodiments, the mutations comprise a knockout mutation, one or more null mutations, the introduction of one or more premature stop codons into the gene(s), the introduction of one or more point mutations into the gene(s), and / or the introduction of a mutation by any other means described herein. In that regard, in some embodiments the present disclosure provides a filamentous fungal strain comprising a gene selected from: rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof, wherein the gene comprises one or more of these mutations within its sequence. In other embodiments, the present disclosure provides a filamentous fungal strain comprising a rco-3 gene having one or more of these mutations within its sequence. In other embodiments, the present disclosure provides a filamentous fungal strain comprising a col-26 gene having one or more of these mutations within its sequence. In still other embodiments, the present disclosure provides a filamentous fungal strain comprising a glt-1 gene having one or more of these mutations within its sequence. In still other embodiments, the present disclosure provides a filamentous fungal strain comprising a cre1 gene having one or more of these mutations within its sequence. In still other embodiments, the present disclosure provides a filamentous fungal strain comprising a hgt gene having one or more of these mutations within its sequence. In still other embodiments, the present disclosure provides a filamentous fungal strain comprising a hxt gene having one or more of these mutations within its sequence. In some embodiments, the mutations comprise the introduction of one or more point mutations into the gene(s), each of which independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). In that regard, in some embodiments the present disclosure provides a filamentous fungal strain comprising a gene selected from: rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof, wherein the gene comprises one or more point mutations within its sequence. In other embodiments, the present disclosure provides a filamentous fungal strain comprising a rco-3 gene having one or more point mutations within its sequence. In other embodiments, the present disclosure provides a filamentous fungal strain comprising a col-26 gene having one or more point mutations within its sequence. In other embodiments, the present disclosure provides a filamentous fungal strain comprising a glt-1 gene having one or more point mutations within its sequence. In other embodiments, the present disclosure provides a filamentous fungal strain comprising a cre1 gene having one or more point mutations within its sequence. In other embodiments, the present disclosure provides a filamentous fungal strain comprising a hgt gene having one or more point mutations within its sequence. In still other embodiments, the present disclosure provides a filamentous fungal strain comprising a hxt gene having one or more point mutations within its sequence. In each of the foregoing embodiments, each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). In some embodiments, the present disclosure provides a filamentous fungal strain comprising one or more mutations in a gene selected from rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof, wherein the strain produces less ethanol than a strain of the same filamentous fungi that does not comprise the mutation(s). Such strains also produce reduced ethanol levels when cultured under conditions that would otherwise cause ethanol production in unmodified strains of the same species. In other embodiments, the gene is rco- 3, col-26, or glt-1. In some embodiments, the present disclosure provides a filamentous fungal strain comprising one or more mutations in a gene selected from rco-3, col-26, glt- 1, cre1, hgt, hxt, and combinations thereof, wherein the strain is incapable of producing ethanol. In other embodiments, the gene is rco-3, col-26, or glt-1. In some embodiments, the present disclosure provides a mycelial biomass, made from a filamentous fungal strain comprising one or more mutations in a gene selected from: rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof. In some embodiments, the mutations comprise a knockout mutation, one or more null mutations, the introduction of one or more premature stop codons into the gene(s), the introduction of one or more point mutations into the gene(s), and / or the introduction of a mutation by any other means described herein. In that regard, in some embodiments the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising a gene selected from: rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof, wherein the gene comprises one or more of these mutations within its sequence. In other embodiments, the gene is rco- 3, col-26, or glt-1. In some embodiments, the mutations comprise the introduction of one or more point mutations into the gene(s), each of which independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). In that regard, in some embodiments the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising a gene selected from: rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof, wherein the gene comprises one or more point mutations within its sequence. In other embodiments, the gene is rco-3, col-26, or glt-1. In each of the foregoing embodiments, each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). In some embodiments, the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising one or more mutations in a gene selected from: rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof, wherein the strain produces less ethanol than a strain of the same filamentous fungi that does not comprise the mutation(s), even when cultured under conditions that would otherwise cause ethanol production in unmodified strains of the same species. In other embodiments, the gene is rco- 3, col-26, or glt-1. In some embodiments, the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising one or more mutations in a gene selected from rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof, wherein the strain is incapable of producing ethanol. In other embodiments, the gene is rco-3, col-26, or glt-1. In some embodiments, the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising one or more genetic mutations such that the strain produces less ethanol, compared to a strain of the same filamentous fungi that does not comprise the mutation(s), even when cultured under conditions that would otherwise cause ethanol production in unmodified strains of the same species. In some embodiments, the present disclosure provides a mycelial biomass made from a filamentous fungal strain comprising one or more genetic mutations and is incapable of producing ethanol. In these embodiments, the genetic mutations are in one or more genes selected from rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof. In other embodiments, the genetic mutations are in the rco-3, col-26, or glt-1 genes. In some embodiments, introducing a null mutation in, or completely knocking out, rco3 allows for glucose metabolism in surface fermentation for biomat production with reduced ethanol production. These embodiments are particularly advantageous for use with those fungal strains that may experience a “bottleneck” or slowdown in the glycolytic pathway that converts glucose to pyruvate (for example, a Fusarium species such as F. flavolapis). This bottleneck can cause a buildup of the intermediate glucose-6-phosphate which then must be channeled to other metabolic pathways, for example heterolactic fermentation, that produce both ethanol and lactic acid which can be toxic to fungi. Rco3 is a glucose sensor that likely regulates the uptake of glucose and / or flux through the glycolytic pathway which allows an organism to utilize glucose more efficiently. Deleting rco3 or mutating it and making it a null gene may reduce the rate of the uptake of glucose uptake and therefore, help to prevent the buildup of the intermediate and allow all the glucose to go to pyruvate. These mutations are also useful in submerged fermentation, as rco-3 knockout and / or null gene mutants will allow for batch fermentation of fungi, where all of the glucose needed for a fermentation process can be added at one time. The rco-3 knockout and / or null gene mutants will prevent the accumulation of G6P intermediates, and thus the production of ethanol via undesirable fermentation pathways. As provided herein, genetic mutation of one or more ethanol-associated genes can result in a filamentous fungal strain that is incapable of producing ethanol, and / or can result in the strain producing less ethanol than the unaltered or naturally occurring strain that does not have the same genetic mutation, when the two strains are grown under substantially the same growth conditions. With respect to production of less ethanol, in some embodiments the filamentous fungal strain produces about 10% - about 100% less, in some embodiments about 20% - about 100% less, in some embodiments about 30% - about 100% less, in some embodiments about 40% - about 100% less, in some embodiments about 50% - about 100% less, in some embodiments about 60% - about 100% less, in some embodiments about 70% - about 100% less, in some embodiments about 80% - about 100% less, in some embodiments about 90% - about 100% less, and in some embodiments about 100% less ethanol than the naturally occurring strain. In some embodiments the filamentous fungal strain produces about 10%, about 15%, about 20%, about 25%, about 30%, about 35%, about 40%, about 45%, about 50%, about 55%, about 60%, about 65%, about 70%, about 75%, about 80%, about 85%, about 90%, about 95%, about 96%, about 97%, about 98%, about 99% or about 100% less ethanol than the naturally occurring strain. In some embodiments, a filamentous fungal strain comprises at least one mutation in a mycotoxin-associated gene and at least one mutation in a pigment-associated gene, and the mutations comprise a knockout mutation, one or more null mutations, the introduction of one or more premature stop codons into the gene(s), the introduction of one or more point mutations into the gene(s), and / or the introduction of a mutation by any other means described herein. In some embodiments, the mycotoxin-associated gene is selected from Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof. In some embodiments, the mycotoxin-associated gene is Fum1. In some embodiments, the mycotoxin-associated gene is Fum6. In some embodiments, the mycotoxin-associated gene is Fum8. In some embodiments, the pigment-associated gene is selected from bik1, bik2, bik3, bik4, bik5, bik6, and combinations thereof. In some embodiments, the pigment-associated gene is bik1. In some embodiments, a filamentous fungal strain comprises at least one mutation in a mycotoxin-associated gene and at least one mutation in an ethanol-associated gene, and the mutations comprise a knockout mutation, one or more null mutations, the introduction of one or more premature stop codons into the gene(s), the introduction of one or more point mutations into the gene(s), and / or the introduction of a mutation by any other means described herein. In some embodiments, the mycotoxin-associated gene is selected from Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof. In some embodiments, the mycotoxin-associated gene is Fum1. In some embodiments, the mycotoxin-associated gene is Fum6. In some embodiments, the mycotoxin-associated gene is Fum8. In some embodiments, the ethanol-associated gene is selected from rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof. In some embodiments, the ethanol-associated gene is rco-3. In some embodiments, a filamentous fungal strain comprises at least one mutation in a pigment-associated gene and at least one mutation in an ethanol-associated gene, and the mutations comprise a knockout mutation, one or more null mutations, the introduction of one or more premature stop codons into the gene(s), the introduction of one or more point mutations into the gene(s), and / or the introduction of a mutation by any other means described herein. In some embodiments, the pigment-associated gene is selected from bik1, bik2, bik3, bik4, bik5, bik6, and combinations thereof. In some embodiments, the pigment- associated gene is bik1. In some embodiments, the mycotoxin-associated gene is Fum6. In some embodiments, the mycotoxin-associated gene is Fum8. In some embodiments, the ethanol-associated gene is selected from rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof. In some embodiments, the ethanol-associated gene is rco-3. In some embodiments, a filamentous fungal strain comprises at least one mutation in a mycotoxin-associated gene, at least one mutation in a pigment-associated gene, and at least one mutation in an ethanol-associated gene, and the mutations comprise a knockout mutation, one or more null mutations, the introduction of one or more premature stop codons into the gene(s), the introduction of one or more point mutations into the gene(s), and / or the introduction of a mutation by any other means described herein. In some embodiments, the mycotoxin-associated gene is selected from Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof. In some embodiments, the mycotoxin-associated gene is Fum1. In some embodiments, the mycotoxin-associated gene is Fum6. In some embodiments, the mycotoxin-associated gene is Fum8. In some embodiments, the mycotoxin-associated gene is Fum8. In some embodiments, the pigment-associated gene is selected from bik1, bik2, bik3, bik4, bik5, bik6, and combinations thereof. In some embodiments, the pigment- associated gene is bik1. In some embodiments, the ethanol-associated gene is selected from rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof. In some embodiments, the ethanol-associated gene is rco-3. Genetic Alteration and Selection The present disclosure is not limited in the manner in which mutations (e.g., stop codons and / or point mutations) are introduced into the genes of a filamentous fungal strain. Generally speaking, mutations may be introduced into one or more mycotoxin-associated genes by mutagenesis, a general process in which mutations are purposely introduced into one or more mycotoxin-associated genes. Mutagenesis typically occurs in one of two ways: via random mutagenesis, or via site directed mutagenesis, though it is possible for both approaches to be used concurrently. The primary difference between random and site directed mutagenesis is the manner in which a mutation is introduced. Briefly, random mutagenesis does exactly what its name implies – introduces mutations into one or more mycotoxin-associated genes randomly. Its mode of operation occurs without direction or conscious decision as to the site of mutation. Site directed mutagenesis, on the other hand, introduces mutations into specific locations, for example to specific chromosomes, genes, or even to specific nucleotides. The specificity of site directed mutations in very high and intentionally directed. Genetic alterations include introduction of one or more mutations that can comprise one or more of loss of function, reduction of function, and / or enhancement of function of a protein. Genetic alterations also include introduction of one or more mutations that affect expression of a gene, for example one or more mutations in a promotor region, repressor region, enhancer region, and the like. Loss of function mutations eliminate the function of a protein, for example by deleting the entire gene that encodes the protein or introduction of a stop codon that leads to complete inaction of the function of the mutant protein and / or degradation of the mutant protein. Reduction of function mutations reduce the activity of one or more functions of a mutant protein relative to the native protein. Reduction of function mutations include loss of function mutations. Enhancement of function mutations enhance the activity of one or more functions of a mutant protein relative to the native protein. A genetic alteration or mutation can comprise deletion of one or more nucleotides. A genetic alteration or mutation can comprise deletion of a portion of a gene. A genetic alteration or mutation can comprise deletion of an entire gene. A genetic alteration or mutation can comprise insertion of one or more nucleotides. A genetic alteration or mutation can comprise insertion of a portion of a gene. A genetic alteration or mutation can comprise insertion of an entire gene. A genetic alteration or mutation can comprise deletion of one or more nucleotides and insertion of one or more nucleotides. A genetic alteration or mutation can comprise deletion of one or more nucleotides and insertion of a portion of a gene. A genetic alteration or mutation can comprise deletion of one or more nucleotides and insertion of an entire gene. A genetic alteration or mutation can comprise deletion of a portion of a gene and insertion of one or more nucleotides. A genetic alteration or mutation can comprise deletion of a portion of a gene and insertion of a portion of a gene. A genetic alteration or mutation can comprise deletion of a portion of a gene and insertion of an entire gene. A genetic alteration or mutation can comprise deletion of an entire gene and insertion of one or more nucleotides. A genetic alteration or mutation can comprise deletion of an entire gene and insertion of a portion of a gene. A genetic alteration or mutation can comprise deletion of an entire gene and insertion of an entire gene. A genetic alteration or mutation can comprise a point mutation. A genetic alteration or mutation can comprise a point mutation and deletion of one or more nucleotides. A genetic alteration or mutation can comprise a point mutation and insertion of one or more nucleotides. A genetic alteration or mutation can comprise a point mutation, deletion of one or more nucleotides, and insertion of one or more nucleotides. Knockout Mutations A knockout mutation, also referred to commonly as a gene knockout, refers to the use of genetic engineering to inactivate or remove one or more specific genes from an organism. When performing a gene knockout, the goal is typically to make a gene completely nonfunctional. Knockout mutations may occur via several ways. The simplest, and perhaps the most effective, way to create a complete gene knockout is to remove the gene entirely by cutting it out of the genome. Alternatively, a knockout mutation can occur by targeting and changing regions of a gene that are known or suspected to be important for its function. The change here can be elimination of these regions, or mutation via any other means disclosed herein. Gene targeting and knockout techniques have been in use for at least about thirty years and during that time thousands of genes have been successfully knocked out of numerous species. As of about 2010, approximately 11,000 genes had been knocked out in murine species alone, accounting for roughly half of the mouse genome (see, e.g., Vogel G., Science (2007) 318:178–179; Sikorski & Peters, Nature Biotech (1997) 15:289). Knockout mutations can occur via any one of several known methods, for example according to any method provided in Gene Knockout Protocols, Wurst and Kühn Eds. (2009), Volume 530, ISBN : 978-1-934115-26-8. Random Mutagenesis As noted above, random mutagenesis refers to a process of introducing mutations to organisms in a random fashion. It is non-specific in its approach, all mutations introduced via random mutagenesis occur randomly. Generally speaking, random mutagenesis involves exposing an organism to a mutagen for a period of time and then selecting for mutant varieties or strains that contain a desired trait. The mutagens employed can be physical mutagens, such as UV radiation, or chemical mutagens like alkylating agents. Advantageously, organisms that are mutated by random mutagenesis are not genetically modified organisms (GMO), as such term is used by regulatory authorities. For example, in 2023 the US FDA considers a GMO to be: a plant, animal, or microorganism that has had its genetic material (DNA) changed using technology that generally involves the specific modification of DNA, including the transfer of specific DNA from one organism to another. U.S. Food & Drug Administration, “Agricultural Biotechnology,” April 19, 2023 (https: / / www.fda.gov / food / consumers / agricultural- biotechnology#:~:text=What%20makes%20it%20a%20GMO,from%20one%20org anism%20to%20another.) Similarly, in 2023 the EU considers a GMO to be a non-human organism “whose genetic material has been altered in a way that does not occur naturally by mating and / or natural recombination” (https: / / eur-lex.europa.eu / EN / legal-content / glossary / genetically-modified- organisms-gmo.html). The use of random mutagenesis avoids both definitions. In some embodiments, the filamentous fungal strain development methods disclosed herein are based on random mutagenesis. For example, mycotoxin-producing strains are exposed to different, random mutagens for a period of time. Thereafter, the ability for the resulting mutant strains to produce one or more mycotoxins is tested. In doing so, the strains that have had their ability to produce one or more mycotoxins reduced, or in some embodiments completely eliminated, can be deduced and selected for further development. For example, it is possible to confirm the presence of a randomly generated mutation in a mycotoxin-associated gene by sequencing that gene and comparing that sequence to the wild-type gene sequence. Random mutagenesis may similarly be used to generate mutations in pigment-associated genes and / or ethanol-associated genes in filamentous fungal strains. The resulting mutants can be screened to identify those that exhibit reduced pigment levels and / or reduced ethanol production, respectively. Site-Directed Mutagenesis As noted above, site directed mutagenesis is an intentional, specific process used to induce mutations into specific locations in a genome. This process is commonly referred to by the umbrella term of “genetic engineering” and is one of the most commonly used laboratory techniques for introducing mutations into DNA sequences. There are numerous methods for achieving site-directed mutagenesis, each having its own process. Oligonucleotide-directed mutagenesis involves the synthesis of a synthetic DNA primer containing a desired mutation. The primer is complementary to the template DNA (e.g., all or a portion of a mycotoxin-associated gene) around the mutation site, which allows it to hybridize with the gene of interest. The mutation may be a point mutation, multiple base changes, deletion, or insertion. Once hybridized to the gene of interest, the primer is extended using a DNA polymerase, which copies the rest of the gene. The resulting copy of the gene contains the mutation(s) and is then introduced into a host cell in a vector and cloned. Mutants are selected by DNA sequencing to confirm that they contain the desired mutation. This was the original method falling under the umbrella of site-directed mutagenesis and is notoriously inefficient due to a low number of successful mutants produced. Kunkel’s method inserts a DNA fragment to be mutated into a phagemid, which is then transformed into a bacterial strain for replication. After replication, the bacterial strain releases single-stranded replicants of the phage DNA into the surrounding environment (for example, into a culture media), which is isolated and used as a template for mutagenesis. More specifically, an oligonucleotide containing the desired mutation is used for primer extension; a heteroduplex DNA complex is created from one parental (non-mutated) strand of DNA and a mutated strand. The heteroduplex is then transformed into a bacterial strain where the non-mutated, parental DNA strand is degraded, leaving nearly all of the resulting DNA containing the desired mutant. Cassette mutagenesis is a method where a fragment of DNA containing a mutant- carrying gene sequence of interest is synthesized, and then inserted into a plasmid via the use of restriction enzyme sites. The plasmid can then be used to transform a cell of interest. This method can generate mutants at close to 100% efficiency, but is limited by the availability of suitable restriction sites flanking the site that is to be mutated. PCR mutagenesis utilizes synthetic oligonucleotide primers to produce a DNA fragment containing the desired mutation in sufficient quantity to be inserted into a cell or other, desired location using standard recombinant molecular biology techniques. In its simplest form, this method utilizes two oligonucleotide fragments, one of which contains the mutation of interest. A single step of PCR will then amplify a heteroduplex containing the desired mutant, which may be used to transform cells using standard techniques. Other variations employ three, four or more synthetic oligonucleotides. These variations utilize multiple steps of PCR so that the final fragment to be ligated can contain the desired mutation. Homologous recombination uses a cell’s DNA repair mechanisms to introduce a mutation, including deletion of a gene or part of a gene and / or genome, alteration of one or more bases in a gene and / or genome, and / or insertion of one or more bases in a gene and / or genome. Homologous recombination is a targeted strategy for mutagenesis that involves insertion of a DNA sequence into a cell, in which the DNA sequence has homology to a target sequence. The inserted DNA, however, also includes one or more mismatches with the genomic DNA, and the mismatch(es) is incorporated into the genome by the cell’s DNA repair machinery to produce a mutant genome. For example, a gene can be knocked out from a genome by inserting into a cell a DNA sequence that has homology to genomic sequences flanking the gene but is missing the sequence of the gene that will be knocked out. For example, a DNA sequence can contain flanking arms of homology to the genomic sequence around a gene to be knocked out but and also a different gene in place of the gene to be knocked out, for example a selectable marker sequence in place of the gene to be knocked out. The DNA sequence can be inserted into a cell, and the cell can use homologous recombination to remove the gene sequence and replace it with the selectable marker sequence. In a similar manner, instead of replacing a whole gene, the DNA sequence can provide for insertion, deletion, or alteration of one or more nucleotides in any genomic sequence. Similarly, the development of CRISPR / Cas9 technology has allowed for elegant and specific editing of the genome, allowing mutagenesis to be performed in vivo with relative ease. Other in vivo site directed mutagenesis techniques include Delitto Perfetto, transplacement "pop-in pop-out," direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker, direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker using long homologous regions, and in vivo site-directed mutagenesis with synthetic oligonucleotides, among others. Selection; Adaptive Laboratory Evolution Once one or more mutations have been successfully introduced into one or more genes of interest, it can be advantageous to identify those strains for further development. In various embodiments, mutant strains are identified by screening for a reduced, or complete lack of any, capacity to produce a reaction product (e.g., an encoded protein, a pigment, a mycotoxin, and / or ethanol). In some embodiments, mutant strains are identified by screening for production of a modified reaction product demonstrating reduced, or eliminated, functionality. Such screening can occur in any number of ways, including for example via assays that measure the production of the reaction product. Other suitable mutation detection techniques include, for example, denaturing gradient gel electrophoresis, constant denaturing gel electrophoresis, temporal temperature gradient gel electrophoresis, single-strand conformation polymorphism, protein truncation tests, and high resolution melt analyses, among others. Many of these techniques utilize DNA amplification via PCR in order to generate sufficient copy numbers of the mutated gene or genes of interest for study. Typically, each of these screening techniques utilize wild-type control samples as a basis for comparison, as such samples do not contain a mutation introduced into the gene or genes of interest. DNA sequencing can also be used to verify the mutation after any of these techniques. Once an initial selection of a mutant strain, containing one or more mutations of interest in a gene or genes of interest, occurs, it can be useful to subject such strain to further development in order to improve one or more desired characteristics. Adaptive laboratory evolution (ALE) involves the use of controlled laboratory experiments to observe evolutionary dynamics. Evolution is observed in the laboratory as individuals / populations adapt to new environmental conditions by natural selection. For example, if a mutated strain containing a desirable mutation in a gene or genes of interest is identified, but demonstrates a slow growth rate, ALE can be utilized to try to improve the growth characteristics of the strain. In various embodiments, ALE can be used to further develop isolated, mutant strains in order to improve one or more growth characteristics of such strains. For example, ALE can be used to push a mutant strain to develop higher growth rates, greater cell densities, diminished reaction product production, and / or other characteristics. In some embodiments, ALE is accomplished by serially diluting a mutant strain in flasks and / or plates. A parental strain is inoculated into medium and cultured for a desired amount of time, for example 24 – 96 hours (or any time within such range). One or more aliquots of the resulting culture are transferred to other flasks or plates containing fresh growth media. This process is repeated a number of times until a desired final dilution is obtained, which is transferred again to fresh flasks or plates for growth. Each passage may incorporate one or more selective pressures, essentially forcing the mutant strain to adapt to the selective pressure(s) with each passage. Suitable selective pressures include, for example, maximum growth rate testing, direct competition testing between a non-mutant strain and its mutant (e.g., via competitive fitness assays), subjecting a mutant strain to toxic concentrations of one or more compounds, contacting a mutant strain with one or more inhibiting compounds, determination of absolute biomass yield, nutrient stress (e.g., nutrient deprivation [carbon source deprivation, nitrogen source deprivation, trace metals deprivation, etc.], omission, excess, etc.), environmental stress (e.g., temperature, pressure, pH, oxygen concentration, osmotic stress, etc.), combinations of any of the foregoing, and others (see, e.g., Dragosits et al., Microb Cell Fact 12, 64 (2013). https: / / doi.org / 10.1186 / 1475-2859-12-64). Evolution occurs via natural genetic and / or stochastic change during this process. In the final growth stage, one or more colonies displaying one or more desired characteristics (e.g., rapid growth rate, high cell density, etc.) are selected as the desired strain(s). Optionally, the mutant gene of interest is then sequenced to confirm the nature of the mutation(s) introduced. In some embodiments adaptive laboratory evolution (ALE) can be used to improve a strain. In some embodiments, ALE involves improving a strain that contains one or more mutations in a gene or genes of interest. In some embodiments, the gene of interest is at least partly responsible for producing a reaction product. In some embodiments, the gene or genes of interest comprises a mycotoxin-associated gene or genes of interest, and the reaction product is one or more mycotoxins. In some embodiments, the gene or genes of interest comprises a pigment-associated gene or genes of interest, and the reaction product is one or more pigments. In some embodiments, the gene or genes of interest comprises an ethanol- associated gene or genes of interest, and the reaction product is ethanol. Methods Mycotoxin-related methods The present disclosure provides methods of producing filamentous fungal strains having one or more mutations introduced into one or more mycotoxin-associated genes. The methods include introducing a knockout mutation or one or more null mutations, premature stop codons, point mutations, and / or a mutation by any other means described herein into the mycotoxin-associated gene(s), wherein each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). The methods can employ either random mutagenesis techniques, site directed mutagenesis techniques, or both. Additionally, the methods can optionally include the use of one or more techniques to select for the mutant strains, and optionally the use of ALE in order to improve one or more of the mutant strain’s characteristics. In some embodiments, the present disclosure provides methods of producing filamentous fungal strains having one or more stop codons introduced into one or more mycotoxin-associated genes. The methods include subjecting a filamentous fungi to random mutagenesis by exposing the fungi to either a physical mutagen or a chemical mutagen for a suitable period of time. The mycotoxin-associated genes can be any one or more of those disclosed herein. In some embodiments, the physical mutagen is selected from gamma rays, X rays, UV light, fast neutrons, thermal neutrons, beta particles, alpha particles, and combinations thereof. In some embodiments, the physical mutagen is UV light. In such embodiments, the exposure occurs for a period of time selected from 30 seconds – 5 minutes, 30 seconds – 4 minutes, 30 seconds to 3 minutes, 30 seconds – 2 minutes, and 30 seconds – 1 minute. In some embodiments, the exposure occurs for a period of time selected from 1 – 5 minutes, 5 – 10 minutes, 10 – 15 minutes, 15 – 20 minutes, 20 – 30 minutes, 30 minutes – 5 hours, 30 minutes – 4 hours, 30 minutes – 3 hours, 30 minutes – 2 hours, 30 minutes – 1 hour, and 30 – 45 minutes. In some embodiments, the chemical mutagen is selected from ethyl methyl sulfate, nitrogen mustards, mitomycin, methyl methane sulfonate, diethyl sulfate, nitrosoguanidine, ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, acridine orange, ethidium bromide, proflavin, daunorubicin, and combinations thereof. In some embodiments, the chemical mutagen is selected from ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, and combinations thereof. In such embodiments, the chemical mutagen is utilized at a concentration of 1 mM or less, 0.9 mM or less, 0.8 mM or less, 0.7 mM or less, 0.6 mM or less, 0.5 mM or less, 0.4 mM or less, or 0.3 mM or less. Alternatively, in such embodiments the chemical mutagen is utilized in an amount of 4% w / w or less, 3% w / w or less, 2% w / w or less, 1.5% w / w or less, 1% w / w or less, 0.75% w / w or less, 0.5% w / w or less, 0.4% w / w or less, 0.3% w / w or less, 0.2% w / w or less, or 0.1% w / w or less. In such embodiments, the period of time is selected from 30 minutes – 5 hours, 30 minutes – 4 hours, 30 minutes – 3 hours, 30 minutes – 2 hours, 30 minutes – 1 hour, and 30 – 45 minutes. In certain embodiments, the period of time increases as the concentration of the chemical mutagen decreases, whereas in other embodiments the period of time is independent of the concentration or amount of the chemical mutagen. Optionally, the methods can further include screening the strains to confirm the presence of the one or more stop codons in the one or more mycotoxin-associated genes. Such screening includes identification of a reduced, or complete lack of any, capacity to produce a mycotoxin in the strains. In some embodiments, the screening method is selected from mycotoxin production assays, denaturing gradient gel electrophoresis, constant denaturing gel electrophoresis, temporal temperature gradient gel electrophoresis, single- strand conformation polymorphism, protein truncation tests, high resolution melt analyses, sequencing the one or more mycotoxin-associated genes, and combinations thereof. In some embodiments, the screening method is mycotoxin production assays, sequencing the one or more mycotoxin-associated genes, or both. Optionally, the methods can further include the use of ALE to develop one or more characteristics in the strains. In some embodiments, ALE is accomplished by serially diluting a mutant strain in flasks and / or plates. In some embodiments, the characteristics are selected from higher growth rates, greater cell densities, diminished mycotoxin production, and combinations thereof. In some embodiments, the present disclosure provides methods of producing filamentous fungal strains having one or more stop codons introduced into one or more mycotoxin-associated genes selected from Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof. The methods include subjecting a filamentous fungus to random mutagenesis by exposing the fungi to either a physical mutagen or a chemical mutagen for a suitable period of time. In some embodiments, the mycotoxin-associated gene is Fum1. In some embodiments, the mycotoxin-associated gene is Fum6. In some embodiments, the mycotoxin-associated gene is Fum8. In some embodiments, the physical mutagen is selected from gamma rays, X rays, UV light, fast neutrons, thermal neutrons, beta particles, alpha particles, and combinations thereof. In some embodiments, the physical mutagen is UV light. In such embodiments, the exposure occurs for a period of time selected from 30 seconds – 5 minutes, 30 seconds – 4 minutes, 30 seconds to 3 minutes, 30 seconds – 2 minutes, and 30 seconds – 1 minute. In some embodiments, the chemical mutagen is selected from ethyl methyl sulfate, nitrogen mustards, mitomycin, methyl methane sulfonate, diethyl sulfate, nitrosoguanidine, ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, acridine orange, ethidium bromide, proflavin, daunorubicin, and combinations thereof. In some embodiments, the chemical mutagen is selected from ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, and combinations thereof. In such embodiments, the chemical mutagen is utilized at a concentration of 1 mM or less, 0.9 mM or less, 0.8 mM or less, 0.7 mM or less, 0.6 mM or less, 0.5 mM or less, 0.4 mM or less, or 0.3 mM or less. Alternatively, in such embodiments the chemical mutagen is utilized in an amount of 4% w / w or less, 3% w / w or less, 2% w / w or less, 1.5% w / w or less, 1% w / w or less, 0.75% w / w or less, 0.5% w / w or less, 0.4% w / w or less, 0.3% w / w or less, 0.2% w / w or less, or 0.1% w / w or less. In such embodiments, the period of time is selected from 30 minutes – 5 hours, 30 minutes – 4 hours, 30 minutes – 3 hours, 30 minutes – 2 hours, 30 minutes – 1 hour, and 30 – 45 minutes. In certain embodiments, the period of time increases as the concentration of the chemical mutagen decreases, whereas in other embodiments the period of time is independent of the concentration or amount of the chemical mutagen. Optionally, the methods can further include screening the strains to confirm the presence of the one or more stop codons in the one or more mycotoxin-associated genes. Such screening includes identification of a strain that produces less fumonisin than a strain of the same filamentous fungi that does not comprise the mutation(s), even in some embodiments when cultured under conditions that would otherwise cause fumonisin production in unmodified strains of the same species. Such screening also includes identification of a strain that is incapable of producing fumonisin. In some embodiments, the screening method is selected from fumonisin production assays, denaturing gradient gel electrophoresis, constant denaturing gel electrophoresis, temporal temperature gradient gel electrophoresis, single-strand conformation polymorphism, protein truncation tests, high resolution melt analyses, sequencing the one or more mycotoxin-associated genes, and combinations thereof. In some embodiments, the screening method is fumonisin production assays, sequencing the one or more mycotoxin-associated genes, or both. Optionally, the methods can further include the use of ALE to develop one or more characteristics in the strains. In some embodiments, ALE is accomplished by serially diluting a mutant strain in flasks and / or plates. In some embodiments, the characteristics are selected from higher growth rates, greater cell densities, diminished fumonisin production, and combinations thereof. In some embodiments, the present disclosure provides methods of producing filamentous fungal strains having one or more stop codons introduced into a beauvericin synthase gene. The methods include subjecting a filamentous fungi to random mutagenesis by exposing the fungi to either a physical mutagen or a chemical mutagen for a suitable period of time. In some embodiments, the physical mutagen is selected from gamma rays, X rays, UV light, fast neutrons, thermal neutrons, beta particles, alpha particles, and combinations thereof. In some embodiments, the physical mutagen is UV light. In such embodiments, the exposure occurs for a period of time selected from 30 seconds – 5 minutes, 30 seconds – 4 minutes, 30 seconds to 3 minutes, 30 seconds – 2 minutes, and 30 seconds – 1 minute. In some embodiments, the chemical mutagen is selected from ethyl methyl sulfate, nitrogen mustards, mitomycin, methyl methane sulfonate, diethyl sulfate, nitrosoguanidine, ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, acridine orange, ethidium bromide, proflavin, daunorubicin, and combinations thereof. In some embodiments, the chemical mutagen is selected from ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, and combinations thereof. In such embodiments, the chemical mutagen is utilized at a concentration of 1 mM or less, 0.9 mM or less, 0.8 mM or less, 0.7 mM or less, 0.6 mM or less, 0.5 mM or less, 0.4 mM or less, or 0.3 mM or less. Alternatively, in such embodiments the chemical mutagen is utilized in an amount of 4% w / w or less, 3% w / w or less, 2% w / w or less, 1.5% w / w or less, 1% w / w or less, 0.75% w / w or less, 0.5% w / w or less, 0.4% w / w or less, 0.3% w / w or less, 0.2% w / w or less, or 0.1% w / w or less. In such embodiments, the period of time is selected from 30 minutes – 5 hours, 30 minutes – 4 hours, 30 minutes – 3 hours, 30 minutes – 2 hours, 30 minutes – 1 hour, and 30 – 45 minutes. In certain embodiments, the period of time increases as the concentration of the chemical mutagen decreases, whereas in other embodiments the period of time is independent of the concentration or amount of the chemical mutagen. Optionally, the methods can further include screening the strains to confirm the presence of the one or more stop codons in the one or more mycotoxin-associated genes. Such screening includes identification of a strain that produces less beauvericin than a strain of the same filamentous fungi that does not comprise the mutation(s), even in some embodiments when cultured under conditions that would otherwise cause beauvericin production in unmodified strains of the same species. Such screening also includes identification of a strain that is incapable of producing beauvericin. In some embodiments, the screening method is selected from beauvericin production assays, denaturing gradient gel electrophoresis, constant denaturing gel electrophoresis, temporal temperature gradient gel electrophoresis, single-strand conformation polymorphism, protein truncation tests, high resolution melt analyses, sequencing the one or more mycotoxin-associated genes, and combinations thereof. In some embodiments, the screening method is beauvericin production assays, sequencing the one or more mycotoxin-associated genes, or both. Optionally, the methods can further include the use of ALE to develop one or more characteristics in the strains. In some embodiments, ALE is accomplished by serially diluting a mutant strain in flasks and / or plates. In some embodiments, the characteristics are selected from higher growth rates, greater cell densities, diminished beauvericin production, and combinations thereof. In some embodiments, the present disclosure provides methods of producing a mycelial biomass from filamentous fungal strains having one or more stop codons introduced into one or more mycotoxin-associated genes. The methods include subjecting a filamentous fungi to random mutagenesis by exposing the fungi to either a physical mutagen or a chemical mutagen for a suitable period of time and producing a mycelial biomass therefrom. The mycotoxin-associated genes can be any one or more of those disclosed herein. In some embodiments, the physical mutagen is selected from gamma rays, X rays, UV light, fast neutrons, thermal neutrons, beta particles, alpha particles, and combinations thereof. In some embodiments, the physical mutagen is UV light. In such embodiments, the exposure occurs for a period of time selected from 30 seconds – 5 minutes, 30 seconds – 4 minutes, 30 seconds to 3 minutes, 30 seconds – 2 minutes, and 30 seconds – 1 minute. In some embodiments, the chemical mutagen is selected from ethyl methyl sulfate, nitrogen mustards, mitomycin, methyl methane sulfonate, diethyl sulfate, nitrosoguanidine, ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, acridine orange, ethidium bromide, proflavin, daunorubicin, and combinations thereof. In some embodiments, the chemical mutagen is selected from ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, and combinations thereof. In such embodiments, the chemical mutagen is utilized at a concentration of 1 mM or less, 0.9 mM or less, 0.8 mM or less, 0.7 mM or less, 0.6 mM or less, 0.5 mM or less, 0.4 mM or less, or 0.3 mM or less. Alternatively, in such embodiments the chemical mutagen is utilized in an amount of 4% w / w or less, 3% w / w or less, 2% w / w or less, 1.5% w / w or less, 1% w / w or less, 0.75% w / w or less, 0.5% w / w or less, 0.4% w / w or less, 0.3% w / w or less, 0.2% w / w or less, or 0.1% w / w or less. In such embodiments, the period of time is selected from 30 minutes – 5 hours, 30 minutes – 4 hours, 30 minutes – 3 hours, 30 minutes – 2 hours, 30 minutes – 1 hour, and 30 – 45 minutes. In certain embodiments, the period of time increases as the concentration of the chemical mutagen decreases, whereas in other embodiments the period of time is independent of the concentration or amount of the chemical mutagen. Optionally, the methods can further include screening the strains to confirm the presence of the one or more stop codons in the one or more mycotoxin-associated genes prior to production of a mycelial biomass. Such screening includes identification of a reduced, or complete lack of any, capacity to produce a mycotoxin in the strains. In some embodiments, the screening method is selected from mycotoxin production assays, denaturing gradient gel electrophoresis, constant denaturing gel electrophoresis, temporal temperature gradient gel electrophoresis, single-strand conformation polymorphism, protein truncation tests, high resolution melt analyses, sequencing the one or more mycotoxin- associated genes, and combinations thereof. In some embodiments, the screening method is mycotoxin production assays, sequencing the one or more mycotoxin-associated genes, or both. Optionally, the methods can further include the use of ALE to develop one or more characteristics in the strains. In some embodiments, ALE is accomplished by serially diluting a mutant strain in flasks and / or plates. In some embodiments, the characteristics are selected from higher growth rates, greater cell densities, diminished mycotoxin production, and combinations thereof. In some embodiments, the present disclosure provides methods of producing a mycelial biomass from filamentous fungal strains having one or more stop codons introduced into one or more mycotoxin-associated genes selected from Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof. The methods include subjecting a filamentous fungus to random mutagenesis by exposing the fungi to either a physical mutagen or a chemical mutagen for a suitable period of time and producing a mycelial biomass therefrom. In some embodiments, the mycotoxin-associated gene is Fum1. In some embodiments, the mycotoxin-associated gene is Fum6. In some embodiments, the mycotoxin-associated gene is Fum8. In some embodiments, the physical mutagen is selected from gamma rays, X rays, UV light, fast neutrons, thermal neutrons, beta particles, alpha particles, and combinations thereof. In some embodiments, the physical mutagen is UV light. In such embodiments, the exposure occurs for a period of time selected from 30 seconds – 5 minutes, 30 seconds – 4 minutes, 30 seconds to 3 minutes, 30 seconds – 2 minutes, and 30 seconds – 1 minute. In some embodiments, the chemical mutagen is selected from ethyl methyl sulfate, nitrogen mustards, mitomycin, methyl methane sulfonate, diethyl sulfate, nitrosoguanidine, ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, acridine orange, ethidium bromide, proflavin, daunorubicin, and combinations thereof. In some embodiments, the chemical mutagen is selected from ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, and combinations thereof. In such embodiments, the chemical mutagen is utilized at a concentration of 1 mM or less, 0.9 mM or less, 0.8 mM or less, 0.7 mM or less, 0.6 mM or less, 0.5 mM or less, 0.4 mM or less, or 0.3 mM or less. Alternatively, in such embodiments the chemical mutagen is utilized in an amount of 4% w / w or less, 3% w / w or less, 2% w / w or less, 1.5% w / w or less, 1% w / w or less, 0.75% w / w or less, 0.5% w / w or less, 0.4% w / w or less, 0.3% w / w or less, 0.2% w / w or less, or 0.1% w / w or less. In such embodiments, the period of time is selected from 30 minutes – 5 hours, 30 minutes – 4 hours, 30 minutes – 3 hours, 30 minutes – 2 hours, 30 minutes – 1 hour, and 30 – 45 minutes. In certain embodiments, the period of time increases as the concentration of the chemical mutagen decreases, whereas in other embodiments the period of time is independent of the concentration or amount of the chemical mutagen. Optionally, the methods can further include screening the strains to confirm the presence of the one or more stop codons in the one or more mycotoxin-associated genes prior to producing a mycelial biomass. Such screening includes identification of a strain that produces less fumonisin than a strain of the same filamentous fungi that does not comprise the mutation(s), even in some embodiments when cultured under conditions that would otherwise cause fumonisin production in unmodified strains of the same species. Such screening also includes identification of a strain that is incapable of producing fumonisin. In some embodiments, the screening method is selected from fumonisin production assays, denaturing gradient gel electrophoresis, constant denaturing gel electrophoresis, temporal temperature gradient gel electrophoresis, single-strand conformation polymorphism, protein truncation tests, high resolution melt analyses, sequencing the one or more mycotoxin- associated genes, and combinations thereof. In some embodiments, the screening method is fumonisin production assays, sequencing the one or more mycotoxin-associated genes, or both. Optionally, the methods can further include the use of ALE to develop one or more characteristics in the strains. In some embodiments, ALE is accomplished by serially diluting a mutant strain in flasks and / or plates. In some embodiments, the characteristics are selected from higher growth rates, greater cell densities, diminished fumonisin production, and combinations thereof. In some embodiments, the present disclosure provides methods of producing a mycelial biomass from filamentous fungal strains having one or more stop codons introduced into a beauvericin synthase gene. The methods include subjecting a filamentous fungi to random mutagenesis by exposing the fungi to either a physical mutagen or a chemical mutagen for a suitable period of time and producing a mycelial biomass therefrom. In some embodiments, the physical mutagen is selected from gamma rays, X rays, UV light, fast neutrons, thermal neutrons, beta particles, alpha particles, and combinations thereof. In some embodiments, the physical mutagen is UV light. In such embodiments, the exposure occurs for a period of time selected from 30 seconds – 5 minutes, 30 seconds – 4 minutes, 30 seconds to 3 minutes, 30 seconds – 2 minutes, and 30 seconds – 1 minute. In some embodiments, the chemical mutagen is selected from ethyl methyl sulfate, nitrogen mustards, mitomycin, methyl methane sulfonate, diethyl sulfate, nitrosoguanidine, ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, acridine orange, ethidium bromide, proflavin, daunorubicin, and combinations thereof. In some embodiments, the chemical mutagen is selected from ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, and combinations thereof. In such embodiments, the chemical mutagen is utilized at a concentration of 1 mM or less, 0.9 mM or less, 0.8 mM or less, 0.7 mM or less, 0.6 mM or less, 0.5 mM or less, 0.4 mM or less, or 0.3 mM or less. Alternatively, in such embodiments the chemical mutagen is utilized in an amount of 4% w / w or less, 3% w / w or less, 2% w / w or less, 1.5% w / w or less, 1% w / w or less, 0.75% w / w or less, 0.5% w / w or less, 0.4% w / w or less, 0.3% w / w or less, 0.2% w / w or less, or 0.1% w / w or less. In such embodiments, the period of time is selected from 30 minutes – 5 hours, 30 minutes – 4 hours, 30 minutes – 3 hours, 30 minutes – 2 hours, 30 minutes – 1 hour, and 30 – 45 minutes. In certain embodiments, the period of time increases as the concentration of the chemical mutagen decreases, whereas in other embodiments the period of time is independent of the concentration or amount of the chemical mutagen. Optionally, the methods can further include screening the strains to confirm the presence of the one or more stop codons in the one or more mycotoxin-associated genes prior to producing a mycelial biomass. Such screening includes identification of a strain that produces less beauvericin than a strain of the same filamentous fungi that does not comprise the mutation(s), even in some embodiments when cultured under conditions that would otherwise cause beauvericin production in unmodified strains of the same species. Such screening also includes identification of a strain that is incapable of producing beauvericin. In some embodiments, the screening method is selected from beauvericin production assays, denaturing gradient gel electrophoresis, constant denaturing gel electrophoresis, temporal temperature gradient gel electrophoresis, single-strand conformation polymorphism, protein truncation tests, high resolution melt analyses, sequencing the one or more mycotoxin- associated genes, and combinations thereof. In some embodiments, the screening method is beauvericin production assays, sequencing the one or more mycotoxin-associated genes, or both. Optionally, the methods can further include the use of ALE to develop one or more characteristics in the strains. In some embodiments, ALE is accomplished by serially diluting a mutant strain in flasks and / or plates. In some embodiments, the characteristics are selected from higher growth rates, greater cell densities, diminished beauvericin production, and combinations thereof. In some embodiments, the present disclosure provides methods of producing filamentous fungal strains having one or more point mutations into one or more mycotoxin- associated genes, wherein each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). The methods include subjecting a filamentous fungi to random mutagenesis by exposing the fungi to either a physical mutagen or a chemical mutagen for a suitable period of time. The mycotoxin-associated genes can be any one or more of those disclosed herein. In some embodiments, the physical mutagen is selected from gamma rays, X rays, UV light, fast neutrons, thermal neutrons, beta particles, alpha particles, and combinations thereof. In some embodiments, the physical mutagen is UV light. In such embodiments, the exposure occurs for a period of time selected from 30 seconds – 5 minutes, 30 seconds – 4 minutes, 30 seconds to 3 minutes, 30 seconds – 2 minutes, and 30 seconds – 1 minute. In some embodiments, the chemical mutagen is selected from ethyl methyl sulfate, nitrogen mustards, mitomycin, methyl methane sulfonate, diethyl sulfate, nitrosoguanidine, ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, acridine orange, ethidium bromide, proflavin, daunorubicin, and combinations thereof. In some embodiments, the chemical mutagen is selected from ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, and combinations thereof. In such embodiments, the chemical mutagen is utilized at a concentration of 1 mM or less, 0.9 mM or less, 0.8 mM or less, 0.7 mM or less, 0.6 mM or less, 0.5 mM or less, 0.4 mM or less, or 0.3 mM or less. Alternatively, in such embodiments the chemical mutagen is utilized in an amount of 4% w / w or less, 3% w / w or less, 2% w / w or less, 1.5% w / w or less, 1% w / w or less, 0.75% w / w or less, 0.5% w / w or less, 0.4% w / w or less, 0.3% w / w or less, 0.2% w / w or less, or 0.1% w / w or less. In such embodiments, the period of time is selected from 30 minutes – 5 hours, 30 minutes – 4 hours, 30 minutes – 3 hours, 30 minutes – 2 hours, 30 minutes – 1 hour, and 30 – 45 minutes. In certain embodiments, the period of time increases as the concentration of the chemical mutagen decreases, whereas in other embodiments the period of time is independent of the concentration or amount of the chemical mutagen. Optionally, the methods can further include screening the strains to confirm the presence of the one or more point mutations in the one or more mycotoxin-associated genes. Such screening includes identification of a reduced, or complete lack of any, capacity to produce a mycotoxin in the strains. In some embodiments, the screening method is selected from mycotoxin production assays, denaturing gradient gel electrophoresis, constant denaturing gel electrophoresis, temporal temperature gradient gel electrophoresis, single- strand conformation polymorphism, protein truncation tests, high resolution melt analyses, sequencing the one or more mycotoxin-associated genes, and combinations thereof. In some embodiments, the screening method is mycotoxin production assays, sequencing the one or more mycotoxin-associated genes, or both. Optionally, the methods can further include the use of ALE to develop one or more characteristics in the strains. In some embodiments, ALE is accomplished by serially diluting a mutant strain in flasks and / or plates. In some embodiments, the characteristics are selected from higher growth rates, greater cell densities, diminished mycotoxin production, and combinations thereof. In some embodiments, the present disclosure provides methods of producing filamentous fungal strains having one or more one or more point mutations into one or more mycotoxin-associated genes selected from Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof, wherein each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). The methods include subjecting a filamentous fungi to random mutagenesis by exposing the fungi to either a physical mutagen or a chemical mutagen for a suitable period of time. In some embodiments, the mycotoxin-associated gene is Fum1. In some embodiments, the mycotoxin-associated gene is Fum6. In some embodiments, the mycotoxin-associated gene is Fum8. In some embodiments, the physical mutagen is selected from gamma rays, X rays, UV light, fast neutrons, thermal neutrons, beta particles, alpha particles, and combinations thereof. In some embodiments, the physical mutagen is UV light. In such embodiments, the exposure occurs for a period of time selected from 30 seconds – 5 minutes, 30 seconds – 4 minutes, 30 seconds to 3 minutes, 30 seconds – 2 minutes, and 30 seconds – 1 minute. In some embodiments, the chemical mutagen is selected from ethyl methyl sulfate, nitrogen mustards, mitomycin, methyl methane sulfonate, diethyl sulfate, nitrosoguanidine, ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, acridine orange, ethidium bromide, proflavin, daunorubicin, and combinations thereof. In some embodiments, the chemical mutagen is selected from ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, and combinations thereof. In such embodiments, the chemical mutagen is utilized at a concentration of 1 mM or less, 0.9 mM or less, 0.8 mM or less, 0.7 mM or less, 0.6 mM or less, 0.5 mM or less, 0.4 mM or less, or 0.3 mM or less. Alternatively, in such embodiments the chemical mutagen is utilized in an amount of 4% w / w or less, 3% w / w or less, 2% w / w or less, 1.5% w / w or less, 1% w / w or less, 0.75% w / w or less, 0.5% w / w or less, 0.4% w / w or less, 0.3% w / w or less, 0.2% w / w or less, or 0.1% w / w or less. In such embodiments, the period of time is selected from 30 minutes – 5 hours, 30 minutes – 4 hours, 30 minutes – 3 hours, 30 minutes – 2 hours, 30 minutes – 1 hour, and 30 – 45 minutes. In certain embodiments, the period of time increases as the concentration of the chemical mutagen decreases, whereas in other embodiments the period of time is independent of the concentration or amount of the chemical mutagen. Optionally, the methods can further include screening the strains to confirm the presence of the one or more point mutations in the one or more mycotoxin-associated genes. Such screening includes identification of a strain that produces less fumonisin than a strain of the same filamentous fungi that does not comprise the mutation(s), even in some embodiments when cultured under conditions that would otherwise cause fumonisin production in unmodified strains of the same species. Such screening also includes identification of a strain that is incapable of producing fumonisin. In some embodiments, the screening method is selected from fumonisin production assays, denaturing gradient gel electrophoresis, constant denaturing gel electrophoresis, temporal temperature gradient gel electrophoresis, single-strand conformation polymorphism, protein truncation tests, high resolution melt analyses, sequencing the one or more mycotoxin-associated genes, and combinations thereof. In some embodiments, the screening method is fumonisin production assays, sequencing the one or more mycotoxin-associated genes, or both. Optionally, the methods can further include the use of ALE to develop one or more characteristics in the strains. In some embodiments, ALE is accomplished by serially diluting a mutant strain in flasks and / or plates. In some embodiments, the characteristics are selected from higher growth rates, greater cell densities, diminished fumonisin production, and combinations thereof. In some embodiments, the present disclosure provides methods of producing filamentous fungal strains having one or more point mutations introduced into a beauvericin synthase gene, wherein each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). The methods include subjecting a filamentous fungi to random mutagenesis by exposing the fungi to either a physical mutagen or a chemical mutagen for a suitable period of time. In some embodiments, the physical mutagen is selected from gamma rays, X rays, UV light, fast neutrons, thermal neutrons, beta particles, alpha particles, and combinations thereof. In some embodiments, the physical mutagen is UV light. In such embodiments, the exposure occurs for a period of time selected from 30 seconds – 5 minutes, 30 seconds – 4 minutes, 30 seconds to 3 minutes, 30 seconds – 2 minutes, and 30 seconds – 1 minute. In some embodiments, the chemical mutagen is selected from ethyl methyl sulfate, nitrogen mustards, mitomycin, methyl methane sulfonate, diethyl sulfate, nitrosoguanidine, ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, acridine orange, ethidium bromide, proflavin, daunorubicin, and combinations thereof. In some embodiments, the chemical mutagen is selected from ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, and combinations thereof. In such embodiments, the chemical mutagen is utilized at a concentration of 1 mM or less, 0.9 mM or less, 0.8 mM or less, 0.7 mM or less, 0.6 mM or less, 0.5 mM or less, 0.4 mM or less, or 0.3 mM or less. Alternatively, in such embodiments the chemical mutagen is utilized in an amount of 4% w / w or less, 3% w / w or less, 2% w / w or less, 1.5% w / w or less, 1% w / w or less, 0.75% w / w or less, 0.5% w / w or less, 0.4% w / w or less, 0.3% w / w or less, 0.2% w / w or less, or 0.1% w / w or less. In such embodiments, the period of time is selected from 30 minutes – 5 hours, 30 minutes – 4 hours, 30 minutes – 3 hours, 30 minutes – 2 hours, 30 minutes – 1 hour, and 30 – 45 minutes. In certain embodiments, the period of time increases as the concentration of the chemical mutagen decreases, whereas in other embodiments the period of time is independent of the concentration or amount of the chemical mutagen. Optionally, the methods can further include screening the strains to confirm the presence of the one or more point mutations in the one or more mycotoxin-associated genes. Such screening includes identification of a strain that produces less beauvericin than a strain of the same filamentous fungi that does not comprise the mutation(s), even in some embodiments when cultured under conditions that would otherwise cause beauvericin production in unmodified strains of the same species. Such screening also includes identification of a strain that is incapable of producing beauvericin. In some embodiments, the screening method is selected from beauvericin production assays, denaturing gradient gel electrophoresis, constant denaturing gel electrophoresis, temporal temperature gradient gel electrophoresis, single-strand conformation polymorphism, protein truncation tests, high resolution melt analyses, sequencing the one or more mycotoxin-associated genes, and combinations thereof. In some embodiments, the screening method is beauvericin production assays, sequencing the one or more mycotoxin-associated genes, or both. Optionally, the methods can further include the use of ALE to develop one or more characteristics in the strains. In some embodiments, ALE is accomplished by serially diluting a mutant strain in flasks and / or plates. In some embodiments, the characteristics are selected from higher growth rates, greater cell densities, diminished beauvericin production, and combinations thereof. In some embodiments, the present disclosure provides methods of producing a mycelial biomass from filamentous fungal strains having one or more point mutations into one or more mycotoxin-associated genes, wherein each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). The methods include subjecting a filamentous fungi to random mutagenesis by exposing the fungi to either a physical mutagen or a chemical mutagen for a suitable period of time prior to producing a mycelial biomass. The mycotoxin-associated genes can be any one or more of those disclosed herein. In some embodiments, the physical mutagen is selected from gamma rays, X rays, UV light, fast neutrons, thermal neutrons, beta particles, alpha particles, and combinations thereof. In some embodiments, the physical mutagen is UV light. In such embodiments, the exposure occurs for a period of time selected from 30 seconds – 5 minutes, 30 seconds – 4 minutes, 30 seconds to 3 minutes, 30 seconds – 2 minutes, and 30 seconds – 1 minute. In some embodiments, the chemical mutagen is selected from ethyl methyl sulfate, nitrogen mustards, mitomycin, methyl methane sulfonate, diethyl sulfate, nitrosoguanidine, ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, acridine orange, ethidium bromide, proflavin, daunorubicin, and combinations thereof. In some embodiments, the chemical mutagen is selected from ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, and combinations thereof. In such embodiments, the chemical mutagen is utilized at a concentration of 1 mM or less, 0.9 mM or less, 0.8 mM or less, 0.7 mM or less, 0.6 mM or less, 0.5 mM or less, 0.4 mM or less, or 0.3 mM or less. Alternatively, in such embodiments the chemical mutagen is utilized in an amount of 4% w / w or less, 3% w / w or less, 2% w / w or less, 1.5% w / w or less, 1% w / w or less, 0.75% w / w or less, 0.5% w / w or less, 0.4% w / w or less, 0.3% w / w or less, 0.2% w / w or less, or 0.1% w / w or less. In such embodiments, the period of time is selected from 30 minutes – 5 hours, 30 minutes – 4 hours, 30 minutes – 3 hours, 30 minutes – 2 hours, 30 minutes – 1 hour, and 30 – 45 minutes. In certain embodiments, the period of time increases as the concentration of the chemical mutagen decreases, whereas in other embodiments the period of time is independent of the concentration or amount of the chemical mutagen. Optionally, the methods can further include screening the strains to confirm the presence of the one or more point mutations in the one or more mycotoxin-associated genes prior to producing a mycelial biomass. Such screening includes identification of a reduced, or complete lack of any, capacity to produce a mycotoxin in the strains. In some embodiments, the screening method is selected from mycotoxin production assays, denaturing gradient gel electrophoresis, constant denaturing gel electrophoresis, temporal temperature gradient gel electrophoresis, single-strand conformation polymorphism, protein truncation tests, high resolution melt analyses, sequencing the one or more mycotoxin- associated genes, and combinations thereof. In some embodiments, the screening method is mycotoxin production assays, sequencing the one or more mycotoxin-associated genes, or both. Optionally, the methods can further include the use of ALE to develop one or more characteristics in the strains prior to producing a mycelial biomass. In some embodiments, ALE is accomplished by serially diluting a mutant strain in flasks and / or plates. In some embodiments, the characteristics are selected from higher growth rates, greater cell densities, diminished mycotoxin production, and combinations thereof. In some embodiments, the present disclosure provides methods of producing a mycelial biomass from filamentous fungal strains having one or more one or more point mutations into one or more mycotoxin-associated genes selected from Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof, wherein each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). The methods include subjecting a filamentous fungi to random mutagenesis by exposing the fungi to either a physical mutagen or a chemical mutagen for a suitable period of time prior to producing a mycelial biomass. In some embodiments, the mycotoxin-associated gene is Fum1. In some embodiments, the mycotoxin-associated gene is Fum6. In some embodiments, the mycotoxin-associated gene is Fum8. In some embodiments, the physical mutagen is selected from gamma rays, X rays, UV light, fast neutrons, thermal neutrons, beta particles, alpha particles, and combinations thereof. In some embodiments, the physical mutagen is UV light. In such embodiments, the exposure occurs for a period of time selected from 30 seconds – 5 minutes, 30 seconds – 4 minutes, 30 seconds to 3 minutes, 30 seconds – 2 minutes, and 30 seconds – 1 minute. In some embodiments, the chemical mutagen is selected from ethyl methyl sulfate, nitrogen mustards, mitomycin, methyl methane sulfonate, diethyl sulfate, nitrosoguanidine, ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, acridine orange, ethidium bromide, proflavin, daunorubicin, and combinations thereof. In some embodiments, the chemical mutagen is selected from ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, and combinations thereof. In such embodiments, the chemical mutagen is utilized at a concentration of 1 mM or less, 0.9 mM or less, 0.8 mM or less, 0.7 mM or less, 0.6 mM or less, 0.5 mM or less, 0.4 mM or less, or 0.3 mM or less. Alternatively, in such embodiments the chemical mutagen is utilized in an amount of 4% w / w or less, 3% w / w or less, 2% w / w or less, 1.5% w / w or less, 1% w / w or less, 0.75% w / w or less, 0.5% w / w or less, 0.4% w / w or less, 0.3% w / w or less, 0.2% w / w or less, or 0.1% w / w or less. In such embodiments, the period of time is selected from 30 minutes – 5 hours, 30 minutes – 4 hours, 30 minutes – 3 hours, 30 minutes – 2 hours, 30 minutes – 1 hour, and 30 – 45 minutes. In certain embodiments, the period of time increases as the concentration of the chemical mutagen decreases, whereas in other embodiments the period of time is independent of the concentration or amount of the chemical mutagen. Optionally, the methods can further include screening the strains to confirm the presence of the one or more point mutations in the one or more mycotoxin-associated genes prior to producing a mycelial biomass. Such screening includes identification of a strain that produces less fumonisin than a strain of the same filamentous fungi that does not comprise the mutation(s), even in some embodiments when cultured under conditions that would otherwise cause fumonisin production in unmodified strains of the same species. Such screening also includes identification of a strain that is incapable of producing fumonisin. In some embodiments, the screening method is selected from fumonisin production assays, denaturing gradient gel electrophoresis, constant denaturing gel electrophoresis, temporal temperature gradient gel electrophoresis, single-strand conformation polymorphism, protein truncation tests, high resolution melt analyses, sequencing the one or more mycotoxin- associated genes, and combinations thereof. In some embodiments, the screening method is fumonisin production assays, sequencing the one or more mycotoxin-associated genes, or both. Optionally, the methods can further include the use of ALE to develop one or more characteristics in the strains prior to producing a mycelial biomass. In some embodiments, ALE is accomplished by serially diluting a mutant strain in flasks and / or plates. In some embodiments, the characteristics are selected from higher growth rates, greater cell densities, diminished fumonisin production, and combinations thereof. In some embodiments, the present disclosure provides methods of producing a mycelial biomass from filamentous fungal strains having one or more point mutations introduced into a beauvericin synthase gene, wherein each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). The methods include subjecting a filamentous fungi to random mutagenesis by exposing the fungi to either a physical mutagen or a chemical mutagen for a suitable period of time prior to producing a mycelial biomass. In some embodiments, the physical mutagen is selected from gamma rays, X rays, UV light, fast neutrons, thermal neutrons, beta particles, alpha particles, and combinations thereof. In some embodiments, the physical mutagen is UV light. In such embodiments, the exposure occurs for a period of time selected from 30 seconds – 5 minutes, 30 seconds – 4 minutes, 30 seconds to 3 minutes, 30 seconds – 2 minutes, and 30 seconds – 1 minute. In some embodiments, the chemical mutagen is selected from ethyl methyl sulfate, nitrogen mustards, mitomycin, methyl methane sulfonate, diethyl sulfate, nitrosoguanidine, ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, acridine orange, ethidium bromide, proflavin, daunorubicin, and combinations thereof. In some embodiments, the chemical mutagen is selected from ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, and combinations thereof. In such embodiments, the chemical mutagen is utilized at a concentration of 1 mM or less, 0.9 mM or less, 0.8 mM or less, 0.7 mM or less, 0.6 mM or less, 0.5 mM or less, 0.4 mM or less, or 0.3 mM or less. Alternatively, in such embodiments the chemical mutagen is utilized in an amount of 4% w / w or less, 3% w / w or less, 2% w / w or less, 1.5% w / w or less, 1% w / w or less, 0.75% w / w or less, 0.5% w / w or less, 0.4% w / w or less, 0.3% w / w or less, 0.2% w / w or less, or 0.1% w / w or less. In such embodiments, the period of time is selected from 30 minutes – 5 hours, 30 minutes – 4 hours, 30 minutes – 3 hours, 30 minutes – 2 hours, 30 minutes – 1 hour, and 30 – 45 minutes. In certain embodiments, the period of time increases as the concentration of the chemical mutagen decreases, whereas in other embodiments the period of time is independent of the concentration or amount of the chemical mutagen. Optionally, the methods can further include screening the strains to confirm the presence of the one or more point mutations in the one or more mycotoxin-associated genes prior to producing a mycelial biomass. Such screening includes identification of a strain that produces less beauvericin than a strain of the same filamentous fungi that does not comprise the mutation(s), even in some embodiments when cultured under conditions that would otherwise cause beauvericin production in unmodified strains of the same species. Such screening also includes identification of a strain that is incapable of producing beauvericin. In some embodiments, the screening method is selected from beauvericin production assays, denaturing gradient gel electrophoresis, constant denaturing gel electrophoresis, temporal temperature gradient gel electrophoresis, single-strand conformation polymorphism, protein truncation tests, high resolution melt analyses, sequencing the one or more mycotoxin- associated genes, and combinations thereof. In some embodiments, the screening method is beauvericin production assays, sequencing the one or more mycotoxin-associated genes, or both. Optionally, the methods can further include the use of ALE to develop one or more characteristics in the strains prior to producing a mycelial biomass. In some embodiments, ALE is accomplished by serially diluting a mutant strain in flasks and / or plates. In some embodiments, the characteristics are selected from higher growth rates, greater cell densities, diminished beauvericin production, and combinations thereof. In some embodiments, the present disclosure provides methods of producing filamentous fungal strains having one or more stop codons introduced into one or more mycotoxin-associated genes. The methods include subjecting a filamentous fungus to site- directed mutagenesis. The mycotoxin-associated genes can be any one or more of those disclosed herein. In some embodiments, the method of site-directed mutagenesis is selected from knockout mutations, oligonucleotide-directed mutagenesis, Kunkel’s method, cassette mutagenesis, PCR mutagenesis, homologous recombination, CRISPR / Cas9 mutagenesis, Delitto Perfetto, transplacement "pop-in pop-out," direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker, direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker using long homologous regions, in vivo site-directed mutagenesis with synthetic oligonucleotides, and combinations thereof. Optionally, the methods can further include screening the strains to confirm the presence of the one or more stop codons in the one or more mycotoxin-associated genes. Such screening includes identification of a reduced, or complete lack of any, capacity to produce a mycotoxin in the strains. In some embodiments, the screening method is selected from mycotoxin production assays, denaturing gradient gel electrophoresis, constant denaturing gel electrophoresis, temporal temperature gradient gel electrophoresis, single- strand conformation polymorphism, protein truncation tests, high resolution melt analyses, sequencing the one or more mycotoxin-associated genes, and combinations thereof. In some embodiments, the screening method is mycotoxin production assays, sequencing the one or more mycotoxin-associated genes, or both. Optionally, the methods can further include the use of ALE to develop one or more characteristics in the strains. In some embodiments, ALE is accomplished by serially diluting a mutant strain in flasks and / or plates. In some embodiments, the characteristics are selected from higher growth rates, greater cell densities, diminished mycotoxin production, and combinations thereof. In some embodiments, the present disclosure provides methods of producing a mycelial biomass from filamentous fungal strains having one or more stop codons introduced into one or more mycotoxin-associated genes. The methods include subjecting a filamentous fungus to site-directed mutagenesis prior to production of a mycelial biomass. The mycotoxin-associated genes can be any one or more of those disclosed herein. In some embodiments, the method of site-directed mutagenesis is selected from knockout mutations, oligonucleotide-directed mutagenesis, Kunkel’s method, cassette mutagenesis, PCR mutagenesis, homologous recombination, CRISPR / Cas9 mutagenesis, Delitto Perfetto, transplacement "pop-in pop-out," direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker, direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker using long homologous regions, in vivo site-directed mutagenesis with synthetic oligonucleotides, and combinations thereof. Optionally, the methods can further include screening the strains to confirm the presence of the one or more stop codons in the one or more mycotoxin-associated genes prior to producing a mycelial biomass. Such screening includes identification of a reduced, or complete lack of any, capacity to produce a mycotoxin in the strains. In some embodiments, the screening method is selected from mycotoxin production assays, denaturing gradient gel electrophoresis, constant denaturing gel electrophoresis, temporal temperature gradient gel electrophoresis, single-strand conformation polymorphism, protein truncation tests, high resolution melt analyses, sequencing the one or more mycotoxin- associated genes, and combinations thereof. In some embodiments, the screening method is mycotoxin production assays, sequencing the one or more mycotoxin-associated genes, or both. Optionally, the methods can further include the use of ALE to develop one or more characteristics in the strains prior to producing a mycelial biomass. In some embodiments, ALE is accomplished by serially diluting a mutant strain in flasks and / or plates. In some embodiments, the characteristics are selected from higher growth rates, greater cell densities, diminished mycotoxin production, and combinations thereof. In some embodiments, the present disclosure provides methods of producing filamentous fungal strains having one or more point mutations into one or more mycotoxin- associated genes, wherein each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). The methods include subjecting a filamentous fungi to site-directed mutagenesis. The mycotoxin- associated genes can be any one or more of those disclosed herein. In some embodiments, the method of site-directed mutagenesis is selected from knockout mutations, oligonucleotide-directed mutagenesis, Kunkel’s method, cassette mutagenesis, PCR mutagenesis, homologous recombination, CRISPR / Cas9 mutagenesis, Delitto Perfetto, transplacement "pop-in pop-out," direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker, direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker using long homologous regions, in vivo site-directed mutagenesis with synthetic oligonucleotides, and combinations thereof. Optionally, the methods can further include screening the strains to confirm the presence of the one or more point mutations in the one or more mycotoxin-associated genes. Such screening includes identification of a reduced, or complete lack of any, capacity to produce a mycotoxin in the strains. In some embodiments, the screening method is selected from mycotoxin production assays, denaturing gradient gel electrophoresis, constant denaturing gel electrophoresis, temporal temperature gradient gel electrophoresis, single- strand conformation polymorphism, protein truncation tests, high resolution melt analyses, sequencing the one or more mycotoxin-associated genes, and combinations thereof. In some embodiments, the screening method is mycotoxin production assays, sequencing the one or more mycotoxin-associated genes, or both. Optionally, the methods can further include the use of ALE to develop one or more characteristics in the strains. In some embodiments, ALE is accomplished by serially diluting a mutant strain in flasks and / or plates. In some embodiments, the characteristics are selected from higher growth rates, greater cell densities, diminished mycotoxin production, and combinations thereof. In some embodiments, the present disclosure provides methods of producing a mycelial biomass from filamentous fungal strains having one or more point mutations into one or more mycotoxin-associated genes, wherein each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). The methods include subjecting a filamentous fungi to site-directed mutagenesis prior to producing a mycelial biomass. The mycotoxin-associated genes can be any one or more of those disclosed herein. In some embodiments, the method of site-directed mutagenesis is selected from knockout mutations, oligonucleotide-directed mutagenesis, Kunkel’s method, cassette mutagenesis, PCR mutagenesis, homologous recombination, CRISPR / Cas9 mutagenesis, Delitto Perfetto, transplacement "pop-in pop-out," direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker, direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker using long homologous regions, in vivo site-directed mutagenesis with synthetic oligonucleotides, and combinations thereof. Optionally, the methods can further include screening the strains to confirm the presence of the one or more point mutations in the one or more mycotoxin-associated genes prior to producing a mycelial biomass. Such screening includes identification of a reduced, or complete lack of any, capacity to produce a mycotoxin in the strains. In some embodiments, the screening method is selected from mycotoxin production assays, denaturing gradient gel electrophoresis, constant denaturing gel electrophoresis, temporal temperature gradient gel electrophoresis, single-strand conformation polymorphism, protein truncation tests, high resolution melt analyses, sequencing the one or more mycotoxin- associated genes, and combinations thereof. In some embodiments, the screening method is mycotoxin production assays, sequencing the one or more mycotoxin-associated genes, or both. Optionally, the methods can further include the use of ALE to develop one or more characteristics in the strains prior to producing a mycelial biomass. In some embodiments, ALE is accomplished by serially diluting a mutant strain in flasks and / or plates. In some embodiments, the characteristics are selected from higher growth rates, greater cell densities, diminished mycotoxin production, and combinations thereof. In some embodiments, the present disclosure provides methods of producing filamentous fungal strains having one or more stop codons and one or more point mutations introduced into one or more mycotoxin-associated genes, wherein each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). The methods include subjecting a filamentous fungi to random mutagenesis by exposing the fungi to either a physical mutagen or a chemical mutagen for a suitable period of time and producing a mycelial biomass therefrom. The mycotoxin- associated genes can be any one or more of those disclosed herein. The methods for physical or chemical mutagenesis are as described above. In some embodiments, the present disclosure provides methods of producing filamentous fungal strains having one or more premature stop codons and one or more point mutations into one or more mycotoxin-associated genes, wherein each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). The methods include subjecting a filamentous fungi to site directed mutagenesis. The mycotoxin-associated genes can be any one or more of those disclosed herein. The methods for site directed mutagenesis are as described above. In some embodiments, the present disclosure provides methods of producing a mycelial biomass from filamentous fungal strains having one or more stop codons and one or more point mutations introduced into one or more mycotoxin-associated genes, wherein each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). The methods include subjecting a filamentous fungi to random mutagenesis by exposing the fungi to either a physical mutagen or a chemical mutagen for a suitable period of time and producing a mycelial biomass therefrom. The mycotoxin-associated genes can be any one or more of those disclosed herein. The methods for physical or chemical mutagenesis are as described above. In some embodiments, the present disclosure provides methods of producing a mycelial biomass from filamentous fungal strains having one or more premature stop codons and one or more point mutations into one or more mycotoxin-associated genes, wherein each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene(s). The methods include subjecting a filamentous fungus to site directed mutagenesis prior to producing a mycelial biomass. The mycotoxin-associated genes can be any one or more of those disclosed herein. The methods for site directed mutagenesis are as described above. In any of the foregoing embodiments, a mutated filamentous fungal strain having been identified as having desired properties via one or more of the disclosed screening processes after a first round of mutagenesis (whether random or site-directed), may be optionally subjected to one or more additional rounds of mutagenesis in order to introduce further mutations into one or more mycotoxin-associated genes. Such additional rounds of mutagenesis may be the same as the first round, or may be different. For example, if the first round of mutagenesis was random mutagenesis, an additional round may also be random mutagenesis, or may instead be site directed mutagenesis. After each additional round of mutagenesis, the resulting mutated strain may be screened for any desirable properties, for example a reduced or eliminated mycotoxin production capability. Ethanol-related methods Glucose is the preferred carbon source for most organisms, including F. flavolapis, and glucose is also advantageous for use in media for the growth of F. flavolapis because glucose is inexpensive compared to other carbon sources. However, including glucose as the carbon source in surface fermentation leads to ethanol production which inhibits growth of the fungi. Ethanol has adverse effects on cell membranes, which can change the permeability of the cell. In higher doses ethanol is toxic to cells. Because of this ethanol production, alternative carbon sources such as dextrose are often used for maximum biomat production. Filamentous fungi internalize glucose and use a glycolytic pathway to convert glucose to pyruvate. High glucose levels can cause a buildup of the intermediate glucose-6- phosphate, which can then be processed by other metabolic pathways, for example one or more pathways that cause ethanol production. For example, glucose-6-phopsphate can be processed by heterolactic fermentation, resulting in production of ethanol and lactic acid. The protein product of the rco-3 gene can be a glucose sensor and can regulate glucose uptake and / or flux through the glycolytic pathway. Introducing a loss of function and / or reduction of function mutation into rco-3 surprisingly facilitates rapid growth of fungus in the presence of glucose, even high levels of glucose, and growth of fungus in the presence of glucose, even high levels of glucose, with little or no ethanol production. Introducing a loss of function and / or reduction of function mutation into rco-3 allows for glucose metabolism during fermentation with reduced or no ethanol production, as compared to a strain with a native rco-3. Introducing a loss of function and / or reduction of function mutation into rco-3 allows for glucose metabolism in biomass growth with reduced or no ethanol production, as compared to a strain with a native rco-3. Introducing a loss of function and / or reduction of function mutation into rco-3 allows for glucose metabolism during fermentation for biomass production with reduced or no ethanol production, as compared to a strain with a native rco-3. In each instance, fermentation can include any one or more fermentation techniques, such as submerged fermentation or a non- submerged fermentation (e.g., liquid surface fermentation, membrane or mesh fermentation, solid substrate fermentation, etc.). In some embodiments, a filamentous fungus with a loss of function and / or reduction of function mutation in rco-3 exhibits reduced or no ethanol production during submerged batch fermentation using glucose as a carbon source, as compared to a strain of the same species with a native rco-3. In some embodiments, a filamentous fungus with a loss of function and / or reduction of function mutation in rco-3 exhibits reduced or no ethanol production during liquid surface fermentation, as compared to a strain of the same species with a native rco-3. In some embodiments, the present disclosure provides methods of producing filamentous fungal strains having a knockout mutation, one or more null mutations, the introduction of one or more premature stop codons, the introduction of one or more point mutations, and / or the introduction of a mutation by any other means described herein introduced into one or more ethanol-associated genes. In some embodiments, the methods include subjecting a filamentous fungi to random mutagenesis by exposing the fungi to either a physical mutagen or a chemical mutagen for a suitable period of time, as disclosed herein. The ethanol-associated genes can be any one or more of those disclosed herein. Pigment-related methods The present disclosure provides a fungal strain with a loss of function and / or reduction of function mutation in bik1 is more white in color than a strain with a native bik1. Introducing a loss of function and / or reduction of function mutation (for example knocking the gene out or introducing one or more null mutations) into bik1 allows for the production of fungal mycelial biomass that is more white in color and that produces less non-white colors. Such bik1 mutants are easier to introduce into a wide variety of food products than a biomass with color, and maintain a more visually acceptable appearance of the resulting product than a biomass with color produced from a strain with a native bik1 sequence. It is believed that bikaverin is mainly synthesized during stress, such as in conditions of nitrogen limitation, highly acidic pH, and / or in the presence of bacterial contamination. In an effort to develop fungal strains that remain white during fermentation, fungal strains that comprise loss of function and / or reduction of function mutations of bik1 can be generated and biomass grown therefrom. The pigmentation of the resulting biomass can then be analyzed for coloration. As shown herein, pink and / or purple pigmentation can occur in fungal strains with native bik1 that are grown under conditions of stress (for example nitrogen depleted and / or high pH conditions). On the other hand, strains where bik1 had been completely knocked out or otherwise rendered inactive remained white, regardless of the manner in which they were grown. It is reasonable to conclude, then, that the pink and / or purple colors observed under stressed growth conditions are caused, at least in part, by bikaverin. Likewise, it is reasonable to conclude that strains with loss of function and / or reduction of function mutations in bik1 can be used to produce white biomass. The human eye can see numerous colors but cannot reliably distinguish colors from one another repeatedly and accurately. Any one individual may perceive two slightly different colors as the same or see differences in objects of identical color, depending on angle and lighting. This creates challenges when considering color, particularly in the food industry where it is desirable for manufacturers to replicate certain desirable color standards and / or to attempt to establish color discrepancies, thereby identifying non-favorable coloration in a product. Fortunately there are methods that are capable of quantifying a color's properties within a substance (e.g., within a fungal mycelial biomass) and determining the numerical difference between such colors. The CIELAB (or CIE L*a*b*) color model is a method for reproducibly measuring and comparing all perceptible colors within a substance utilizing three color values. In this color model, numerical disparities between values represent a degree of color change that humans can perceive. The CIELAB operational assumption is that the human brain interprets retinal color inputs as differences between both light and dark (lightness) and mutually exclusive zones of opposing colors (red / green and blue / yellow). This is commonly known as the "principle of color opposition correlation" since color cannot be simultaneously red and green, or yellow and blue, to the human eye. In this color model, L* is a color value that represents lightness, having a value that ranges from 0 to 100 where 0 is pure black and 100 is pure white. The other two values are a*, which represents red-green, and b*, which represents blue-yellow, based on the opponent model of human vision, above. The a and b values are therefore chromatic, describing the color character and the type of light. The degree of “whiteness” (measured, in some embodiments, as an absence of other pigments) of a fungal biomass can therefore be reproducibly determined using the Whiteness Index Test from the CIE L*, a*, b*, where both color (D65 / 10) and opacity (Y) values for a biomass can be determined via the use of a colorimeter (e.g., a ColorFlex® Spectrocolorimeter, Hunter Associates Laboratory, Reston, VA). “L*” represents lightness (100-0), “a*” redness (+) or greenness (−), and “b*” yellowness (+) or blueness (−) of a sample on the CIE L*, a*, b* scale. In some embodiments, this scale can be used as described in ASTM E 308 Standard Practice for Computing the Colors of Objects by Using the CIE System (ASTM International, West Conshohocken, PA, USA), where the Whiteness Index is calculated by the formula (L* / b*)−a*. Using this standard, typically a value of >7.5 implies the sample looks white to the human eye based on physical observation. Taxonomy, Species, and Strains Filamentous fungal strains suitable for use in the disclosed methods, and which may have one or more genetic alterations introduced into one or more mycotoxin-associated genes, can vary. Suitable filamentous fungal strains that may be used include any filamentous fungal strains selected from the phyla or divisions of basidiomycota or ascomycota. In some embodiments, the fungus belongs to an order selected from the group consisting of Mucorales, Ustilaginales, Russulales, Agaricales, Pezizales, and Hypocreales. In some embodiments, the fungus belongs to a family selected from the group consisting of Mucoraceae, Ustilaginaceae, Hericiaceae, Polyporaceae, Grifolaceae, Lyophyllaceae, Strophariaceae, Lycoperdaceae, Agaricaceae, Pleurotaceae, Physalacriaceae, Omphalotaceae, Tuberaceae, Morchellaceae, Sparassidaceae, Nectriaceae, Bionectriaceae, and Cordycipitaceae. In some embodiments, the fungus belongs to a genus selected from the group consisting of Agaricus, Calocybe, Calvatia, Cordyceps, Disciotis, Fomes, Fusarium, Ganoderma, Grifola, Hericulum, Hypholoma, Hypsizygus, Morchella, Pholiota, Pleurotus, Polyporous, Sparassis, Stropharia, Tuber, and Ustilago. In some embodiments, the fungus is selected from the group consisting of Rhizopus oligosporus, Ustilago esculenta, Hericulum erinaceus, Polyporous squamosus, Grifola fondosa, Hypsizygus marmoreus, Hypsizygus ulmarius, Calocybe gambosa, Pholiota nameko, Calvatia gigantea, Agaricus bisporus, Stropharia rugosoannulata, Hypholoma lateritium, Pleurotus eryngii, Pleurotus ostreatus, Pleurotus ostreatus var. columbinus, Tuber borchii, Morchella esculenta, Morchella conica, Morchella importuna, Sparassis crispa, Fusarium venenatum, Fusarium strain flavolapis (ATCC Accession Deposit No. PTA-10698), Disciotis venosa, Clonostachys rosea, Cordyceps militaris, Trametes versicolor, Ganoderma lucidum, Flammulina velutipes, Lentinula edodes, Pleurotus djamor, Pleurotus ostreatus, and Leucoagaricus spp. In some embodiments, the fungus is a Fusarium species. In some embodiments the fungus is Fusarium strain flavolapis (ATCC Accession Deposit No. PTA-10698). In some embodiments, the fungus is selected from Fusarium venenatum and Fusarium venenatum strain A3 / 5 (formerly classified as Fusarium graminearum). In some embodiments, the fungus is Fusarium venenatum A3 / 5. In some embodiments, the fungus is Fusarium venenatum. In some embodiments, the fungus is selected from Pleurotus ostreatus, Agrocybe brasiliensis, Flammulina velutipes, Hypholoma capnoides, Hypholoma sublaterium, Morchella angusticeps, Macrolepiota procera, Coprinus comatus, Agaricus arvensis, Ganoderma tsugae, and lnonotus obliquus. In some embodiments, the fungus is Pleurotus ostreatus. In some embodiments, the fungus is Ganoderma lucidum. In some embodiments, the fungus is selected from a fungus belonging to the order Polyporales, a member of the family Ganodermataceae, Ganoderma lucidum, Ganoderma tsugae, Ganoderma applanatum, Ganoderma resinaceum, Ganoderma oregonense, Trametes versicolor, Trametes pubescens, Schizophyllum commune, and Polyporous squamosus. In some embodiments, the fungus is selected from a fungus belonging to Ascomycota, Zygomycota, Aspergillus, Fusarium, Neurospora, Monascus, Basidiomycota, Lentinula, and Neurospora. In some embodiments, the fungus is Neurospora crassa. In some embodiments, the fungus is selected from Agaricus arvensis; Agrocybe brasiHensis; Amylomyces rouxii; Amylomyces sp.; Armillaria mellea; Aspergillus nidulans; Aspergillus niger; Aspergillus oryzae; Ceriporia lacerata; Coprinus comatus; Fibroporia vaillantii; Fistulina hepatica; Flammulina velutipes; Fomitopsis officinalis; Ganoderma sessile; Ganoderma tsugae; Hericium erinaceus; Flypholoma capnoides; Flypholoma sublateritium; Inonotus obliguus; Lactarius chrysorrheus; Macrolepiota procera; Morchella angusticeps; Myceliophthora thermophila; Neurospora crassa; Penicillium camemberti; Penicillium chrysogenum; Penicillium rubens; Phycomyces blakesleeanus; Pleurotus djamor; Pleurotus ostreatus; Polyporus sguamosus; Psathyrella aguatica; Rhizopus microsporus; Rhizopus oryzae; Schizophyllum commune; Streptomyces venezuelae; Stropharia rugosoannulata; Thielavia terrestris; Ustilago maydis; Fusarium sp.; and Gibberella sp. In some embodiments, the fungus used includes Ganoderma sessile, Neurospora crassa, and / or Phycomyces blakesleeanus. In some embodiments, the fungus is a mutant strain of any of the above-identified fungal species. In some embodiments, the fungus is RMs2374, a Neurospora crassa mutant that can be obtained from the Fungal Genetics Stock Center (FGSC 5140). In some embodiments, the fungus is Ganoderma lucidum. In some embodiments, the fungus is selected from Aspergillus oryzae, Rhizopus oryzae, Rhizopus oligosporus and Rhizopus microspores, Fusarium graminareum, Cordyceps militaris, Cordyceps sinensis, Tuber melanosporum, Tuber magnatum, Pennicillium camemberti, Neurospora intermedia, Neurospora sitophila, Xylaria hypoxion, and Neurospora crassa. In some embodiments, the fungus is selected from brewer’s yeast (e.g., nutritional yeast, Saccharomyces cerevisiae, etc.), Brettanomyces bruxellensis, Brettanomyces anomalus, Brettanomyces custersianus, Brettanomyces naardenensis, Brettanomyces nanus, Dekkera bruxellensis, Dekkera anomala, Candida stellata, Schizosaccharomyces pombe, Torulaspora delbrueckii, Zygosaccharomyces bailii, Pichia pastoris (also called, in some cases, Komagataella phaffii, K. pastoris, or K. pseudopastoris), Agaricus bisporus, Pleurotus ostreatus, Lentinula edodes, Auricularia auricula-judae, Volvariella volvacea, Flammulina velutipes, Tremella fuciformis, Hypsizygus tessellatus, Stropharia rugosoannulata, Cyclocybe aegerita, Hericium erinaceus, Boletus edulis, Calbovista subsculpta, Calvatia gigantean, Cantharellus cibarius, Craterellus tubaeformis, Clitocybe nuda, Cortinarius caperatus, Craterellus cornucopioides, Grifola frondosa, Gyromitra esculenta, Hericium erinaceus, Hydnum repandum, Lactarius deliciosus, Morchella, Pleurotus ostreatus, Tricholoma matsutake, and Tuber sp. In some embodiments, the fungus is selected from Rasamsonia composticola, Talaromyces emersonii, Rasamsonia emersonii, Thermomucor indicae- seudaticae, Rhizomucor miehei, Rhizomucor pusillus, Thielavia terricola var minor, a Rhizopus sp., and Thermoascus thermophilus. In some embodiments, the fungus is selected from Aspergillus oryzae, Rhizopus oryzae, Fusarium graminareum, Cordyceps militaris, Cordyceps sinensis, Tuber melanosporum, Tuber magnatum, Pennicillium camemberti, Neurospora intermedia, Neurospora sitophila, and Xylaria hypoxion. In some embodiments, the fungus is Neurospora. In some embodiments, the fungus is selected from Candida etchellsii, Candida guilliermondii, Candida humilis, Candida utilis, Candida versatilis, Debaryomyces hansenii, Kluyveromyces lactis, Kluyveromyces marxianus, Kluyveromyces thermotolerans, Pichia pastoris, Rhodotorula sp., Saccharomyces bayanus, Saccharomyces beticus, Saccha- romyces cerevisiae, Saccharomyces chevalieri, Saccharomyces diastaticus, Saccharomyces ellipsoideus, Saccharomyces exiguus, Saccharomyces florentinus, Saccharomyces pastoria- nus, Saccharomyces pombe, Saccharomyces sake, Saccharomyces uvarum, Sporidiobolus johnsonii, Sporidiobolus salmonicolor, Sporobolomyces roseus, Xanthophyllomyces dendro- rhous, Yarrowia lipolytica, and Zygosaccharomyces rouxii. Sequences Mycotoxin-related Sequences In various embodiments, a mutated filamentous fungal strain provided by the present disclosure is derived from Fusarium strain flavolapis (ATCC Accession Deposit No. PTA- 10698), the complete genome of which has been sequenced and is publicly available (Nucleotide [Internet]. Bethesda (MD): National Library of Medicine (US), National Center for Biotechnology Information; (Oct 13, 2020) – Genome Assembly No. ASM1488504v1, Fusarium sp. 'flavolapis', complete contig-level genome. Available from: https: / / www.ncbi.nlm.nih.gov / datasets / genome / GCA_014885045.1 / ). In some of these embodiments, the genetic alteration comprises a mutation introduced into the Fum1 gene of F. flavolapis. SEQ ID NO:2, disclosed herein, provides the complete genomic sequence of the F. flavolapis Fum1 gene, which extends 1500 bases from either side of the coding sequence; SEQ ID NO: 1 shows the coding sequence of Fum1 in this strain. In some embodiments, the present disclosure provides a mutant strain of Fusarium strain flavolapis having one or more mutations introduced into the Fum1 mycotoxin- associated gene(s). In such embodiments, those mutations are premature stop codons and the strain displays reduced production of fumonisin as compared to a strain without the mutation(s), eliminated production of fumonisin, production of a non-functional fumonisin as compared to a strain without the mutation(s), or any combination of the foregoing. In these embodiments, the mutated Fum1 gene sequence is at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to SEQ ID NO:1. In some embodiments, the mutated Fum1 gene is at least about 70% identical to SEQ ID NO:1. In some embodiments, the mutated Fum1 gene is at least about 90% identical to SEQ ID NO:1. In some embodiments, the mutated Fum1 gene is at least about 95% identical to SEQ ID NO:1. In some embodiments, the mutated Fum1 gene is at least about 97% identical to SEQ ID NO:1. In some embodiments, the mutated Fum1 gene is at least about 99% identical to SEQ ID NO:1. In some embodiments, the present disclosure provides a mutant strain of Fusarium strain flavolapis having one or more mutations introduced into the Fum1 mycotoxin- associated gene(s). In such embodiments, those mutations are point mutations that result in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene and the strain displays reduced production of fumonisin as compared to a strain without the mutation(s), eliminated production of fumonisin, production of a non-functional fumonisin as compared to a strain without the mutation(s), or any combination of the foregoing. In these embodiments, the mutated Fum1 gene sequence is at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to SEQ ID NO:1. In some embodiments, the mutated Fum1 gene is at least about 70% identical to SEQ ID NO:1. In some embodiments, the mutated Fum1 gene is at least about 90% identical to SEQ ID NO:1. In some embodiments, the mutated Fum1 gene is at least about 95% identical to SEQ ID NO:1. In some embodiments, the mutated Fum1 gene is at least about 97% identical to SEQ ID NO:1. In some embodiments, the mutated Fum1 gene is at least about 99% identical to SEQ ID NO:1. In some embodiments, the present disclosure provides a mutant strain of Fusarium strain flavolapis having one or more mutations introduced into the Fum1 mycotoxin- associated gene(s). In such embodiments, those mutations are premature stop codons and point mutations, where the point mutations result in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene and the strain displays reduced production of fumonisin as compared to a strain without the mutation(s), eliminated production of fumonisin, production of a non-functional fumonisin as compared to a strain without the mutation(s), or any combination of the foregoing. In these embodiments, the mutated Fum1 gene sequence is at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to SEQ ID NO:1. In some embodiments, the mutated Fum1 gene is at least about 70% identical to SEQ ID NO:1. In some embodiments, the mutated Fum1 gene is at least about 90% identical to SEQ ID NO:1. In some embodiments, the mutated Fum1 gene is at least about 95% identical to SEQ ID NO:1. In some embodiments, the mutated Fum1 gene is at least about 97% identical to SEQ ID NO:1. In some embodiments, the mutated Fum1 gene is at least about 99% identical to SEQ ID NO:1. In various embodiments, a mutated filamentous fungal strain provided by the present disclosure is derived from Fusarium strain flavolapis (ATCC Accession Deposit No. PTA- 10698). In some of these embodiments, the genetic alteration comprises a mutation introduced into the beauvericin synthase gene of F. flavolapis, bea1. SEQ ID NO:6, disclosed herein, provides the complete genomic sequence of the F. flavolapis bea1 gene, which extends 1500 bases from either side of the coding sequence; SEQ ID NO: 5 shows the coding sequence of bea1 in this strain. In some embodiments, the present disclosure provides a mutant strain of Fusarium strain flavolapis having one or more mutations introduced into the bea1 mycotoxin- associated gene. In such embodiments, those mutations are premature stop codons and the strain displays reduced production of beauvericin as compared to a strain without the mutation(s), eliminated production of beauvericin, production of a non-functional beauvericin as compared to a strain without the mutation(s), or any combination of the foregoing. In these embodiments, the mutated bea1 gene sequence is at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to SEQ ID NO:5. In some embodiments, the mutated bea1 gene is at least about 70% identical to SEQ ID NO:5. In some embodiments, the mutated bea1 gene is at least about 90% identical to SEQ ID NO:5. In some embodiments, the mutated bea1 gene is at least about 95% identical to SEQ ID NO:5. In some embodiments, the mutated bea1 gene is at least about 97% identical to SEQ ID NO:5. In some embodiments, the mutated bea1 gene is at least about 99% identical to SEQ ID NO:5. In some embodiments, the F. flavolapis bea1 gene contains one or more of the premature stop codons identified in Figure 8. In some embodiments, the present disclosure provides a mutant strain of Fusarium strain flavolapis having one or more mutations introduced into the bea1 mycotoxin- associated gene. In such embodiments, those mutations are point mutations that result in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene and the strain displays reduced production of beauvericin as compared to a strain without the mutation(s), eliminated production of beauvericin, production of a non-functional beauvericin as compared to a strain without the mutation(s), or any combination of the foregoing. In these embodiments, the mutated bea1 gene sequence is at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to SEQ ID NO:5. In some embodiments, the mutated bea1 gene is at least about 70% identical to SEQ ID NO:5. In some embodiments, the mutated bea1 gene is at least about 90% identical to SEQ ID NO:5. In some embodiments, the mutated bea1 gene is at least about 95% identical to SEQ ID NO:5. In some embodiments, the mutated bea1 gene is at least about 97% identical to SEQ ID NO:5. In some embodiments, the mutated bea1 gene is at least about 99% identical to SEQ ID NO:5. In some embodiments, the present disclosure provides a mutant strain of Fusarium strain flavolapis having one or more mutations introduced into the bea1 mycotoxin- associated gene. In such embodiments, those mutations are premature stop codons and point mutations, where each point mutation independently results in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene and the strain displays reduced production of beauvericin as compared to a strain without the mutation(s), eliminated production of beauvericin, production of a non-functional beauvericin as compared to a strain without the mutation(s), or any combination of the foregoing. In these embodiments, the mutated bea1 gene sequence is at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to SEQ ID NO:5. In some embodiments, the mutated bea1 gene is at least about 70% identical to SEQ ID NO:5. In some embodiments, the mutated bea1 gene is at least about 90% identical to SEQ ID NO:5. In some embodiments, the mutated bea1 gene is at least about 95% identical to SEQ ID NO:5. In some embodiments, the mutated bea1 gene is at least about 97% identical to SEQ ID NO:5. In some embodiments, the mutated bea1 gene is at least about 99% identical to SEQ ID NO:5. In various embodiments, a mutated filamentous fungal strain provided by the present disclosure is derived from Fusarium venenatum. In some of these embodiments, the genetic alteration comprises a mutation introduced into the beauvericin synthase gene of Fusarium venenatum, bea1. SEQ ID NO:10, disclosed herein, provides the complete genomic sequence of the Fusarium venenatum bea1 gene, which extends 1500 bases from either side of the coding sequence; SEQ ID NO: 9 shows the coding sequence of bea1 in this strain. In some embodiments, the present disclosure provides a mutant strain of Fusarium venenatum having one or more mutations introduced into the bea1 mycotoxin-associated gene. In such embodiments, those mutations are premature stop codons and the strain displays reduced production of beauvericin as compared to a strain without the mutation(s), eliminated production of beauvericin, production of a non-functional beauvericin as compared to a strain without the mutation(s), or any combination of the foregoing. In these embodiments, the mutated bea1 gene sequence is at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to SEQ ID NO:9. In some embodiments, the mutated bea1 gene is at least about 70% identical to SEQ ID NO:9. In some embodiments, the mutated bea1 gene is at least about 90% identical to SEQ ID NO:9. In some embodiments, the mutated bea1 gene is at least about 95% identical to SEQ ID NO:9. In some embodiments, the mutated bea1 gene is at least about 97% identical to SEQ ID NO:9. In some embodiments, the mutated bea1 gene is at least about 99% identical to SEQ ID NO:9. In some embodiments, the present disclosure provides a mutant strain of Fusarium venenatum having one or more mutations introduced into the bea1 mycotoxin-associated gene. In such embodiments, those mutations are point mutations that result in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene and the strain displays reduced production of beauvericin as compared to a strain without the mutation(s), eliminated production of beauvericin, production of a non-functional beauvericin as compared to a strain without the mutation(s), or any combination of the foregoing. In these embodiments, the mutated bea1 gene sequence is at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to SEQ ID NO:9. In some embodiments, the mutated bea1 gene is at least about 70% identical to SEQ ID NO:9. In some embodiments, the mutated bea1 gene is at least about 90% identical to SEQ ID NO:9. In some embodiments, the mutated bea1 gene is at least about 95% identical to SEQ ID NO:9. In some embodiments, the mutated bea1 gene is at least about 97% identical to SEQ ID NO:9. In some embodiments, the mutated bea1 gene is at least about 99% identical to SEQ ID NO:9. In some embodiments, the present disclosure provides a mutant strain of Fusarium venenatum having one or more mutations introduced into the bea1 mycotoxin-associated gene. In such embodiments, those mutations are premature stop codons and point mutations, where the point mutations each independently can result in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene. The strain displays reduced production of beauvericin as compared to a strain without the mutation(s), eliminated production of beauvericin, production of a non-functional beauvericin as compared to a strain without the mutation(s), or any combination of the foregoing. In these embodiments, the mutated bea1 gene sequence is at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to SEQ ID NO:9. In some embodiments, the mutated bea1 gene is at least about 70% identical to SEQ ID NO:9. In some embodiments, the mutated bea1 gene is at least about 90% identical to SEQ ID NO:9. In some embodiments, the mutated bea1 gene is at least about 95% identical to SEQ ID NO:9. In some embodiments, the mutated bea1 gene is at least about 97% identical to SEQ ID NO:9. In some embodiments, the mutated bea1 gene is at least about 99% identical to SEQ ID NO:9. Ethanol-related Sequences In various embodiments, a mutated filamentous fungal strain provided by the present disclosure is derived from Fusarium strain flavolapis (ATCC Accession Deposit No. PTA- 10698), the complete genome of which has been sequenced and is publicly available (Nucleotide [Internet]. Bethesda (MD): National Library of Medicine (US), National Center for Biotechnology Information; (Oct 13, 2020) – Genome Assembly No. ASM1488504v1, Fusarium sp. 'flavolapis', complete contig-level genome. Available from: https: / / www.ncbi.nlm.nih.gov / datasets / genome / GCA_014885045.1 / ). In some of these embodiments, the genetic alteration comprises a mutation introduced into the rco-3 gene of F. flavolapis. SEQ ID NO:11, disclosed herein, provides the complete coding sequence of the F. flavolapis rco-3 gene. In some embodiments, the present disclosure provides a mutant strain of Fusarium strain flavolapis having one or more mutations introduced into the rco-3 ethanol-associated gene(s). In such embodiments, those mutations are premature stop codons and the strain displays reduced production of ethanol as compared to a strain without the mutation(s), eliminated production of ethanol, production of a non-functional ethanol as compared to a strain without the mutation(s), or any combination of the foregoing. In these embodiments, the mutated rco-3 gene sequence is at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to SEQ ID NO:11. In some embodiments, the mutated rco-3 gene is at least about 70% identical to SEQ ID NO:11. In some embodiments, the mutated rco-3 gene is at least about 90% identical to SEQ ID NO:11. In some embodiments, the mutated rco-3 gene is at least about 95% identical to SEQ ID NO:11. In some embodiments, the mutated rco-3 gene is at least about 97% identical to SEQ ID NO:11. In some embodiments, the mutated rco-3 gene is at least about 99% identical to SEQ ID NO:11. In some embodiments, the present disclosure provides a mutant strain of Fusarium strain flavolapis having one or more mutations introduced into the rco-3 ethanol-associated gene(s). In such embodiments, those mutations are point mutations that result in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene and the strain displays reduced production of ethanol as compared to a strain without the mutation(s), eliminated production of ethanol, production of a non-functional ethanol as compared to a strain without the mutation(s), or any combination of the foregoing. In these embodiments, the mutated rco-3 gene sequence is at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to SEQ ID NO:11. In some embodiments, the mutated rco-3 gene is at least about 70% identical to SEQ ID NO:11. In some embodiments, the mutated rco-3 gene is at least about 90% identical to SEQ ID NO:11. In some embodiments, the mutated rco-3 gene is at least about 95% identical to SEQ ID NO:11. In some embodiments, the mutated rco-3 gene is at least about 97% identical to SEQ ID NO:11. In some embodiments, the mutated rco-3 gene is at least about 99% identical to SEQ ID NO:11. In some embodiments, the mutated rco-3 gene comprises SEQ ID NO:12 or SEQ ID NO:13. In some embodiments, the mutated rco-3 gene encodes a protein comprising SEQ ID NO:14, SEQ ID NO:15, or SEQ ID NO:16. In some embodiments, the present disclosure provides a mutant strain of Fusarium strain flavolapis having one or more mutations introduced into the rco-3 ethanol-associated gene(s). In such embodiments, those mutations are premature stop codons and point mutations, where the point mutations result in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene and the strain displays reduced production of ethanol as compared to a strain without the mutation(s), eliminated production of ethanol, production of a non-functional ethanol as compared to a strain without the mutation(s), or any combination of the foregoing. In these embodiments, the mutated rco-3 gene sequence is at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to SEQ ID NO:11. In some embodiments, the mutated rco-3 gene is at least about 70% identical to SEQ ID NO:11. In some embodiments, the mutated rco-3 gene is at least about 90% identical to SEQ ID NO:11. In some embodiments, the mutated rco-3 gene is at least about 95% identical to SEQ ID NO:11. In some embodiments, the mutated rco-3 gene is at least about 97% identical to SEQ ID NO:11. In some embodiments, the mutated rco-3 gene is at least about 99% identical to SEQ ID NO:11. Pigment-related Sequences In various embodiments, a mutated filamentous fungal strain provided by the present disclosure is derived from Fusarium strain flavolapis (ATCC Accession Deposit No. PTA- 10698), the complete genome of which has been sequenced and is publicly available (Nucleotide [Internet]. Bethesda (MD): National Library of Medicine (US), National Center for Biotechnology Information; (Oct 13, 2020) – Genome Assembly No. ASM1488504v1, Fusarium sp. 'flavolapis', complete contig-level genome. Available from: https: / / www.ncbi.nlm.nih.gov / datasets / genome / GCA_014885045.1 / ). In some of these embodiments, the genetic alteration comprises a mutation introduced into the bik1 gene of F. flavolapis. SEQ ID NO:18, disclosed herein, provides the complete genomic sequence of the F. flavolapis bik1 gene. In some embodiments, the present disclosure provides a mutant strain of Fusarium strain flavolapis having one or more mutations introduced into the bik1 pigment-associated gene(s). In such embodiments, those mutations are premature stop codons and the strain displays reduced production of pigment as compared to a strain without the mutation(s), eliminated production of pigment, production of a non-functional pigment as compared to a strain without the mutation(s), or any combination of the foregoing. In these embodiments, the mutated bik1 gene sequence is at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to SEQ ID NO:18. In some embodiments, the mutated bik1 gene is at least about 70% identical to SEQ ID NO:18. In some embodiments, the mutated bik1 gene is at least about 90% identical to SEQ ID NO:18. In some embodiments, the mutated bik1 gene is at least about 95% identical to SEQ ID NO:18. In some embodiments, the mutated bik1 gene is at least about 97% identical to SEQ ID NO:18. In some embodiments, the mutated bik1 gene is at least about 99% identical to SEQ ID NO:18. In some embodiments, the present disclosure provides a mutant strain of Fusarium strain flavolapis having one or more mutations introduced into the bik1 pigment-associated gene(s). In such embodiments, those mutations are point mutations that result in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene and the strain displays reduced production of pigment as compared to a strain without the mutation(s), eliminated production of pigment, production of a non-functional pigment as compared to a strain without the mutation(s), or any combination of the foregoing. In these embodiments, the mutated bik1 gene sequence is at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to SEQ ID NO:18. In some embodiments, the mutated bik1 gene is at least about 70% identical to SEQ ID NO:18. In some embodiments, the mutated bik1 gene is at least about 90% identical to SEQ ID NO:18. In some embodiments, the mutated bik1 gene is at least about 95% identical to SEQ ID NO:18. In some embodiments, the mutated bik1 gene is at least about 97% identical to SEQ ID NO:18. In some embodiments, the mutated bik1 gene is at least about 99% identical to SEQ ID NO:18. In some embodiments, the present disclosure provides a mutant strain of Fusarium strain flavolapis having one or more mutations introduced into the bik1 pigment-associated gene(s). In such embodiments, those mutations are premature stop codons and point mutations, where the point mutations result in either a frameshift mutation, a nonsense mutation, or a missense mutation within the gene and the strain displays reduced production of pigment as compared to a strain without the mutation(s), eliminated production of pigment, production of a non-functional pigment as compared to a strain without the mutation(s), or any combination of the foregoing. In these embodiments, the mutated bik1 gene sequence is at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to SEQ ID NO:18. In some embodiments, the mutated bik1 gene is at least about 70% identical to SEQ ID NO:18. In some embodiments, the mutated bik1 gene is at least about 90% identical to SEQ ID NO:18. In some embodiments, the mutated bik1 gene is at least about 95% identical to SEQ ID NO:18. In some embodiments, the mutated bik1 gene is at least about 97% identical to SEQ ID NO:18. In some embodiments, the mutated bik1 gene is at least about 99% identical to SEQ ID NO:18. Growth of Filamentous Fugal Strains In another aspect, the present disclosure provides methods of growing the filamentous fungal strains provided by the present disclosure. Fungal fermentations can be of many kinds, and more than one method may be used to successfully grow a strain of fungus. Generally speaking, the disclosed filamentous fungal strains can be grown by any suitable method. For example, submerged fermentation, surface fermentation, submerged solid substrate fermentation, solid substrate fermentation, membrane fermentation, air- medium colloid fermentation, or combinations of any of the foregoing. In some embodiments, the filamentous fungus is inactivated after achieving a desired point of growth by rendering the fungal cells nonviable, deactivating those enzymes capable of degrading or causing biochemical transformations within the filamentous fungus, or both. Inactivation may be achieved, for example, by boiling, dehydration, immersion in an organic liquid (e.g., an alcohol, peracetic acid, etc.), irradiation, pressure treatment, rinsing, size reduction, steaming, temperature cycling, or any combination of the foregoing. In various aspects, growth of the filamentous fungal strains can be selective in that the growing method includes some manner of isolating strains containing a desired mutation. Nonselective, conventional culture media may be insufficient for accurately selecting for a filamentous fungal strain containing a desired mutation. More selective fungal culture media may yield greater success in identifying fungal strains containing a desired mutation. For example, a liquid-media alternative to the solid culture methods typically used to grow fumonisin B1-producing strains of fungi is known and has been used to successfully isolate fumonisin B1-producing fungal strains (Keller, et al., Liquid culture methods for the production of fumonisin. Adv Exp Med Biol. (1996); 392:205-12. doi: 10.1007 / 978-1-4899-1379-1_18. PMID: 8850618). Growth of the disclosed filamentous fungal strains can be accomplished via submerged fermentation, surface fermentation, submerged solid substrate fermentation, solid substrate fermentation, membrane fermentation, air-medium colloid fermentation, or combinations thereof. Depending on the type of fermentation method used, or combination of fermentation methods used, growth typically involves inoculating a solid or liquid medium containing a carbon source and a nitrogen source with filamentous fungal cells (e.g., mutated filamentous fungal cells). Suitable carbon sources are sugars (e.g., sucrose, maltose, glucose, fructose, Japan rare sugars, etc.), sugar alcohols (e.g., glycerol, polyol, etc.), starch (e.g., corn starch, etc.), starch derivative (e.g., maltodextrin, cyclodextrin, glucose syrup, hydrolysates and modified starch), starch hydrolysates, hydrogenated starch hydrolysates (HSH; e.g., hydrogenated glucose syrups, maltitol syrups, sorbitol syrups, etc.), lignocellulosic pulp or feedstock (e.g., sugar beet pulp, agricultural pulp, lumber pulp, distiller dry grains, brewery waste, etc.), corn steep liquors, acid whey, sweet whey, milk serum, wheat steep liquors, carbohydrates, food waste, olive oil processing waste, hydrolysate from lignocellulosic materials, or combinations of any of the foregoing. The filamentous fungi generate a mycelial biomass, consistent with the fermentation method(s) chosen. Suitable growth media will typically be characterized by a desired, or preselected, mass ratio of carbon to nitrogen (“C:N ratio”). The C:N ratio of growth media can be about 1:1 – about 50:1, about 2.5:1 – about 30:1, about 5:1 – about 10:1, about 2.5:1, about 5:1, about 7.5:1, about 10:1, about 12.5:1, about 15:1, about 17.5:1, about 20:1, about 22.5:1, about 25:1, about 27.5:1, about 30:1, about 32.5:1, about 35:1, about 37.5:1, about 40:1, about 42.5:1, about 45:1, about 47.5:1, about 50:1, or any ratio of the form X:2, where X is an integer between 2 and 100. Inoculation may be done with an inoculum comprising planktonic filamentous fungal cells, conidia, microconidia, macroconidia, spores, fruiting bodies, or combinations of the foregoing. In some embodiments, growth media is inoculated with an inoculum comprising planktonic filamentous fungal cells, conidia, microconidia, macroconidia, or combinations thereof. Depending on the fermentation method chosen, cells or clumps of cells of the inoculum may float on the surface of the growth media (surface fermentation), may be submerged beneath the surface of the growth media (submerged fermentation), or both. While a number of different media can be used, certain media may perform better than others for growth of the disclosed filamentous fungal strains. For growth in a non- selective media, for example, Hansen’s media (per liter = 1.0 g peptone, 0.3 g KH2PO4·7H2O, 2.0 g MgSCr·7H2O, 5.0 g glucose with a C:N ratio of 26.9) may be used as may any of the growth media disclosed in WO 2017 / 151684 and / or WO 2020 / 176758. For growth of a strain containing a mutation having a desired trait, a selective media may be employed that will selectively grow the desired mutant strain. In various embodiments, the methods of growing the disclosed filamentous fungal strains comprises inoculating an artificial growth medium with a filamentous fungal strain (e.g., a strain containing one or more mutations in one or more mycotoxin-associated genes), incubating the inoculated filamentous fungal strain to produce a mycelial biomass, consistent with the fermentation method(s) chosen, and harvesting the biomass. Optionally, the method may further include inactivating the biomass after harvest. Uses Filamentous fungal strains provided by the present disclosure are useful in the production of food products, textile products, packaging products, and building materials. Food products derived from the disclosed filamentous fungal strains have the clear advantage of reduced or eliminated mycotoxin production, and thus the reduction or elimination of the toxic effects to humans or animals eating the food products. Textile products, packaging products, and building materials derived from the disclosed filamentous fungal strains have a similar advantage in that they will not be toxic to the touch. Many textile materials, such as mycelium-based leather products and the like, are intended to be worn and extensively handled by an end user. Contact with a product that is not toxic is, thus, safer for the end user. Similarly, packaging materials, are intended to be extensively handled by an end user and may contain things such as food products. Here again, contact with a product that is not toxic is safer for the end user. Building materials derived from the disclosed filamentous fungal strains (for example, bricks) are also intended to be handled extensively by an end user. Moreover, such materials may be in the presence of multiple third parties during their lifetime, each of whom may make physical contact with the materials. Contact with a building material that is not toxic is, again, safer for the end user. Food Products Described herein are food products – including human food, animal feed (for growth and production of animals to produce meat, fish and / or dairy products), aquaculture feed, and pet food – comprising and / or derived from one or more filamentous fungal strains provided by the present disclosure. In various embodiments, a food product may be prepared from a mycelial biomass made from a disclosed filamentous fungal strain. In some embodiments, the present disclosure provides a mycelial biomass prepared from a disclosed filamentous fungal strain, where the biomass is edible. In such embodiments, the biomass is edible due to a low, or nonexistent, mycotoxin content, and / or the production of a modified mycotoxin demonstrating reduced or eliminated functionality. Such a biomass can be processed into various formats, including a liquid dispersion to form a milk analog that can used in dairy applications, a mycelial flour that can be used in baked goods in the same manner as traditional flours, particles that can be used as analogs of meat, tofu, textured vegetable protein, and similar products. In some embodiments, the biomass is formulated into a liquid dispersion, where particles of the biomass are dispersed in an aqueous medium, thereby forming a milk analog product. Suitable particle sizes are typically less than about 10 microns. The liquid dispersion is formed by blending the particles with water, optionally while heating, whereby the milk analog is formed upon cooling. The ratio of biomass to water can range from about 1:10 to about 10:1, or any range of ratios in between. The liquid dispersion can be used as a drink or beverage, including as a substitute for any milk product such as dairy milk, almond milk, rice milk, soy milk, etc. It can be used in a number of recipes including soups, ice cream, yogurt, smoothies, fudge, and candies such as caramel and truffles. In some cases, biomass produced from different fungal strains, different feedstocks, different carbon sources, and the like, can result in liquid dispersions having different flavors. For example, when the feedstock / carbon source is glycerol, the resulting liquid dispersion produced from the biomass is sweet, while a liquid dispersion resulting from biomass grown on an acid whey feedstock / carbon source will be more sour. In some embodiments, the liquid dispersion can be used to form a stable foam that does not collapse upon cessation of the foaming process. The foam is smooth and creamy in appearance and shows the presence of bubbles in a distribution of sizes. A foam product of this nature has the compositional characteristics of a liquid dispersion and additionally has air or other gas incorporated into the foam in a stable manner. Such a foam is suitable for preparing ice cream products (with more fat and emulsifiers), frozen yogurt, cheesecake batters, whipped toppings, and the like. In some embodiments, the foam may incorporate nitrogen to modify its smoothness. In some embodiments, the liquid dispersion is used to prepare a cultured food product in which a microbial food culture (i.e., live bacteria, yeasts, or molds) is introduced to a liquid dispersion. Examples of such a cultured food product include yogurt analog or other dairy analog food products (e.g., with the addition of Lactobacillus spp. or other lactic acid bacteria), baked food products or alcoholic beverage analog food products (e.g., with the addition of Saccharomyces cerevisiae or other yeasts used in brewing or baking), sausage analog food products (e.g., with the addition of Penicillium chyrsogenum, Penicillium nalgiovense, or other molds traditionally used to make sausages), soy sauce analogues (e.g., with the addition of Aspergillus oryzae or Aspergillus sojae), and so on. In some embodiments, cultured food products are produced from two or more microbial food cultures (simultaneously or sequentially) to produce products such as semi-soft ripened cheese analogs (e.g., with the first addition of Lactobacillus spp. or other lactic acid bacteria and a second addition of a cheese ripening yeast), blue cheese analog food products (e.g., with a first addition of Lactobacillus spp. or other lactic acid bacteria and a second addition of a mold such as Penicillium roqueforti), soft ripened cheese (e.g., Brie or Camembert) analogs, etc. In addition to the aforementioned drink products and cultured food products, the liquid dispersion may be used to prepare any of the following: egg analogs (e.g., scrambled egg analogs), hard cheese analogs (e.g., Parmesan), semi-hard cheese analogs (e.g., Gouda), semi-soft cheese analogs (e.g., Havarti), soft or soft ripened cheese analogs (e.g., Brie), cream cheese analogs, sour milk cheese analogs, blue cheese analogs, mascarpone cheese analogs, pasta filata analogs (e.g., Mozzarella), brined cheese analogs (e.g., Feta), whey cheese analogs (e.g., Ricotta or Brunost), fresh cheese analogs (e.g., cottage cheese), butter analogs (e.g., raw cream butter analogs, butterfat analogs, clarified butter analogs, whey butter analogs, cultured butter analogs, mild cultured butter analogs, sweet cream butter analogs, buttermilk analogs, etc.), whey analogs (e.g., sour whey analogs, sweet whey analogs, etc.), cream analogs (e.g., cuisine cream analogs, creme fraiche analogs, smetana analogs, sour cream analogs, half-and-half analogs, table cream analogs, whipping cream analogs, double cream analogs, clotted cream analogs, soured cream analogs, pasteurized cream analogs, condensed cream analogs), sour milk analogs (e.g., quark analogs, cheese curd analogs, soured milk analogs, kefir analogs, organic yogurt or mild yogurt analogs, yogurt analogs, cream yogurt analogs, cultured buttermilk analogs), milk analogs (e.g., raw milk analogs, low fat or skimmed raw milk analogs, pasteurized milk analogs, fresh whole milk analogs, low fat milk analogs, skimmed milk analogs, extended shelf-life (ESL) milk analogs, ultra-high temperature processed (UHT) milk analogs, sterilized milk analogs, condensed or evaporated milk analogs, part-skim condensed milk analogs, condensed skimmed milk analogs), powdered dairy analogs (e.g., powdered whey analogs, powdered milk analogs, powdered skimmed milk analogs), ice cream analogs, and the like. In some embodiments, the biomass is formulated into a flour, where the biomass is dehydrated and reduced in size to small, fine particles. Suitable particle sizes are typically less than about 1 microns. The flour is formed by dehydrating the biomass (e.g., via spray- drying) and size-reducing the biomass. In some embodiments, dry biomass is ground or otherwise size-reduced into relatively fine particles that resemble traditional flour, before being incorporated into a food product. In some embodiments, the flour is used in the place of some or all of traditional flour in a baked food product (i.e., bread, etc.). Biomass flour is also suitable for use as an addition / supplement to other standard flours (e.g., all-purpose flour, self-rising flour, cake flour, bread flour, pastry flour, high-protein flour, etc.). Biomass flour can be used as a substitute for about 5% - about 30% traditional flour with no deleterious effects on taste, rising, texture, appearance, or smell. Biomass flour can be used to make, for example, bread of any kind (e.g., 7 grain, white, wheat, etc.), rolls, muffins, cakes, pastries (e.g., Pate a Choux), cookies, pies, pasta, dumplings and the like. In some embodiments, the biomass is formulated into small particles, where the biomass is size-reduced in size to small particles and added to a meat product, as a suitable meat extender. Suitable particle sizes are typically less than about 10 microns. The ratio of biomass particles to meat can range from about 10:90 – about 90:10, or any ratio in between. In such embodiments, the biomass is used to increase the amount of total food product by the addition of biomass particles to other meat products (e.g., beef, pork, poultry, fish, etc.). For example, a meat product can be extended by the addition of about 10% – about 50% of biomass particles. Smaller particle sizes produce denser, creamier textures, whereas larger particles produce more texture and mouthfeel, requiring more chewing. In some embodiments, the biomass is formulated into particles that can be used as analogs of meat, tofu, textured vegetable protein, and similar products. In such embodiments, the biomass is processed to formulate an analog of a meat product, such as whole cuts of meat, bacon, ground meat (and derivative products, e.g., meatballs, meatloaves, burger patties, etc.), shredded meat, jerky, and the like. Here, biomass is size- reduced (e.g., by grinding, pulverizing, etc.) into coarse particles in which at least about 90% of the particles have a length of about 4 mm – about 10 mm, a width of about 1 mm – about 3 mm, and a height of up to about 0.75 mm, resembling ground or processed meat. From there, the biomass can be formulated into any number of meat analog food products. Additionally, analogs of a wide variety of conventional meat products (e.g., smoked meat products, meat jerky, etc.) that are meat-free, lactose-free, egg-free, soy-free, dairy- free, and / or vegan, may be produced from the disclosed biomass. In some embodiments, certain ingredients that may pose health risks to certain individuals can be replaced by the disclosed biomass. For example, red meat or other tissues that may have adverse effects on the cardiovascular health of certain individuals can be replaced by the disclosed biomass. Textiles, Packaging Materials Described herein are textiles and packaging products comprising and / or derived from one or more filamentous fungal strains provided by the present disclosure. In various embodiments, such products may be prepared from a mycelial biomass made from a disclosed filamentous fungal strain. In some embodiments, the present disclosure provides durable sheet materials, such as textiles, fabrics and leather analogs, comprising and / or derived from one or more filamentous fungal strains provided by the present disclosure. In such embodiments, the biomass is processed to impart specific visual, olfactory and tactile properties, e.g., those associated with animal leather. Such materials may be produced, for example, as described in U.S. Patent No. 11,649,586. In some embodiments, such methods include preparing a durable sheet material comprising the biomass by inactivating the biomass and size reducing it; combining the size reduced biomass with at least one component selected from a plasticizer, a polymer, a crosslinker, and a dye to form a blended composition; casting the blended composition to form a cast sheet; removing solvent from the cast sheet; and curing the cast sheet, such as by drying or heat-pressing the cast sheet, to form a durable sheet material. This method may also include adding a natural fiber material or a synthetic material to the blended composition. Alternatively, the method can be conducted without size reducing, in which case there is no need to cast the fungal biomass material. In some embodiments, the present disclosure provides packaging materials, such as containers, components of packaging containers, packing “peanuts,” and the like comprising and / or derived from one or more filamentous fungal strains provided by the present disclosure. In such embodiments, the biomass is processed to impart specific structural properties, e.g., those associated with traditional packaging materials and components. In some embodiments, such methods include preparing a packaging material comprising the biomass by inactivating the biomass and size reducing it; optionally combining the size reduced biomass with at least one component selected from a plasticizer, a polymer, a crosslinker, and a dye to form a blended composition; placing the blended composition into a mold; and curing the molded composition, such as by drying to form a durable sheet material. Alternatively, the method can be conducted by aerating the blended composition and extruding it, to form packing “peanuts.” EXAMPLES Example 1. Elimination of fumonisin and beauvericin in non-genetically modified organism (non-GMO) F. flavolapis-based strains. An approach to reduce production of the mycotoxins beauvericin and fumonisin was undertaken, without the use of genetic engineering. The approach reduces or eliminates the possibility of mycotoxin production during growth of a mutant strain and, thus, during the production of a mycelial biomass derived from such strain. The approach utilized random mutagenesis to create non-genetically modified organisms (non-GMO). The approach included: • Design of the mutagenesis procedure (e.g., exposure to a physical or chemical mutagen) • Construction of a library of mutagenized F. flavolapis fungi • Screening for changes to a fumonisin gene (a Fum gene) and / or the beauvericin synthase gene • Identification of suitable fungal strains, with a premature stop codon in a fumonisin gene and / or the beauvericin synthase gene Genetic alteration proceeded via two approaches. First, fungus of the F. flavolapis strain was treated with ethyl methanesulfonate (EMS) to induce random, non-site-directed, mutagenesis. Second, fungus of the F. flavolapis strain was treated with N-methyl-N'- nitro-N-nitrosoguanidine (NTG) to induce random, non-site-directed mutagenesis. A library of mutagenized fungi was thus constructed. The library was divided into pools, and each pool was screened by digital PCR for a premature stop codon in a fumonisin gene (a Fum gene) and / or the beauvericin synthase gene. Pools with the desired sequence present were then divided into smaller pools and screened again by digital PCR. Repeated rounds of division of positive pools and further screening by digital PCR were undertaken until single colonies were obtained with the desired sequence (e.g., a premature stop codon in a fumonisin gene (a Fum gene) and / or the beauvericin synthase gene). Example 1A. Mapping of Premature Stop Codons In developing the general approach of Example 1, gene sequences identifying all possible locations for premature stop codons in certain fumonisin and beauvericin genes were generated. A complete genomic sequence of the F. flavolapis Fum1 gene showing all possible locations for premature stop codons was produced, as was a complete genomic sequence of the F. flavolapis bea1 gene, again showing the location of all possible premature stop codons (Figure 8). Additionally, a complete genomic sequence of the F. venenatum bea1 gene showing all possible locations for premature stop codons was produced. During the screening process described in Example 1, if a mutant strain was identified containing one or more of these premature stop codons, it was isolated for further evaluation. Example 2. Analysis of F. flavolapis strain TR1. Using the procedure described in Example 1, F. flavolapis fungal strain TR1 was identified containing a premature stop codon in its beauvericin synthase gene. TR1 contained 13 single nucleotide variants in coding regions of genes, one of which resulted in a premature stop codon in the beauvericin synthase gene. The stop codon is expected to cause premature truncation of the beauvericin synthase protein and loss-of-function, reduced expression, and / or accelerated degradation of the beauvericin synthase protein. Example 3. Adaptive laboratory evolution (ALE) approach to improve growth of TR1 strain. As described in detail hereinabove, adaptive laboratory evolution (ALE) is a technique for the selection of strains with desired phenotypes by long-term culture under selective pressure, which in this Example was growth with glycerol as the carbon source and without yeast extract as a supplemental nutrient. In this Example, using ALE serial dilution, fast growing colonies were selected to isolate a new strain that is both fast- growing and highly productive. The TR1 strain was diluted into shaker flask cultures in each of two different media (described in WO 2017 / 151684 A1): MK7-1 and MK7-1 without yeast extract (YE). Cells were passaged every two to three days by transferring a passage volume from a culture in one flask to a new flask. Low passage volumes of 20 μL were used to maintain low cell densities. Cells were grown at 25° C. After culture in flasks, cells were transferred to plates for colony selection. One colony was selected from a plate with MK7-1 without yeast extract; this colony was termed AL1. AL1 was selected for further serial dilutions to isolate a fast growing and productive colony, with each dilution involving further growth on a plate for four days at 25° C. Mutant strain AL1 was selected for further analyses. Example 4. Characterization of AL1 growth. Growth of AL1 was compared to growth of parental mutant strain TR1 and native / non-mutated F. flavolapis by dilution and growth on plates. As can be seen in Figures 1 and 2, growth of AL1 was similar to, if not faster than, that of F. flavolapis, demonstrating that the adaptive laboratory evolution procedure implemented in Example 3 yielded production of the faster growing AL1 strain. Growth of AL1 was faster than that of native / non-mutated F. flavolapis at 72 hours and similar to that of native / non-mutated F. flavolapis at 96 hours. Therefore, mutant strain AL1, containing a premature stop codon in its bea1 gene, grows at least at a similar rate and at least to similar density as native / non- mutated F. flavolapis. Example 5. AL1 mycotoxin production. A comparative analysis of mycotoxin production between native / non-mutated F. flavolapis and mutant strain AL1 was performed. Samples of each of the three test strains were grown on plates under conditions that induce high levels of fumonisin and beauvericin production, and production levels of beauvericin and fumonisin were measured. Mandel and Reese medium was prepared to pH 3.3 with phosphoric acid and sterilized. Each strain was incubated in shake flasks in MK7-1 medium prior to inoculation at 5% (v / v) in 25 mL of the Mandel’s and Reese medium in sterile petri dishes. The cultures were incubated at 30°C, 90% relative humidity for 144 hours (6 days) prior to harvesting the biomass. After removal of excess liquid by blotting on a paper towel, the biomass was placed in vacuum seal bags, boiled for 5 minutes, allowed to cool, then submitted for LCMS analysis to quantify the amount of fumonisin and beauvericin present in the biomass. As shown in Table 1, in all three trials AL1 produced less than 10 ppb of beauvericin and, in one trial, produced less than 10 ppb of fumonisin. This demonstrated that non-targeted disruption of full length beauvericin synthase expression was highly effective in abolishing beauvericin production. Table 1. Mycotoxin production by strain Furthermore, genetic analyses of AL1 confirmed that the premature stop codon in beauvericin synthase present in TR1 is preserved in AL1, as are other genetic mutations introduced in Example 2. Example 6. AL1 grows faster and to higher densities than TR1. The growth rate and productivity in submerged culture, in terms of cell density, of AL1, TR1, and native / non-mutated F. flavolapis were analyzed (Figure 3). Flasks were each inoculated with one of the three strains and cultured at 25° C in a glycerol carbon source media with or without yeast extract (YE). Cell density was measured at 24, 48, 72, and 96 hours (shown as 24 hours in left column for each strain and condition to 96 hours in right column). AL1 obtained cell densities similar to native-non-mutated F. flavolapis at each time point with or without YE, and AL1 grew to higher density at each time point than TR1 with or without YE. Example 7. AL1 produces cohesive mycelial biomass of a similar yield as F. flavolapis in small scale studies. Native / non-mutated F. flavolapis, mutant parent strain TR1, and AL1 were cultured by liquid surface fermentation in parallel experiments: (i) in culture dishes with liquid media containing YE for 72 hours (Figure 4, top row), and (ii) in culture dishes with liquid media without YE for 72 hours (Figure 4, bottom row). Under both conditions, AL1 produced cohesive mycelial biomasses of similar yield to native / non-mutated F. flavolapis, and produced cohesive mycelial biomasses of higher yield than TR1 (Figure 4). Example 8. AL1 produces cohesive mycelial biomasses of a similar yield as F. flavolapis in large scale liquid surface fermentation. Cohesive mycelial biomass production by liquid surface fermentation was compared between native / non-mutated F. flavolapis and AL1 in liquid media with varying amounts of YE. Inocula were prepared by growth in parent flasks at 23° C and then at 30° C in a fermenter. Trays with the liquid media were then inoculated and cultured at 30° C at 90% relative humidity for approximately 72 hours to produce cohesive mycelial biomasses. Yield and cell density of the biomasses were then measured. AL1 and F. flavolapis produced cohesive mycelial biomasses of similar yield and density under all conditions. The biomasses also had similar appearances, as shown in Figure 5. The use of varying amounts of YE enabled testing of biomass production under conditions with reduced or no YE and showed that F. flavolapis and AL1 can tolerate growth under conditions with less YE and can do so similarly. Example 9. Production and analysis of beauvericin synthase negative strain TR4. Using the procedure described in Example 1, F. flavolapis fungal strain TR4 was identified. TR4 was determined to contain 22 single nucleotide variants in the coding regions of genes that result in codon changes, as compared to native / non-mutated F. flavolapis, including a change from tryptophan to a premature stop codon at position 1135 of bea1 and a change from tryptophan to a premature stop codon at position 953 of Fum1. The sequence analysis procedure is described below. Summary Variant analysis of strain TR4 detected 59 single nucleotide variants (SNVs) between the native / non-mutated F. flavolapis genome assembly (FSFLver0) and strain TR4. Twenty-seven of the SNVs occurred in gene coding regions. Of these 27, 22 SNVs resulted in non-synonymous codon changes. The impact of the codon changes was scored using SNAP2 and indicated that in five of the single amino acid variants (SAVs), the amino acid substitution could influence protein function. In addition, the SNV responsible for the p.Trp1135* single amino acid variant in the bea1 gene of the beauvericin biosynthetic gene cluster (BGC) and the p.Trp953* single amino acid variant in the Fum1 gene of the fumonisin BCG, both of which abolish production of the associated secondary metabolite, were confirmed. All the SAVs had identities below the identity cutoffs in the AllergenONline database v21 (February 14, 2021). Introduction Previous bioinformatic analysis of the genome of native strain F. flavolapis had identified the presence of the beauvericin biosynthetic gene cluster (BGC) and assays of some native F. flavolapis strain fermentations had shown the presence of beauvericin. A non-transgenic mutation strategy was undertaken to substitute a stop codon for a tryptophan at position 1135 in bea1, the core biosynthetic gene in the beauvericin BGC. This Example identifies the SNVs between the parental / native F. flavolapis strain and that of the mutant strain TR4, confirms the specific SNV in bea1 that would inhibit beauvericin production, and computationally attempts to determine if the TR4 genome has incurred any mutations that may negatively impact the strain. Materials and Methods 16,706,374 Illumina paired end reads (Illumina, Inc., San Diego, CA USA), with an average length of 238 bp, were generated by Mr. DNA (Shallowater, TX USA) from strain TR4. These reads were trimmed using “Trim Reads” as implemented in CLC Genomics Workbench Version 22.0.2 (Qiagen, Hilden, Germany). The trimmed reads were used to detect SNVs between native strain F. flavolapis (FSFLver0 assembly) and mutant strain TR4 using a CLC Genomics Workbench analysis workflow (Qiagen, Hilden, Germany). Functional annotations were taken from the F. flavolapis FSFLver0 genome assembly. Annotations for genes with SNVs that resulted in non-synonymous amino acid changes were supplemented with information obtained from NCBI (United States National Library of Medicine, Bethesda, MD USA). PFAM domains for bea1 were determined using InterProScan (Cambridgeshire, UK). Signal peptides were predicted using SignalP 6.0 (DTU Health Tech, Lyngby, Denmark). Discussion Trimming of the raw data resulted in over 16.4 million reads with an average after trim read length of 232 bp. Over 95% of the trimmed TR4 reads mapped to the FSFLver0 assembly. With a genome size of 45 Mb, these trimmed reads represent an 81x read coverage of the TR4 genome. The variant analysis workflow mapped the trimmed TR4 Illumina reads to the control FSFLver0 (F. flavolapis) genome assembly. Variations from the F. flavolapis genome sequence were then detected in the mapped reads and those changes reported. If the variant was in a gene, its impact on the amino acid sequence was also reported. Using this analysis strategy, 66 SNVs were detected between the two strains.27 of those SNVs occurred within gene coding sequences, resulting in 22 single amino acid variants (SAVs) in the encoded protein sequences. BLASTp and PFam analysis for the TR4 SAVs were performed. All the SAVs had protein sequences with identities greater than 98% to Fusarium protein sequences found in NCBI NR database. Query coverage was 100% in all but two SAVs, where the predicted gene models in F. flavolapis were extended compared to the models found in the NCBI NR protein database. 68% of the SAVs have highest hits to proteins in described NCNI NR database as hypothetical or uncharacterized. Many variants will have some degree of impact, under some condition, on an organism. SNAP2 is a neural network-based tool that attempts to predict the functional impact of a SAV in a protein sequence. It is primarily designed for elucidating the effects of naturally occurring genetic variation in human health and personalized medicine. Most of the variants predicted to have some bioinformatically inferred function were analyzed with SNAP2. SNAP2 calculated that changes in five of the SAVs would have an effect: 1. FSFL_12262:p.Gly160Asp, the Importin beta subunit, which mediates the transport between the nucleus and cytoplasm of macromolecules that contain nuclear import or export signals, 2. FSFL_03862:p.Pro177Ser, 3-hydroxyacyl-CoA dehydrogenase an enzyme that metabolizes medium-chain fatty acids and short-chain fatty acids, 3. FSFL_12971:p.Gln397His, a protein with predicted transmembrane domains, 4. FSFL_00465:p.Arg307Lys, a protein containing a RING (Really Interesting New Gene) finger domain, which plays a key role in the ubiquitination pathway that targets proteins for degradation, 5. FSFL_13023:p.Pro346Leu, annotated as a Heterokaryon incompatibility protein (HET), which has been proposed to represent a vegetative self / non- self recognition system preventing heterokaryon formation between unlike individuals to limit horizontal transfer of cytoplasmic infectious elements. Bea1 is an essential gene in the production of beauvericin. Variant analysis confirmed the presence and position of a SNV in the bea1 gene. This SNV resulted in a tryptophan to stop amino acid substitution at position 1135. The BEA1 protein in TR4 (SEQ ID NO: 8) is truncated at the second condensation domain and lacks most of the essential functional domains needed to produce beauvericin. For comparative basis, SEQ ID NO: 7 shows the native protein sequence produced by the bea1 gene from F. flavolapis. The 22 SAVs of TR4 were run against the AllergenOnline (http: / / www.allergenonline.org / databasefasta.shtml) to determine if any SAVs were potential allergens. Using a limit of >35% sequence identity over more than 80 amino acids, none of the SAVs were found in the AllergenONline database v21 (February 14, 2021). Example 10. TR4 does not produce beauvericin under mycotoxin inducing conditions and grows similarly to F. flavolapis. Production of beauvericin and fumonisin was analyzed under growth conditions that would induce production of beauvericin and fumonisin. As expected, native / non- mutated F. flavolapis produced both beauvericin and fumonisin. TR4 produced fumonisin but did not produce detectable beauvericin, as shown in Table 2: Table 2. Mycotoxin Production TR4 also has similar advantageous growth characteristics as native F. flavolapis. TR4 cultures grown on glycerol plates produced colonies of similar size to native F. flavolapis, and larger than those of TR1, when grown at 25, 27, or 30 degrees C (Figure 6). TR4 also produced similar cell densities as native F. flavolapis when grown in a shaker flask or a fermenter, and TR4 also produced cohesive mycelial biomasses of similar yield as native F. flavolapis (Figures 7A, 7B, 7C). Results are summarized in Table 3: Table 3. Example 11. Production and analysis of beauvericin synthase negative and fumonisin synthase negative strain TR5. Another strain that is deficient in production of both beauvericin synthase and fumonisin synthase was produced as described in Example 1, except that TR4 was used as the parental strain instead of native F. flavolapis, and the genome of the resulting mutant strain was analyzed as described in Example 9. This newly identified mutant strain, TR5, contains 53 nonsynonymous changes in coding regions of genes, relative to strain TR4, including a change from tryptophan to a stop codon at Fum 1 position 953. This strain was subjected to further testing (see, e.g., Example 12). Example 12. TR5 produces cohesive mycelial biomasses of a similar yield as F. flavolapis in large scale liquid surface fermentation. Cohesive mycelial biomass production by liquid surface fermentation was compared between native / non-mutated F. flavolapis and TR5 in liquid. Inocula were prepared by growth in parent shake flasks at 23° C and then at 30° C in a fermenter. Trays with the liquid media were then inoculated and cultured at 30° C at 90% relative humidity for approximately 72 hours to produce cohesive mycelial biomasses. TR5 reached similar cell densities in each state of the fermentation (shake flask fermentations and fermenters) and similar yields in the liquid surface fermentation (Table 4). In all cases the differences were not statistically significant, as indicated by the Student’s t-test (p>0.05, Table 4). Table 4. *Student’s t-test comparing F. flavolapis and TR5. Example 13. TR5 does not produce beauvericin or fumonisin under induction conditions. A comparative analysis of mycotoxin production between native / non-mutated F. flavolapis and mutant strain TR5 Strains were grown under conditions that induce high levels of fumonisin and beauvericin production as follows. Mandel’s and Reese medium was prepared to pH 3.3 with phosphoric acid and sterilized. Each strain was incubated in shake flasks in MK7-1 medium prior to inoculation at 5% (v / v) in 25 mL of the Mandel’s and Reese medium in sterile petri dishes. The cultures were incubated at 30°C, 90% relative humidity for 144 hours (6 days) prior to harvesting the biomass. After removal of excess liquid by blotting on a paper towel, the biomass was placed in vacuum seal bags, boiled for 5 minutes, allowed to cool, then submitted for LCMS analysis to quantify the amount of fumonisin and beauvericin present in the biomass. As shown in Table 5, the parent F. flavolapis strain produced beauvericin and fumonisin under induction conditions. As expected, TR5 does not produce beauvericin or fumonisin (both <10 ppb, Table 5), consistent with complete loss of function of both beauvericin synthase and the polyketide synthase encoded by Fum1. Table 5. Example 14. Production and analysis of a Fum 1 negative mutant strain. Using the procedure described in Example 1, a novel mutant strain derived from native F. flavolapis is identified. This strain is determined to contain one or more single nucleotide variants in the coding region of the Fum 1 gene as compared to native / non- mutated F. flavolapis. A sequence analysis procedure is performed consistent with that shown in Example 9. Bioinformatic analysis of the genome of native strain F. flavolapis identifies the presence of the Fum 1 gene cluster and assays of native F. flavolapis strain fermentations show the presence of fumonisin. A non-transgenic mutation strategy is undertaken to introduce one or more stop codons into the Fum 1 gene of this novel mutant strain. This Example identifies the SNVs between the parental / native F. flavolapis strain and that of the novel mutant strain, confirms the specific SNV in Fum 1 that would inhibit fumonisin production, and computationally attempts to determine if the genome of this novel mutant strain has incurred any mutations that may negatively impact the strain. Fum 1 is an essential gene in the production of fumonisin. Variant analysis confirms the presence and position of one or more SNVs in the Fum 1 gene that result in one or more stop amino acid substitutions in such gene. The fumonisin protein in this novel mutant strain (SEQ ID NO: 4) is truncated and lacks one or more essential features needed to produce fumonisin. For comparative basis, SEQ ID NO: 3 shows the native fumonisin protein sequence produced from native F. flavolapis. Example 15. Generation and identification rco-3 mutants RD6 and RD7 This Example describes the production of rco-3 mutants by ultraviolet light (UV)- induced mutagenesis in F. flavolapis. Briefly, cells were treated with UV light to induce mutagenesis, and resulting strains capable of growth using glucose as a carbon source were isolated. Conidia were purified from 10 mL of a 48 hour glycerol shake-flask culture of TR5 using a cell strainer, which retains hyphal fragments and conidiophores and allows conidia to pass through. The conidia were counted using a hemocytometer, indicating a concentration of 3.97 x 107conidia per mL. This was diluted 1:10 four times for a final concentration of about 400 conidia in 100 uL (80,000 conidia in 20 mL). 20 mL was transferred to a sterile petri dish. The petri dish was placed for mutagenesis in NUAIRE Class II Type A2 biosafety cabinet that produced UV light, 95% of which is 253.7 nm region, at an intensity of 100 mW per cm2. The petri dish was exposed to the UV light and sampled from during UV exposure at the following time points: 0 min, 0.5 min, 1 min, 1.5 min, 2 min, 2.5 min, 3 min, and 3.5 min. At each time point of UV exposure, 800 uL was retrieved from the petri dish.100 uL of the 800 uL retrieved at each time point was spread on a YPD plate (e.g., Teknova, catalog number Y1000) , plates without glycerol supplemented with 5% glucose (5% glucose plates), and plates without glycerol supplemented with 10% glucose (10% glucose plates). YPD, which contains dextrose as a carbon source was used as a control, and plates with glucose as a carbon source were used to identify cells capable of growing using glucose as a carbon source. The plates were wrapped in foil and incubated at 25° C. The plates were analyzed 48 hours after UV exposure. Cells on YPD plates grew after exposure to UV light, regardless of the duration of UV exposure. Possible filaments were observed on the 5% glucose plates from the unexposed sample, i.e., the sample exposed to UV light for 0 minutes. No other growth was observed at 48 hours on plates containing glucose. At 5 days after UV exposure, colonies were observed on both YPD and glucose-containing plates. Three fast growing colonies, shown in Figure 9A, were selected. These selected 3 colonies of interest were: • RD6: also referred to as UV1. RD6 is a colony that was exposed to UV light for 1.5 minutes and was grown on 5% glucose plates. • UV2: UV2 was grown on 5% glucose plates, after exposure to UV for 2.5 min. • RD7: also referred to as UV3. RD7 is a colony that was exposed to UV light for 2 minutes and was grown on 10% glucose plates . To purify colonies of interest, three rounds of purification were performed. First, the three colonies of interest were picked and expanded to produce conidia in 125 mL shaker flasks in 50 mL of its respective shake flask medium: RD6 and UV2 in MK7-1 with 5% glucose, and RD7 in MK7-1 with 10% glucose. Flasks were incubated at 23° C, with shaking at 160 RPM for 2 days. Next, 5 mL from each shake-flask was pipetted into a cell strainer to purify conidia. Flasks were examined, and no contamination was observed. Conidia were counted, and dilutions were made to reach 15-30 cells in 100 uL for each of strains RD6, UV2, and RD7. These conidia suspensions containing RD6, UV2, or RD7 were used to spread conidia on nine plates: three RD6 samples were spread on 5% glucose, three UV2 samples were spread on 5% glucose, and three RD7 samples were spread on 10% glucose agar plates. Plates were then incubated at 25° C. To do a second round of purification, three single colonies (one each of RD6, UV2, and RD7, noted by arrows in Figure 9B) were picked from plates produced from the first round of purification. RD6 and UV2 grew on 5% glucose plates and RD7 grew on 10% glucose plates. Each plate was incubated for four days at 25° C, which resulted in the colonies shown in Figure 9B. The three colonies noted by arrows in Figure 19B were picked, and each colony was placed into a shake flask containing 50 mL of its respective medium (RD6 in MK7-1 with 5% glucose, UV2 in MK7-1 with 5% glucose, and RD7 in MK7-1 with 10% glucose). Shake flasks were incubated at 23° C, with shaking at160 RPM for 2 days. During the third round of purification, conidia were purified from the shake-flasks, spread onto glucose NF agar plates (RD6 in MK7-1 with 5% glucose, UV2 in MK7-1 with 5% glucose, and RD7 in MK7-1 with 10% glucose), and incubated for 4 days at 25° C. Figure 9C shows plates after four days of incubation, from which purified RD6 and purified RD7 colonies were picked. UV2 demonstrated consistently slower growth on glucose media compared to RD6 and RD7 and thus was not used in the subsequent analyses discussed below. The genomes of RD6 and RD7 were analyzed, and a single nucleotide variant was identified in each of RD6 and RD7 in the rco-3 gene, as indicated in Table 6. Table 6. SNVs detected in FSFL_05357 between strain TR5 and strain RD6 or strain RD7. (TC O: 14) (TC O: 14) Example 16. Generation and identification rco-3 knock-out mutants This Example describes the production of rco-3 mutants by homologous recombination in F. flavolapis. Briefly, cells were treated to induce homologous recombination to knock out the rco-3 gene, and resulting strains capable of growth using glucose as a carbon source were isolated. A homologous recombination-mediated gene knockout approach was taken to knock-out the rco-3 gene from the TR5 genome. This involved exchanging DNA segments between two similar strands of DNA. The aim was to replace the complete rco-3 gene with a hygromycin phosphotransferase gene (hph) that confers resistance to antibiotic hygromycin B, to facilitate selection and screening of produced strains. To generate rco-3 knockout strains, the NEBuilder® HiFi DNA Assembly Cloning Kit (New England Biolabs) was used, and the primers were designed using NEBuilder® Assembly Tool. Three fragments were assembled into the construct used to knock out rco-3 from the TR5 genome (as shown in Figure 10): 1. rco-3-LHA: rco-3 left homology arm (LHA) or 5’-flanking sequence of native TR5 rco-3 (1000 bp) 2. rco-3-RHA: rco-3 right homology arm (RHA) or 3’-flanking sequence of native TR5 rco-3 (1000 bp) 3. HygR cassette (hygromycin resistance)- hygromycin phosphotransferase gene (hph), which encodes hygromycin B resistance, driven under Aspergillus niger glucoamylase promoter and trpC terminator of Aspergillus nidulans. The HygR cassette was flanked by rco-3-LHA on the 5’ end and rco-3-RHA on the 3’ end. Figure 10 shows The DNA amplicon for rco-3 KO, which contained rco-3-LHA, Aspergillus niger glucoamylase (glaA) promoter, hph, trpC terminator of Aspergillus nidulans, and rco-3-RHA. PEG-CaCl2-mediated transformation was used to introduce the construct into cells, followed by selection on media containing hygromycin. See, e.g., Li, D., Tang, Y., Lin, J. et al. Methods for genetic transformation of filamentous fungi. Microb Cell Fact 16, 168 (2017). Colonies representing potential transformants were screened genetically by sequencing the region surrounding and including the rco-3 gene, to select the true positive transformants, henceforth called the rco-3-knockout mutants (referred to herein as rco3KO). In total three rco3KO mutants were obtained, and named as rco3KO#1, rco3KO#2, and rco3KO#3 respectively. Example 17. rco3KO, RD6 and TR5 growth on Agar Plates Conidia stock vials of rco3KO, RD6 and TR5 were thawed from a -80° C freezer and run through a cell strainer to isolate conidia. Conidia was counted using a hemocytometer. First, dilutions were made to reach about 20-30 conidia per 100 uL. Each strain was plated in duplicate on YPD, PDA (e.g., Teknova, catalog number P0047), and 10% glucose plates. One plate of each treatment was incubated at 25° C and the other at 30° C. Figure 11A shows that rco3KO strain and RD6 strain grew identically to TR5 on YPD and PDA media and outgrew TR5 on 10% glucose plates, when cultivated at 25° C. The rco3KO also outgrew RD6 on glucose plates at 30° C (data not shown). Next, isolated conidia from the conidia stock vials was diluted to reach 100 conidia / 10 uL and 10 conidia / 10 uL. Each strain was plated (with 100 conidia or 10 conidia) on different glucose concentration plates: 0.25%, 5% and 20%. A dot was marked on the back of the plates and 10 uL was pipetted onto the dot. Plates were left to dry in the hood for about 15-20 minutes prior to wrapping in electrical tape. Plates were incubated at 25° C and the radius of each growing colony was measured at day 4, 5 and 6 using a caliper. Figure 11B shows the observed colony radii at each time point. These results demonstrate that colony growth was identical between rco3KO and RD6 strains on different glucose concentrations, while cultivated at 25° C and significantly different from TR5 colony growth on glucose. Figure 11A shows colonies at 96 hours, when cultivated at 25° C. Strains rco3KO, RD6 and TR5 were grown on YPD, PDA and 10% glucose plates. Figure 11B shows the growth of rco3KO, RD6 and TR5 colonies that started from 100 conidia. The size of each colony was expressed as colony radius. Example 18. rco-3 effect on utilization of glucose as carbon source in surface fermentation This Example describes the effects of rco-3 knockout on the use of glucose as a carbon source. (A) RD6 & RD7 To show the RD6 and RD7 capability to utilize glucose as a carbon source in batch surface fermentation for biomats, multiple experiments of varying scale were performed. i. RD6 and RD7 biomat formation in Petri dishes 75 mL of MK7-1 glucose media was added to 125 mL autoclaved baffled shake flasks and inoculated with 10% (75 uL) of TR5, RD6, or RD7. Flasks were incubated at 23° C, with shaking at 160 RPM for 48 hours. 25 mL of R2 (e.g., Teknova, catalog number R0005) with 5% glucose was poured into each of six petri dishes and 25 mL of R2 with 10% glucose was poured into each of six petri dishes. Each of TR5, RD6, or RD7 were inoculated into the petri dishes, in duplicate, by adding 5% (1.25 mL) of inoculum from a shake flask. The plates were incubated at 30° C with 90% relative humidity (RH). After 48 hours, the petri dishes were harvested by squeezing the mats dry and placing the mats in a drying oven. Carbohydrates and organic acids in the media samples at 48 hours were analyzed using high performance liquid chromatography (HPLC). RD6 and RD7 strains grew on high glucose concentrations at higher yield than TR5 and produced less ethanol than TR5, as demonstrated by the data shown in Figure 12A. Figure 12A shows recalculated yields in initial Petri dish surface fermentation experiment. ‘5% glc’ indicates 5% glucose concentration in R2 medium in Petri dishes. ‘10% glc’ indicates 10% glucose concentration in R2 medium in Petri dishes. Table 7 shows glucose consumption and key byproduct production (on the right) in initial Petri dish surface fermentation experiment. Table 7. Byproduct production in Petri dish surface fermentation. ii. RD6 and RD7 biomat formation in Glass Trays 125mL shake flasks were each filled with 75 mL of MK7-1 with 10% glucose shake flask medium. Each shake flask was inoculated with 10% (75 uL) TR5 conidia stock, 10% RD6 conidia stock, or 10% RD7 conidia stock. The flasks were incubated at 23° C, with shaking at 160 RPM for 48 hours. 140 g of R2 media with 10% glucose, 12.5% glucose, 15% glucose, and 20% glucose was poured into autoclaved glass trays. Each tray was inoculated with 7 mL of inoculum from 48-hour TR5, RD6, or RD7 shake flasks and incubated at 30° C, 90% relative RH. After 48 hours, biomats were harvested. Mats were hand squeezed and placed in a drying oven. No post processing was performed. Figure 12B shows photographs of mats prior to harvesting from glass trays, and the data in Figure 12C show the yield of TR5, RD6, and RD7 mats from Figure 12B grown in varying concentrations of glucose. iii. RD6 and RD7 biomat formation in Blue Trays RD6 and RD7 strains were used in a scaled-up surface fermentation process in Blue trays. For inoculum,1.5L MK7-1 glucose shake flasks were prepared as described above, and 1.5 mL of conidia stock from each strain, RD6 and RD7, was used to inoculate these shake-flasks. Flasks were incubated at 23° C, with shaking at 160 RPM for 48h prior to Blue Tray pour. Multiple Blue Tray experiments were performed to demonstrate that RD6 and RD7 can form high yielding biomats in high glucose batch surface fermentations. Data from at least two or three true replicate were used to create the following reported data and plots. Figures 13A-13D demonstrate that both strains RD6 and RD7 form high yield biomats in high glucose media. Specifically, Figures 13A-13D show RD6 and RD7 growth in high glucose batch surface fermentation conditions. In Figure 13A, the x-axis indicates cultivation time in hours (h), media volume in Liters (L), and glucose concentration (%) in R2 media at the start of the culture. Yields were re-calculated per wet gram basis after biomats were harvested, washed in boiling water, and pressed in a hydraulic press. Figure 13B shows total protein detected in RD6 and RD7 biomats per dry biomat basis. The x-axis indicates cultivation time in hours (h), media volume in Liters (L), and glucose concentration (%) in R2 media at the start of the culture. In Figure 13C, the x-axis indicates cultivation time in hours (h), media volume in Liters (L), and glucose concentration (%) in R2 media at the start of the culture. Dry biomass numbers after biomats were harvested, washed in boiling water, and pressed in a hydraulic press were used to calculate Biomass / glucose (g / g) conversion. In Figure 13D, yields from Figure 13A and glucose conversion efficiency from Figure 13C were plotted against each other for each respective growth condition to visualize their co-dependency. Figure 13A shows biomat yields obtained at varying cultivation times, media volumes and glucose concentrations in R2 media. Yields were re-calculated per wet gram basis after biomats were harvested, washed in boiling water, and pressed in a hydraulic press. Figure 13B shows total protein detected in RD6 and RD7 biomats per dry biomat basis at varying cultivation times, media volumes and glucose concentrations. Figure 13C shows dry biomass mass (after biomats were harvested, washed in boiling water, and pressed in a hydraulic press) per mass of glucose at varying cultivation times, media volumes and glucose concentrations, indicating the efficiency of glucose conversion to biomass. Figure 13D shows a plot of yields (from Figure 13A) against glucose conversion efficiency (from Figure 13C), demonstrating their co-dependency. Blue dots indicate RD6 samples, and red dots indicate RD7 samples. The data shown in Figure 13A demonstrate that biomat yields of more than 1.0 kg / m2can be reached in 72 hours, as observed with sufficient glucose (20% glucose instead of 12.5% glucose), growth time (72 hours instead of 48 hours), and media volume (2.5L instead of 2L). Yields of even 1.2 wet kg / m2for RD6 were attained with 20% of glucose, 2.5L of media, and 72 hours of mat growth. RD7 data was available only for the 2L, 12.5% 48h and 72h conditions. As shown in Figure 13B, a protein content of about 55% was attained at 48 hours of growth and of about 48% at 72 hours of growth, and protein amount per biomat (dry basis) was independent of the amount of media or glucose supplied. Glucose conversion to biomass efficiency was highest at 48 hours and was equal to 0.25 (g / g). The data presented is from biomats after harvesting, washing in boiling water, and pressing in a hydraulic press. The data shown in Figure 13D also demonstrated that overall biomat production process efficiency was highest at 48 hours. The rate of RD6 growth at various times and in different glucose concentrations was determined (Figure 14). This study included three independent Blue Tray experiments.2.5L of media was used per tray, and biomats were grown in controlled 30° C & 90% RH environment. Biomats were harvested at 48, 60, or 72 hours. Results showed that raising glucose concentration in the media from 12.5% to 15%, 17.5%, or 20% caused increasing biomat yields (Figure 14A), even of 1.2 wet kg / m2at 20% of glucose at 72 hours. The data shown in Figures 14A and 14B demonstrate that biomass production rates were highest in the time period between 48h and 60h. Productivity of 34.4 wet g / m2 / hour during time period of 48 to 60 hours was attained with 20% glucose. Specifically, Figures 14A and 14B show RD6 growth is dependent on amount of glucose provided, concentration of glucose in the media and time of biomat growth. Figure 14A shows yields that were re-calculated per wet gram basis after biomats were harvested, washed in boiling water, and pressed in a hydraulic press. 12.5%, 15%, 17.5% and 20% stands for % of glucose in R2 media used. In Figure 14B, yield rates, i.e., yield produced per hour in certain time periods: 1) first 48h of the culture, 2) 48h to 60h hour of the culture, or 3) 60h to 72h of the culture were calculated. 12.5%, 15%, 17.5% and 20% note the concentration of glucose in R2 media used. RD6 biomats grown at different glucose concentrations and harvested at 72 hours were subjected to macro-compositional analysis (performed by Eurofins) (Figure 15A and 15B). Macro-composition was calculated per dry weight. The plot in Figure 15A is made from all measured macro-compounds: total protein, total fat, total ash and total fiber. Since total fiber measurement is not total carbohydrate measurement, total macro-composition does not add up to 100%. In the plot in Figure 15B, carbohydrate value is calculated by subtracting the total fat, total protein, and total ash to provide the calculated carbohydrate value. Initial sensory analysis was also performed with RD6 glucose biomats grown in Blue Trays and compared to control F. flavolapis biomat sensory data. Spectrum with Hedonic sensory method and other physico-chemical analyses were performed. No significant differences were found between control (F. flavolapis) and RD6 samples, but, in general, RD6 glucose samples were lower in overall aromatics such as earthy / fungal / musty, rancidity and sulfuric / rotten notes. RD6 grown with glucose tasted more sour than control. RD6 samples were at slightly lower pH and had higher total acidity, which might cause the observed higher sourness. Most of RD6 milk samples were low in bitterness. RD6 glucose milk samples were darker and more tannish in color than F. flavolapis milk samples. (B) rco-3 knock-out (rco3KO) mutants Small-scale surface-fermentation experiments were carried out in square petri plates without lids and deep-well troughs without lids. Figure 16A depicts the rco3KO Small-scale Surface Fermentation Experiment Design, testing all rco3KO mutant strains for surface fermentation growth in 10% glucose. Three technical replicates were used in this experiment and all showed growth on 10% glucose. Biomats were harvested, including inactivation by boiling. Wet and dry weights were determined, and HPLC analysis was performed. Figure 16B shows the yield of each strain after harvesting biomats from petri plates or deep-well troughs. Columns from left to right for each of petri plates and deep well troughs indicate RD6, rco3KO#1, rco3KO#2, and rco3KO#3. Both petri plates and troughs produced higher yield of all three rco3KO mutants in comparison to RD6. Figure 16C shows photographs of the biomats produced by each of RD6, rco3KO#1, rco3KO#2, and rco3KO#3. Example 19. rco-3 effect on utilization of glucose as carbon source in submerged batch fermentation F. flavolapis, RD6, and RD7 were evaluated by a scaled-down 3-stage batch submerged fermentation process to evaluate differences in strain performance. As shown in Figure 17A, depicting measured cell density from seed fermenter routine sampling, F. flavolapis cell density was significantly negatively impacted by batch fermentation, depicted by a linear growth rate of in production stages and accumulation of ethanol and organic acids in fermentation broth. Also as shown in Figure 17A, RD6 and RD7 both show improved growth performance, depicted by an exponential growth rate under the same conditions, and RD6 produced significantly less ethanol and organic acids than both RD7 and F. flavolapis at equivalent titers. Experimental Methods: Shake Flask Growth 1L of MK7-1 shake flask media was aliquoted into 2L baffled Erlenmeyer flasks and sterilized by au...

Claims

CLAIMS 1. A filamentous fungal strain, comprising one or more reduced function mutations in one or more mycotoxin-associated genes.

2. The filamentous fungal strain of claim 1, wherein the one or more mutations comprise at least one loss of function mutation.

3. The filamentous fungal strain of claim 1 or claim 2, wherein the one or more mutations are selected from the group consisting of one or more knockout mutations, one or more introduced premature stop codons, one or more introduced point mutations, and combinations thereof.

4. The filamentous fungal strain of claim 3, wherein each point mutation independently produces a frameshift mutation, a nonsense mutation, or a missense mutation.

5. The filamentous fungal strain of any one of claims 1-4, wherein the mycotoxin is selected from the group consisting of aflatoxins, beauvericin, fusarins, citrinin, ochratoxins, trichothecenes, zearalenone, fumonisins, mycophenolic acid, penicillic acid, patulin, cyclopiazonic acid, ergot alkaloids, cyclopiazonic acid, gliotoxin, sterigmatocystin, and combinations thereof.

6. The filamentous fungal strain of any one of claims 1 – 5, wherein production of a mycotoxin in the strain is reduced as compared to a filamentous fungal strain of the same species without the one or more mutations in one or more mycotoxin-associated genes when grown under the same conditions.

7. The filamentous fungal strain of any one of claims 1-6, wherein the mycotoxin is beauvericin or a fumonisin.

8. The filamentous fungal strain of any one of claims 1-6, wherein the mycotoxin is beauvericin and the mycotoxin-associated gene is beauvericin synthase.

9. The filamentous fungal strain of claim 8, wherein the filamentous fungal strain is incapable of producing beauvericin.

10. The filamentous fungal strain of claim 8, wherein the filamentous fungal strain produces less beauvericin than a strain of the same filamentous fungi without the one or more mutations.

11. The filamentous fungal strain of claim 8, wherein the filamentous fungal strain produces a modified beauvericin demonstrating reduced or eliminated functionality, or both, as compared to a strain of the same filamentous fungi without the one or more mutations.

12. The filamentous fungal strain of any one of claims 1-6, wherein the mycotoxin is a fumonisin and the mycotoxin-associated gene is selected from the group consisting of Fum1, Fum2, Fum3, Fum6, Fum7, Fum8, Fum10, Fum11, Fum13, Fum14, Fum15, Fum16, Fum17, Fum18, Fum19, Fum20, Fum21, and combinations thereof.

13. The filamentous fungal strain of claim 12, wherein the mycotoxin-associated gene is Fum1, Fum6, Fum8, or combinations thereof.

14. The filamentous fungal strain of claim 12 or claim 12, wherein the filamentous fungal strain is incapable of producing fumonisin.

15. The filamentous fungal strain of claim 12 or claim 13, wherein the filamentous fungal strain produces less fumonisin than a strain of the same filamentous fungi without the one or more mutations.

16. The filamentous fungal strain of claim 12 or claim 13, wherein the filamentous fungal strain produces a modified fumonisin demonstrating reduced or eliminated functionality, or both, as compared to a strain of the same filamentous fungi without the one or more mutations.

17. The filamentous fungal strain of any one of claims 1-16, wherein the filamentous fungus further comprises: one or more rco-3 gene mutations; and / or a mutation in a pigment-associated gene.

18. The filamentous fungal strain of claim 17, wherein the pigment-associated gene is selected from the group consisting of bik1, bik2, bik3, bik4, bik5, and bik6.

19. The filamentous fungal strain of any one of claims 1-18, wherein the filamentous fungal strain is selected from Rhizopus oligosporus, Ustilago esculenta, Hericulum erinaceus, Polyporous squamosus, Grifola fondosa, Hypsizygus marmoreus, Hypsizygus ulmarius, Calocybe gambosa, Pholiota nameko, Calvatia gigantea, Agaricus bisporus, Stropharia rugosoannulata, Hypholoma lateritium, Pleurotus eryngii, Pleurotus ostreatus, Pleurotus ostreatus var. columbinus, Tuber borchii, Morchella esculenta, Morchella conica, Morchella importuna, Sparassis crispa, Fusarium venenatum, Fusarium venenatum A3 / 5, Fusarium strain flavolapis (ATCC Accession Deposit No. PTA- 10698), Disciotis venosa, Clonostachys rosea, Cordyceps militaris, Trametes versicolor, Ganoderma lucidum, Flammulina velutipes, Lentinula edodes, Pleurotus djamor, Pleurotus ostreatus, and Leucoagaricus spp.

20. The filamentous fungal strain of any one of claims 1-18, wherein the filamentous fungal strain is Fusarium strain flavolapis (ATCC Accession Deposit No. PTA-10698).

21. A method of making a mutant filamentous fungal strain, comprising: exposing the fungal strain to a physical mutagen or a chemical mutagen, and / or performing site-directed mutagenesis on the fungal strain; wherein the exposing or the performing introduces at least one reduction of function mutation into at least one mycotoxin-associated gene.

22. The method of claim 21, wherein the mutation comprises at least one loss of function mutation.

23. The method of claim 21 or claim 22, wherein the mutation comprises at least one mutation selected from the group consisting of a knockout mutation, one or more introduced premature stop codons, one or more introduced point mutations, and combinations thereof.

24. The method of claim 23, wherein each point mutation independently produces a frameshift mutation, a nonsense mutation, or a missense mutation.

25. The method of any one of claims 21-24, wherein the physical mutagen is selected from gamma rays, X rays, UV light, fast neutrons, thermal neutrons, beta particles, alpha particles, and combinations thereof.

26. The method of any one of claims 21-24, wherein the chemical mutagen is selected from ethyl methyl sulfate, nitrogen mustards, mitomycin, methyl methane sulfonate, diethyl sulfate, nitrosoguanidine, ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N- nitrosoguanidine, acridine orange, ethidium bromide, proflavin, daunorubicin, and combinations thereof.

27. The method of any one of claims 21-24, wherein the site-directed mutagenesis is selected from knockout mutations, oligonucleotide-directed mutagenesis, Kunkel’s method, cassette mutagenesis, PCR mutagenesis, homologous recombination, CRISPR / Cas9 mutagenesis, Delitto Perfetto, transplacement "pop-in pop-out," direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker, direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker using long homologous regions, in vivo site-directed mutagenesis with synthetic oligonucleotides, and combinations thereof.

28. The method of any one of claims 21-27, further comprising confirming the presence of the at least one reduction of function mutation in the genes.

29. The method of any one of claims 21-28, further comprising exposing the strain to adaptive laboratory evolution to develop a characteristic in the strain selected from a higher growth rate, greater cell density, diminished mycotoxin production, and combinations thereof.

30. The method of claim 29, wherein the adaptive laboratory evolution occurs by serially diluting the mutant strain under selective pressure.

31. A mutant strain of Fusarium flavolapis having one or more reduction of function mutations introduced into its Fum1 gene or having its Fum1 gene deleted.

32. The mutant strain of claim 31, which is incapable of producing more than 10 ppb of fumonisin.

33. The mutant strain of claim 31, which is incapable of producing detectable levels of fumonisin.

34. The mutant strain of claim 31, which is incapable of producing fumonisin.

35. The mutant strain of claim 31, which produces less fumonisin than a Fusarium flavolapis strain without the mutations or deletion.

36. The mutant strain of claim 31, which produces a modified fumonisin demonstrating reduced or eliminated functionality, or both, as compared to a Fusarium flavolapis strain without the mutations or deletion.

37. The mutant strain of any one of claims 31-36, wherein the Fum1 gene sequence is at least about 90% identical to SEQ ID NO:

1.

38. The mutant strain of any one of claims 31-36, which produces a fumonisin protein that is at least 90% identical to SEQ ID NO:

3.

39. The mutant strain of any one of claims 31-36, wherein the Fum1 amino acid sequence comprises an amino acid change from tryptophan to a premature stop codon at position 953.

40. The mutant strain of claim 39, which produces a fumonisin protein having the amino acid sequence of SEQ ID NO:

4.

41. A mutant strain of Fusarium flavolapis having one or more reduction of function mutations introduced into its bea1 gene, or having its bea1 gene deleted.

42. The mutant strain of claim 41, which is incapable of producing beauvericin.

43. The mutant strain of claim 41, which produces less beauvericin than a Fusarium flavolapis strain without the mutations or deletion.

44. The mutant strain of claim 41, which produces a modified beauvericin demonstrating reduced or eliminated functionality, or both, as compared to a Fusarium flavolapis strain without the mutations or deletion.

45. The mutant strain of any one of claims 41-44, wherein the bea1 gene sequence is at least about 90% identical to SEQ ID NO:

5.

46. The mutant strain of any one of claims 41-44, which produces a beauvericin protein that is at least 90% identical to SEQ ID NO:

7.

47. The mutant strain of claim 46, wherein the bea1 amino acid sequence comprises an amino acid change from tryptophan to a premature stop codon at position 1135.

48. The mutant strain of claim 47, which produces a beauvericin protein having the amino acid sequence of SEQ ID NO:

8.

49. A mutant strain of Fusarium venenatum having one or more reduction of function mutations introduced into its bea1 gene, or having its bea1 gene deleted.

50. The mutant strain of claim 49, which is incapable of producing beauvericin.

51. The mutant strain of claim 49, which produces less beauvericin than a Fusarium venenatum strain without the mutations or deletion.

52. The mutant strain of claim 49, which produces a modified beauvericin demonstrating reduced or eliminated functionality, or both, as compared to a Fusarium venenatum strain without the mutations or deletion.

53. The mutant strain of any one of claims 49-52, wherein the bea1 gene sequence is at least about 90% identical to SEQ ID NO:

9.

54. A filamentous fungal strain, comprising one or more one or more reduced function mutations in one or more pigment-associated genes.

55. The filamentous fungal strain of claim 54, wherein the one or more mutations comprises at least one loss of function mutation.

56. The filamentous fungal strain of claim 54 or claim 55, wherein the one or more mutations are selected from the group consisting of a knockout mutation, one or more introduced premature stop codons, one or more introduced point mutations, and combinations thereof.

57. The filamentous fungal strain of claim 56, wherein each point mutation independently produces a frameshift mutation, a nonsense mutation, or a missense mutation.

58. The filamentous fungal strain of any one of claims 54-57, which is incapable of producing bikaverin.

59. The filamentous fungal strain of claim 54-57, wherein the filamentous fungal strain produces less bikaverin than a filamentous fungal strain of the same species without the mutations.

60. The filamentous fungal strain of claim 54-57, which produces a modified bikaverin demonstrating reduced or eliminated functionality, or both, as compared to a filamentous fungal strain of the same species without the mutations.

61. The filamentous fungal strain of any one of claims 54-60, wherein the pigment- associated gene is selected from the group consisting of bik1, bik2, bik3, bik4, bik5, and bik6.

62. The filamentous fungal strain of any one of claims 54-61, wherein the pigment- associated gene is selected from the group consisting of bik1, bik2, and bik3.

63. The filamentous fungal strain of any one of claims 54-62, wherein the pigment- associated gene is bik1.

64. The filamentous fungal strain of any one of claims 54-63, wherein production of a pigment in the strain is reduced as compared to a filamentous fungal strain of the same species without the one or more mutations.

65. The filamentous fungal strain of claim 64, wherein the strain is grown under conditions of nitrogen limitation during submerged fermentation.

66. The filamentous fungal strain of any one of claims 54-65, wherein a biomass of the filamentous fungal strain has a whiter color than a biomass of a filamentous fungal strain of the same species without the one or more mutations.

67. The filamentous fungal strain of any one of claims 54-66, wherein a biomass of the filamentous fungal strain has a Whiteness Index of at least 7.

5.

68. The filamentous fungal strain of any one of claims 54-67, wherein a biomass of the filamentous fungal strain has a high L* value.

69. The filamentous fungal strain of any one of claims 54-68, wherein a biomass of the filamentous fungal strain has an L* value of about 75 – about 100 or about 50 – about 100.

70. The filamentous fungal strain of any one of claims 54-69, wherein a biomass of the filamentous fungal strain has a low a* value and a low b* value.

71. The filamentous fungal strain of any one of claims 54-70, wherein an a* value and a b* value of a biomass of the filamentous fungal strain is each independently about 0 – about 30, or about 0 – about 25.

72. The filamentous fungal strain of any one of claims 54-71, further comprising an rco-3 gene mutation, a mutation in a mycotoxin-associated gene, or both.

73. The filamentous fungal strain of claim 72, wherein the mycotoxin-associated gene is selected from the group consisting of bea1, Fum1, Fum6, and Fum8.

74. The filamentous fungal strain of any one of claims 54-73, wherein the filamentous fungus is selected from the group consisting of Rhizopus oligosporus, Ustilago esculenta, Hericulum erinaceus, Polyporous squamosus, Grifola fondosa, Hypsizygus marmoreus, Hypsizygus ulmarius, Calocybe gambosa, Pholiota nameko, Calvatia gigantea, Agaricus bisporus, Stropharia rugosoannulata, Hypholoma lateritium, Pleurotus eryngii, Pleurotus ostreatus, Pleurotus ostreatus var. columbinus, Tuber borchii, Morchella esculenta, Morchella conica, Morchella importuna, Sparassis crispa, Fusarium venenatum, Fusarium venenatum A3 / 5, Fusarium strain flavolapis (ATCC Accession Deposit No. PTA-10698), Disciotis venosa, Clonostachys rosea, Cordyceps militaris, Trametes versicolor, Ganoderma lucidum, Flammulina velutipes, Lentinula edodes, Pleurotus djamor, Pleurotus ostreatus, and Leucoagaricus spp.

75. The filamentous fungal strain of any one of claims 54-74, wherein the filamentous fungus is Fusarium strain flavolapis (ATCC Accession Deposit No. PTA-10698).

76. A method of making a mutant filamentous fungal strain, comprising: exposing the fungal strain to a physical mutagen or a chemical mutagen, and / or performing site-directed mutagenesis on the fungal strain; wherein the exposing or the performing introduces at least one reduction of function mutation into at least one pigment-associated gene.

77. The method of claim 76, wherein the mutation comprises at least one loss of function mutation.

78. The method of claim 76 or claim 77, wherein the mutation comprises at least one mutation selected from the group consisting of one or more knockout mutations, one or more introduced premature stop codons, one or more introduced point mutations, and combinations thereof.

79. The method of claim 78, wherein each point mutation independently produces a frameshift mutation, a nonsense mutation, or a missense mutation.

80. The method of any one of claims 76-79, wherein the physical mutagen is selected from gamma rays, X rays, UV light, fast neutrons, thermal neutrons, beta particles, alpha particles, and combinations thereof.

81. The method of any one of claims 76-79, wherein the chemical mutagen is selected from ethyl methyl sulfate, nitrogen mustards, mitomycin, methyl methane sulfonate, diethyl sulfate, nitrosoguanidine, ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N- nitrosoguanidine, acridine orange, ethidium bromide, proflavin, daunorubicin, and combinations thereof. In some embodiments, the chemical mutagen is selected from ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, and combinations thereof.

82. The method of any one of claims 76-79, wherein the site-directed mutagenesis is selected from oligonucleotide-directed mutagenesis, Kunkel’s method, cassette mutagenesis, PCR mutagenesis, homologous recombination, CRISPR / Cas9 mutagenesis, Delitto Perfetto, transplacement "pop-in pop-out," direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker, direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker using long homologous regions, in vivo site-directed mutagenesis with synthetic oligonucleotides, and combinations thereof.

83. The method of any one of claims 76-82, further comprising confirming the presence of the reduction of function mutation in the gene.

84. The method of any one of claims 76-83, further comprising exposing the strain to adaptive laboratory evolution to develop a characteristic in the strain selected from a higher growth rate, greater cell density, diminished pigment production, and combinations thereof.

85. The method of claim 84, wherein the adaptive laboratory evolution occurs by serially diluting the mutant strain under selective pressure.

86. A mutant strain of Fusarium flavolapis having one or more premature stop codons and / or one or more point mutations introduced into its bik1 gene or having its bik1 gene deleted.

87. The mutant strain of claim 86, which is incapable of producing detectable levels of bikaverin.

88. The mutant strain of claim 86, which is incapable of producing bikaverin.

89. The mutant strain of claim 86, which produces less bikaverin than a Fusarium flavolapis strain without the stop codons or point mutations.

90. The mutant strain of claim 86, which produces a modified bikaverin demonstrating reduced or eliminated functionality, or both, as compared to a Fusarium flavolapis strain without the stop codons or point mutations.

91. The mutant strain of any one of claims 86-90, wherein the bik1 gene sequence is at least about 90% identical to SEQ ID NO:

18.

92. The mutant strain of any one of claims 86-91, which produces a bikaverin synthase protein that is at least 90% identical to SEQ ID NO:

20.

93. A filamentous fungal strain, comprising one or more one or more reduced function mutations in one or more ethanol-associated genes.

94. The filamentous fungal strain of claim 93, wherein the one or more mutations comprise at least one loss of function mutation.

95. The filamentous fungal strain of claim 93 or claim 94, wherein the one or more mutations are selected from the group consisting of one or more knockout mutations, one or more introduced premature stop codons, one or more introduced point mutations, and combinations thereof.

96. The filamentous fungal strain of claim 95, wherein each point mutation independently produces a frameshift mutation, a nonsense mutation, or a missense mutation.

97. The filamentous fungal strain of any one of claims 93-96, wherein production of ethanol in the strain when grown using glucose as a carbon source is reduced as compared to a filamentous fungal strain of the same species without the one or more mutations.

98. The filamentous fungal strain of claim 97, which exhibits increased growth when grown using glucose as a carbon source as compared to a filamentous fungal strain of the same species without the one or more mutations.

99. The filamentous fungal strain of claim 97 or claim 98, wherein growth occurs via submerged fermentation.

100. The filamentous fungal strain of claim 97 or claim 98, wherein growth occurs via liquid surface fermentation.

101. The filamentous fungal strain of any one of claims 93-100, wherein the filamentous fungal strain is incapable of producing ethanol.

102. The filamentous fungal strain of any one of claims 93-100, wherein the filamentous fungal strain produces less ethanol than a filamentous fungal strain of the same species without the mutations.

103. The filamentous fungal strain of any one of claims 93-100, wherein the filamentous fungal strain exhibits increased growth using glucose as a carbon source when compared to a filamentous fungal strain of the same species without the mutations.

104. The filamentous fungal strain of any one of claims 93-103, wherein the one or more ethanol-associated genes are selected from the group consisting of rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof.

105. The filamentous fungal strain of any one of claims 93-104, wherein the one or more ethanol-associated genes are selected from the group consisting of rco-3, col-26, glt-1, cre1, hgt, and combinations thereof.

106. The filamentous fungal strain of any one of claims 93-105, wherein the ethanol- associated gene is rco-3.

107. The filamentous fungal strain of claim 106, wherein ethanol production in the strain when grown using glucose as a carbon source is reduced as compared to a filamentous fungal strain of the same species comprising a wild-type rco-3 gene.

108. The filamentous fungal strain of claim 106, wherein growth in the strain when grown using glucose as a carbon source is increased as compared to a filamentous fungal strain of the same species comprising a wild-type rco-3 gene.

109. The filamentous fungal strain of claim 107 or claim 108, wherein growth occurs via submerged fermentation.

110. The filamentous fungal strain of claim 107 or claim 108, wherein growth occurs via liquid surface fermentation.

111. The filamentous fungal strain of any one of claims 93-110, further comprising a mutation in a pigment-associated gene, a mutation in a mycotoxin-associated gene, or both.

112. The filamentous fungal strain of claim 111, wherein the mycotoxin-associated gene is selected from the group consisting of bea1, Fum1, Fum6, Fum8, and combinations thereof.

113. The filamentous fungal strain of claim 111 or claim 112, wherein the pigment- associated gene is selected from the group consisting of bik1, bik2, bik3, bik4, bik5, bik6, and combinations thereof.

114. The filamentous fungal strain of claim 111 or claim 112, wherein the pigment- associated gene is selected from the group consisting of rco-3, col-26, glt-1, cre1, hgt, hxt, and combinations thereof.

115. The filamentous fungal strain of any one of claims 93-114, wherein the filamentous fungus is selected from the group consisting of Rhizopus oligosporus, Ustilago esculenta, Hericulum erinaceus, Polyporous squamosus, Grifola fondosa, Hypsizygus marmoreus, Hypsizygus ulmarius, Calocybe gambosa, Pholiota nameko, Calvatia gigantea, Agaricus bisporus, Stropharia rugosoannulata, Hypholoma lateritium, Pleurotus eryngii, Pleurotus ostreatus, Pleurotus ostreatus var. columbinus, Tuber borchii, Morchella esculenta, Morchella conica, Morchella importuna, Sparassis crispa, Fusarium venenatum, Fusarium venenatum A3 / 5, Fusarium strain flavolapis (ATCC Accession Deposit No. PTA-10698), Disciotis venosa, Clonostachys rosea, Cordyceps militaris, Trametes versicolor, Ganoderma lucidum, Flammulina velutipes, Lentinula edodes, Pleurotus djamor, Pleurotus ostreatus, and Leucoagaricus spp.

116. The filamentous fungal strain of any one of claims 93-115, wherein the filamentous fungus is Fusarium strain flavolapis (ATCC Accession Deposit No. PTA-10698).

117. A method of making a mutant filamentous fungal strain, comprising: exposing the fungal strain to a physical mutagen or a chemical mutagen, and / or performing site-directed mutagenesis on the fungal strain; wherein the exposing or the performing introduces at least one reduction of function mutation into at least one ethanol-associated gene.

118. The method of claim 117, wherein the mutation comprises at least one loss of function mutation.

119. The method of claim 117 or claim 118, wherein the mutation is selected from the group consisting of one or more knockout mutations, one or more introduced premature stop codons, one or more introduced point mutations, and combinations thereof.

120. The method of claim 119, wherein each point mutation independently produces a frameshift mutation, a nonsense mutation, or a missense mutation.

121. The method of any one of claims 117-120, wherein the physical mutagen is selected from gamma rays, X rays, UV light, fast neutrons, thermal neutrons, beta particles, alpha particles, and combinations thereof.

122. The method of any one of claims 117-120, wherein the chemical mutagen is selected from ethyl methyl sulfate, nitrogen mustards, mitomycin, methyl methane sulfonate, diethyl sulfate, nitrosoguanidine, ethyl methanesulfonate, sodium azide, N-methyl-N'- nitro-N-nitrosoguanidine, acridine orange, ethidium bromide, proflavin, daunorubicin, and combinations thereof. In some embodiments, the chemical mutagen is selected from ethyl methanesulfonate, sodium azide, N-methyl-N'-nitro-N-nitrosoguanidine, and combinations thereof.

123. The method of any one of claims 117-120, wherein the site-directed mutagenesis is selected from oligonucleotide-directed mutagenesis, Kunkel’s method, cassette mutagenesis, PCR mutagenesis, homologous recombination, CRISPR / Cas9 mutagenesis, Delitto Perfetto, transplacement "pop-in pop-out," direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker, direct gene deletion and site-specific mutagenesis with PCR and one recyclable marker using long homologous regions, in vivo site-directed mutagenesis with synthetic oligonucleotides, and combinations thereof.

124. The method of any one of claims 117-123, further comprising confirming the presence of the reduction of function mutation in the gene.

125. The method of any one of claims 117-124, further comprising exposing the strain to adaptive laboratory evolution to develop a characteristic in the strain selected from a higher growth rate, greater cell density, diminished pigment production, and combinations thereof.

126. The method of claim 125, wherein the adaptive laboratory evolution occurs by serially diluting the mutant strain under selective pressure.

127. A mutant strain of Fusarium flavolapis having one or more reduction of function mutations introduced into its rco-3 gene, or having its rco-3 gene deleted.

128. The mutant strain of claim 127, which exhibits increased growth when grown using glucose as a carbon source as compared to a filamentous fungal strain of the same species without the mutations or deletion.

129. The mutant strain of claim 127 or claim 128, which is incapable of producing ethanol.

130. The mutant strain of any one of claims 127-129, which produces less ethanol than a Fusarium flavolapis strain without the mutations or deletion.

131. The mutant strain of any one of claims 127-130, which exhibits increased growth and reduced ethanol production when grown using glucose as a carbon source as compared to a filamentous fungal strain of the same species without the mutations or deletion.

132. The mutant strain of any one of claims 127-131, wherein the rco-3 gene sequence is at least about 90% identical to SEQ ID NO:

11.

133. The mutant strain of any one of claims 127-132, which produces a RCO3 protein that is at least 90% identical to SEQ ID NO:

14.

134. A mycelial biomass comprising the filamentous fungal strain of any one of claims 1-20, 31-75, 86-116, or 127-133.

135. A cohesive mycelial biomass comprising the filamentous fungal strain of any one of claims 1-20, 31-75, 86-116, or 127-133.

136. A mycelial biomass made by the method of any one of claims 21-30, 76-85, or 117- 126.

137. A cohesive mycelial biomass made by the method of any one of claims 21-30, 76- 85, or 117-126.

138. A food product comprising the mycelial biomass of claim 136 or claim 137, wherein the food product is selected from human food, animal feed, aquaculture feed, and pet food.

139. The food product of claim 138, wherein the mycelial biomass is formulated as a liquid dispersion, a mycelial flour, or particles.

140. The food product of claim 138, wherein the biomass is formulated as a liquid dispersion and the food product is a dairy analog.

141. The food product of claim 140, wherein the dairy analog is selected from: hard cheese analogs, semi-hard cheese analogs, semi-soft cheese analogs, soft or soft ripened cheese analogs, cream cheese analogs, sour milk cheese analogs, blue cheese analogs, mascarpone cheese analogs, pasta filata analogs, brined cheese analogs, whey cheese analogs, fresh cheese analogs, butter analogs, whey analogs, cream analogs, sour milk analogs, yogurt analogs, milk analogs, powdered dairy analogs, ice cream analogs, and combinations thereof.

142. The food product of claim 138 or claim 139, wherein: the biomass is formulated as a mycelial flour and the food product is one or more baked goods; or the biomass is formulated as a mycelial flour and the food product is fried to create a noodle analog food product.

143. The food product of claim 29, wherein the biomass is formulated as particles and the food product is selected from a meat analog, a tofu analog, and textured vegetable protein analog.

144. A textile product comprising the mycelial biomass of claim 136 or claim 137.

145. The textile product of claim 144, which comprises a fungal durable sheet material.

146. The textile product of claim 145, wherein the sheet material is selected from textiles, fabrics and leather analogs.

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