Genetically modified yeast for production of non-alcoholic beverages

Abstract

Provided herein are genetically modified yeast cells that comprise genetic modifications to reduce sensory detection of one or more wort-associated off-flavors of a fermented beverage and the cell is not capable of converting maltose and / or maltotriose to ethanol. Also provided are methods of producing fermented products (e.g., non-alcoholic fermented beverages) using the genetically modified yeast cells described herein.

Description

[0001] GENETICALLY MODIFIED YEAST FOR PRODUCTION OF NON-ALCOHOLIC BEVERAGES CROSS-REFERENCE TO RELATED APPLICATIONS The present application claims the benefit of U.S. provisional application No. 63 / 579,269, filed August 28, 2023, the content of which is hereby incorporated in its entirety. SEQUENCE LISTING The application contains a Sequence Listing which has been submitted electronically in .XML format and is hereby incorporated by reference in its entirety. Said .XML copy, created on August 27, 2024, is named “129085.00043.xml” and is 142,566 bytes in size. The sequence listing contained in this .XML file is part of the specification and is hereby incorporated by reference herein in its entirety. BACKGROUND Consumer demand for non-alcoholic (NA) beer has grown dramatically over the last decade. In 2023, sales of NA beer (usually defined as beer containing less than .5% ABV) are projected to total nearly $25B, up from $13B in 2015 (Smith, S. Trends Revealed: The Non- Alcoholic Beer Market Is Bubbling Up. HubSpot: blog.hubspot.com / the-hustle / the-non- alcoholic-beer-market-is-bubbling-up#article (2022)). This near doubling in market size represents an 8.3% compound annual growth rate (CAGR), which far surpassed the 1.8% CAGR of the alcoholic beer sector during this period (Non-Alcoholic Beer Market Share, Trends, and Global Sales Analysis to 2030: marketresearchfuture.com / reports / non-alcoholic- beer-market-3912). The rapidly growing popularity of NA beer has predominantly been attributed to the shifting preferences of pre-existing beer drinkers. In recent years, numerous studies have found that excessive consumption of alcohol poses serious health risks (Rehm, J. et al. The relation between different dimensions of alcohol consumption and burden of disease: an overview. Addiction 105, (2010); White, A. & Hingson, R. The burden of alcohol use: excessive alcohol consumption and related consequences among college students. Alcohol Res.35, (2013); Behaviors, A. Global status report on alcohol and health 2018: who.int / publications / i / item / 9789241565639 (2018)), and as a result consumers have become increasingly motivated to reduce their consumption of alcoholic beverages (Bronin, A. Beyond JAAD January 2023. J. Am. Acad. Dermatol.88, e1–e4 (2023)). This shift away from alcoholic beverages, when paired with an overall global trend towards healthier eating habits (International Food Information Council.2022 Food and Health Survey; Grimmelt, A., Moulton, J., Pandya, C. & Snezhkova, N. Hungry and confused: The winding road to conscious eating. mckinsey.com / industries / consumer-packaged-goods / our-insights / hungry- and-confused-the-winding-road-to-conscious-eating (2022)), may underlie much of the recent uptick in consumer interest in NA beer. Growth of the NA beer market is expected to continue at a rapid pace into the foreseeable future, with global NA beer sales projected to surpass $40B annually by 2032 (Pulidindi, K. & Ahuja, K. Non-Alcoholic Beer Market - By Product (Alcohol Free {By Material [Malted Grains, Hops, Yeast and Enzymes], By Technology [Restricted Fermentation and Dealcoholization {Reverse Osmosis}], By Sales Channel (Liquor Stores, Convenience Stores]}, Low Alcohol) & Forecast, 2023-2032, gminsights.com / industry-analysis / non-alcoholic-beer-market (2022)). SUMMARY In one aspect, provided herein is a genetically modified yeast cell, e.g. a brewing yeast cell, that is incapable of or has a reduced capability of converting maltose and / or maltotriose to ethanol. In some embodiments, the genetically modified yeast cell comprises a heterologous nucleic acid encoding an enzyme having alcohol acyltransferase (EC 2.3.1.84) activity. In another aspect, a liquid fermentation composition is provided that comprises: (a) a population of genetically modified yeast cells that are genetically modified to produce one or more acetate esters and / or ethyl esters, wherein the yeast cells are incapable of or have a reduced capability of converting maltose and / or maltotriose to ethanol, (b) a sugar source comprising wort, wherein total sugar in the wort has been attenuated by no more than 25% by the population of genetically modified yeast cells, (c) one or more wort-derived aldehydic and / or non-aldehyde molecules; and (d) no more than 1.0% (v / v) alcohol. In another aspect, a liquid fermentation composition is provided that comprises: (a) a population of genetically modified yeast cells that are genetically modified to be incapable of or to have a reduced capability of converting maltose and / or maltotriose to ethanol, (b) a sugar source comprising wort, wherein total sugar in the wort has been attenuated by no more than 25% by the population of genetically modified yeast cells, and (c) no more than 1.0% (v / v) alcohol. In another aspect, a method of producing a fermented beverage is provided, comprising: (a) providing a genetically modified yeast cell comprising a functional disruption in one or more proteins associated with maltose and / or maltotriose transport, and / or maltose and / or maltotriose hydrolysis in the yeast cell, wherein the functional disruption(s) result in reduced growth of the yeast cell on maltose as a sole sugar source compared to a yeast cell not comprising the genetic modification, (b) providing a medium comprising a wort-derived sugar source, (c) combining the genetically modified yeast cell and the medium to form a fermentation composition, and (d) allowing the fermentation composition to ferment to produce a fermented beverage. In another aspect, a method of producing a fermented beverage is provided, comprising contacting of a population of genetically modified yeast cells of the present disclosure with a medium comprising a wort-derived sugar source during a fermentation process to produce the fermented beverage. Aspects of the present disclosure provide genetically modified yeast cells (modified cells) comprising one or more genetic modifications to reduce sensory detection of one or more wort-associated off-flavors of a fermented beverage; wherein the modified cell is not capable of converting maltose and / or maltotriose to ethanol. In some embodiments, the wort- associated off-flavors comprise aldehydic and / or non-aldehyde molecules. In some embodiments, the aldehydic molecule is 2-methylbutanal, 2-methylpropanal, hexanal, benzaldehyde, furfural, acetaldehyde, methional, phenylacetaldehyde, or 5-hydrox-methyl- furfural. In some embodiments, the non-aldehyde molecule is (E)-beta-damascenone or 5- ethyl-3-hydroxy-4-methyl-2(5H)-furanone. In some embodiments, the modified cell is capable of converting glucose to ethanol. In some embodiments, the modified cell comprises one or more genetic modifications to functionally disrupt one or more proteins associated with maltose and / or maltotriose transport into the modified cell and / or maltose and / or maltotriose hydrolysis by the modified cell. In some embodiments, the modified cell comprises one or more genetic modifications to functionally disrupt a maltose and / or maltotriose transporter. In some embodiments, the modified cell is genetically modified to be deficient in MAL31 and MAL11 (AGT1). In some embodiments, the one or more genetic modifications to reduce sensory detection of one or more wort-associated off-flavors results in increased production of one or more acetate esters and / or ethyl esters as compared to a cell that does not comprise the genetic modification(s). In some embodiments, the acetate ester is ethyl acetate, isoamyl acetate, and / or phenethyl acetate. In some embodiments, the ethyl ester is ethyl hexanoate, ethyl octanoate, and / or ethyl decanoate. In some embodiments, the one or more genetic modifications that increases production of one or more acetate esters and / or ethyl esters comprises overexpression of an enzyme having alcohol acyltransferase (AAT) activity. In some embodiments, the enzyme having AAT activity comprises a sequence set forth in SEQ ID NO: 5. In some embodiments, the one or more genetic modifications that increase production of one or more acetate esters and / or ethyl esters comprises expression of a heterologous enzyme having alcohol acyltransferase (AAT) activity. In some embodiments, the heterologous enzyme having AAT activity comprises a sequence set forth in SEQ ID NO: 7. In some embodiments, the one or more genetic modifications to reduce sensory detection of one or more wort-associated off-flavors results in increased production of 3- mercaptohexanol (3MH). In some embodiments, the one or more genetic modifications that increases production of 3MH comprises expression of a bacterial enzyme having carbon- sulfur-lyase (CSL) activity. In some embodiments, the bacterial enzyme having CSL activity comprises a sequence set forth in SEQ ID NO: 9. In some embodiments, the one or more genetic modifications to reduce sensory detection of one or more wort-associated off-flavors results in increased production of one or more monoterpene. In some embodiments, the monoterpene is linalool, geraniol, and / or citronellol. In some embodiments, the one or more genetic modifications that increases production of one or more monoterpenes comprises expression of one or more of: (a) a truncated variant of a yeast HMG1 enzyme; (b) a variant of a ERG20 enzyme; (c) a linalool synthase; and / or (d) a geraniol synthase. In some embodiments, the truncated variant of a yeast HMG1 enzyme comprises a sequence set forth in SEQ ID NO: 11. In some embodiments, the variant of ERG20 enzyme comprises a sequence set forth in SEQ ID NO: 13. In some embodiments, the linalool synthase comprises a sequence set forth in SEQ ID NO: 15. In some embodiments, the geraniol synthase comprises a sequence set forth in SEQ ID NO: 17. In some embodiments, the yeast cell is of the genus Saccharomyces. In some embodiments, the yeast cell is of the species Saccharomyces cerevisiae (S. cerevisiae). In some embodiments, the yeast cell is S. cerevisiae Chico Ale yeast, London Ale yeast, Andechs Lager yeast, Augustiner Lager yeast, or American Ale yeast. Aspects of the present disclosure provide methods of producing a fermented beverage, comprising contacting any of the modified cells described herein with a medium comprising at least one fermentable sugar, wherein the contacting is performed during at least a first fermentation process, to produce a fermented beverage. In some embodiments, the fermented beverage is a reduced alcohol fermented beverage. In some embodiments, the fermented beverage has an alcohol content of less than or equal to about 1.0% (v / v) alcohol. In some embodiments, the fermented beverage has an alcohol content of about 0.01% (v / v) to about 1.0% (v / v). In some embodiments, the fermented beverage has an alcohol content of about 0.01% (v / v) to about 0.5% (v / v). In some embodiments, the method does not include a step of physically removing alcohol from the beverage or prematurely halting fermentation. In some embodiments, at least one fermentable sugar is provided in at least one sugar source. In some embodiments, the fermentable sugar is glucose, fructose, and / or sucrose. In some embodiments, the first fermentation process results in a reduction in the level of the fermentable sugar by at least 15%. In some embodiments, the fermented beverage is beer. In some embodiments, the sugar source comprises wort. In some embodiments, the sugar source is wort and the method further comprises producing the medium, wherein producing the medium comprises (a) contacting a plurality of grains with water; and (b) boiling or steeping the water and grains to produce wort. In some embodiments, the method further comprises adding at least one hop variety to the wort to produce a hopped wort. In some embodiments, the method further comprises adding at least one hop variety to the medium. In some embodiments, the method further comprises at least one additional fermentation process. In some embodiments, the method further comprises carbonating the fermented product. Other aspects of the present disclosure provide a genetically modified beer fermentation yeast cell (modified cell) comprising one or more genetic modifications to functionally disrupt maltose / maltotriose transporters MAL31 and MAL11 (AGT1). The details of one or more embodiments of the invention are set forth in the description below. Other features or advantages of the present invention will be apparent from the following drawings and detailed description of several embodiments, and also from the appended claims. BRIEF DESCRIPTION OF THE DRAWINGS The accompanying drawings are not intended to be drawn to scale. In the drawings, each identical or nearly identical component that is illustrated in various figures is represented by a like numeral. For purposes of clarity, not every component may be labeled in every drawing. In the drawings: FIG.1 shows chemical structures of the exemplary fermentable sugars glucose, maltose, and maltotriose. FIG.2 shows attenuation of wort sugars by S. cerevisiae Chico lacking MAL31 and MAL11 (AGT1) (MAL31:: Δ AGT1::Δ, also referred to as BY632 (orange line)) and wild- type S. cerevisiae Chico strain (blue line) in a representative 20 L beer fermentation. Fermentations were started with a total wort sugar content of 12° Plato. Percent attenuation was calculated as (1- (°Plato at fermentation endpoint / °Plato at start of fermentation)) * 100. BY632 strain attenuated wort sugars by 21.7%, and Chico attenuated wort sugars by 79.1%. FIG.3A shows the concentrations of ethyl acetate, isoamyl acetate, and phenethyl acetate in 250 different commercial alcoholic beers. Data used in the figure was collected in [Cite PMID: 38531860]. FIG.3B shows relative levels of acetate esters and ethyl esters in small scale fermentations with Chico and strains unable to convert maltose and maltotriose to ethanol (“maltose negative” (MN) strains). The values reported in each cell represents log2 of the peak-area fold change for each ester measured in fermentations with the indicated strains, relative to its peak area in fermentations with the wild-type S. cerevisiae Chico strain. All fermentations were performed in duplicate, and the values reported are the mean of these replicates. More positive values indicate esters at higher concentrations than in fermentations with the wild-type S. cerevisiae Chico strain, and more negative values indicate esters at lower concentrations than in fermentations with the wild-type S. cerevisiae Chico strain. The percent attenuation achieved by each strain is indicated to the right of the strain name. The genotype of each strain is shown in the table below the heatmap, alongside aroma notes detected at the end of fermentation. FIG.4 shows blinded sensory panel evaluation of beers brewed with the wild-type S. cerevisiae Chico strain, BY632 (MAL31:: Δ AGT1::Δ), and S. cerevisiae Chico strain BY1505 (MAL31:: Δ; AGT1::Δ; YPS3::pNCP1-tmcHMG,pERG11-ERG20(F96W;N127W), pHSP26-tmcMcLIS, pPGK1-tmcObGES,). These beers were included in a sensory evaluation alongside three additional beers brewed with MN strains (not shown). All six beers were rated on a scale of 1 (best) to 6 (worst) by each of the five sensory judges. Each point reports the rating given to each beer by one judge, and lines report the mean rating of each beer across all judges. Beer produced by fermentation with strain BY1505 was rated significantly better than beer produced using strain BY632 (p=.008, two-sided Wilcoxon Rank Sum Test), and nominally better than beer produced using the wild-type S. cerevisiae Chico strain (not significant). FIG.5A shows blinded sensory panel evaluation of beers brewed with BY632, BY1575, BY1578, BY1576, BY1574, BY1503, BY1573, and BY1504 at different isoamyl acetate concentrations. All eight beers were rated on a scale of 0 (absent) to 10 (most intense) by each of the twelve sensory judges for tomato intensity, vegetal intensity and cereal intensity. Each plot shows the intensity of one wort-associated sensory attribute for all eight NA beers assessed. Each point represents one beer, and the beer's position along the x- axis reflects the concentration of isoamyl acetate present in the beer. Points report the mean intensity rating of the indicated flavor attribute among all sensory panelists, and error bars report one standard deviation of this mean. The blue trendline shows the correlation between isoamyl acetate concentration and perceived intensity of the indicated sensory attribute. All correlation coefficients are statistically significant. FIG.5B shows the analogous plots with phenethyl acetate. FIG.5C shows the analogous plots with ethyl acetate. FIG.6A shows blinded sensory panel evaluation of beers brewed with BY632, BY1575, BY1578, BY1576, BY1574, BY1503, BY1573, and BY1504 at different isoamyl acetate concentrations. All eight beers were rated on a scale of 0 (absent) to 10 (most intense) by each of the twelve sensory judges for banana intensity and solvent intensity. Each plot shows the intensity of one sensory attribute for all eight NA beers assessed. Each point represents one beer, and the beer's position along the x-axis reflects the concentration of isoamyl acetate present in the beer. Points report the mean intensity rating of the indicated flavor attribute among all sensory panelists, and error bars report one standard deviation of this mean. The blue trendline shows the correlation between isoamyl acetate concentration and perceived intensity of the indicated sensory attribute. All correlation coefficients are statistically significant. FIG.6B shows the analogous plots with phenethyl acetate. FIG.6C shows the analogous plots with ethyl acetate. FIG.7 shows blinded ranked preferences for five beers brewed with BY632, BY1574, BY1503, BY1573 and BY1504 strains. The boxplot displays the rankings of each of these beers by the sensory panel, as identified by the strain numbers used to brew them (x- axis, labeled with the “B” at the beginning of the strain name). FIGS.8A-C show modeling of ranked preference versus acetate esters to determine preferred desirable concentration ranges for isoamyl acetate (A), ethyl acetate (B) and phenethyl acetate (C). Black points report the mean preference rank and error bars report 1 standard deviation of the mean. These data are the same as is shown in figure 3. The horizontal black bar represents the mean preference rank of beer produced by the y632 strain, which was not engineered for heterologous AAT expression. The parabola represents the polynomial equation shown in the subtitle of each panel, and mathematically describes the relationship between the concentration of each acetate ester and its preference rank. For each molecule, we defined a range of concentrations that improve the sensory ranking of the beer above the mean ranking of y632. This range is defined as the concentration of a given acetate ester that gives a flavor ranking that is greater than the mean y632 ranking and for which the concentration of the acetate ester is greater than in y632 beer. The boundaries of this range are indicated as vertical dashed lines in each panel, and the concentrations at these boundaries are reported in text. DETAILED DESCRIPTION While consumer demand for non-alcoholic (NA) beer (i.e., beer having less than or equal to 0.5% vol / vol) has increased in recent years, the quality of NA beers that are commercially available is generally considered to be poor (Blanco, C. A., Andrés-Iglesias, C. & Montero, O. Low-alcohol Beers: Flavor Compounds, Defects, and Improvement Strategies. Crit. Rev. Food Sci. Nutr. (2016) doi:10.1080 / 10408398.2012.733979; Gernat, D. C., Brouwer, E. & Ottens, M. Aldehydes as Wort Off-Flavours in Alcohol-Free Beers— Origin and Control. Food Bioprocess Technol.13, 195–216 (2019); Piornos, J. A., Koussissi, E., Balagiannis, D. P., Brouwer, E. & Parker, J. K. Alcohol-free and low-alcohol beers: Aroma chemistry and sensory characteristics. Compr. Rev. Food Sci. Food Saf.22, 233–259 (2023)). Compared to alcoholic beer, NA beer is often characterized as having muted “beer- like” flavors, thin mouthfeel, and off-putting aromas. It is well understood that NA beers have these negative sensorial attributes because of limitations in the production processes used to make them non-alcoholic (Salan^ă, L. C. et al. Non-Alcoholic and Craft Beer Production and Challenges. Processes 8, 1382 (2020)). While several different processes for NA beer production exist, all have drawbacks that negatively impact the flavor and aroma of the beer that is produced. Because of the poor taste of most commercially available NA beers, consumers are often forced to choose between drinking a good-tasting alcoholic beer, and a healthier, but less appealing NA beer. The present disclosure describes the development of genetically engineered yeast strains that allow for the production of NA beer with fewer undesirable off-flavors (e.g., wort-associated off-flavors) and aromas. Also provided herein are modified yeast cells that are incapable of or have a reduced capability of fermenting maltose and / or maltotriose to ethanol but also overexpress an alcohol-acyltransferase (AAT) enzyme to improve the sensory profile of NA beer. Also provided herein are modified yeast cells that are incapable of or have a reduced capability of fermenting maltose and / or maltotriose to ethanol but express enzymes having cysteine S-conjugate beta-lyase enzyme (CSL) activity to improve the sensory profile of NA beer. Also provided herein are modified yeast cells that express one or more enzymes for the production of monoterpenes that improve the sensory profile of NA beer. Conventional processes for the production of non-alcoholic beer include (1) normal fermentation followed by physical dealcoholization, and 2) arrested fermentation (Muller, C., Neves, L. E., Gomes, L., Guimarães, M. & Ghesti, G. Processes for alcohol-free beer production: a review. Food Sci. Technol.40, 273–281 (2019)). For processes involving normal yeast fermentation followed by physical dealcoholization, the beer is first produced by typical alcoholic fermentation that results in a beverage with an ethanol content of 3-10%. Following fermentation, the beer is treated by one of various methods for removing most of the ethanol, such as thermal processes like evaporation and rectification, or membrane-based processes like dialysis and reverse osmosis (Muller, C., Neves, L. E., Gomes, L., Guimarães, M. & Ghesti, G. Processes for alcohol-free beer production: a review. Food Sci. Technol.40, 273–281 (2019); Kozłowski, R., Dziedziński, M., Stachowiak, B. & Kobus-Cisowska, J. Non- and low-alcoholic beer - popularity and manufacturing techniques. Acta Sci. Pol. Technol. Aliment.20, (2021)). These processes can result in NA beers containing less than 0.01% ABV, however physical dealcoholization not only removes ethanol but also removes many of the desirable flavor and aroma molecules that impart the expected flavor and aroma of beer (A review of methods of low alcohol and alcohol-free beer production. J. Food Eng. 108, 493–506 (2012); Production of Alcohol-Free Beer. in Beer in Health and Disease Prevention 61–75 (Academic Press, 2009)). Following dealcoholization, the concentrations of these desirable flavor molecules – predominantly esters, terpenes, thiols, and fusel alcohols – can be reduced by over 80% compared to the beer prior to the dealcoholization process (A review of methods of low alcohol and alcohol-free beer production. J. Food Eng.108, 493– 506 (2012)). Combined with the sensory and mouthfeel impact of removing ethanol, the loss of these flavor molecules results in an NA beer that is severely lacking in “beer-like” flavors and aromas. An additional disadvantage of physical dealcoholization methods is the requirement of specialized equipment that can be costly and is not typically found in breweries, presenting a substantial barrier of entry for small and medium sized breweries (Navrátil, M., Dömény, Z., Sturdík, E., Smogrovicová, D. & Gemeiner, P. Production of non-alcoholic beer using free and immobilized cells of Saccharomyces cerevisiae deficient in the tricarboxylic acid cycle. Biotechnol. Appl. Biochem.35, 133–140 (2002)). As an alternative to physical dealcoholization, arrested fermentation (AF) methods involve halting (arresting) the fermentation of the brewing wort before the concentration of ethanol exceeds a certain threshold (often around 0.5% ABV). In practice, this frequently means that the fermentation is stopped when sugar attenuation (the percent reduction in wort sugars due to consumption by yeast) reaches between 10% and 20%. In contrast, in a typical alcoholic beer fermentation, attenuation will be between 70% and 90% at the time that fermentation finishes. Because the amount of ethanol produced during fermentation is directly proportional to the amount of sugar that is consumed by yeast, an arrested fermentation in which only 10-20% of the sugar is consumed can be used to produce a beer with less than about 0.5% ABV. Methods to arrest yeast fermentation at a desired percent attenuation and ethanol concentration include, for example, cold contact fermentation and fermentation with a yeast strain unable to consume the sugars maltose and maltotriose. For cold contact fermentation, wort fermentation is performed with standard brewing yeast strains, but at low temperatures (~4˚C), and for short periods of time (24 – 48hrs) (A review of methods of low alcohol and alcohol-free beer production. J. Food Eng.108, 493–506 (2012)). Under these conditions, consumption of wort sugars is far less than in an alcoholic fermentation, and ethanol concentration can be kept below about 0.5% ABV. In the case of arrested fermentation using yeast strains unable to consume maltose and maltotriose, beer brewers use specialized strains of yeast that do not express the genes necessary to consume these sugars (Yabaci Karaoglan, S., Jung, R., Gauthier, M., Kinčl, T. & Dostálek, P. Maltose-Negative Yeast in Non-Alcoholic and Low-Alcoholic Beer Production. Fermentation 8, 273 (2022)). Maltose and maltotriose are composed of either two (maltose) or three (maltotriose) monomers of glucose, arranged in a linear chain via glycosidic bonds (FIG.1). As maltose and maltotriose comprise ~80-90% of the normally fermented sugars in brewing wort (He, Y. et al. Wort composition and its impact on the flavour-active higher alcohol and ester formation of beer – a review. J. Inst. Brew.120, 157–163 (2014); Jacques, K. A., Lyons, T. P. & Kelsall, D. R. The Alcohol Textbook: A Reference for the Beverage, Fuel and Industrial Alcohol Industries. (2003)), fermentation with these specialized strains allows brewers to limit wort attenuation to 10-20%, and the ethanol concentration can be kept under about 0.5% v / v. Within the brewing industry, yeast strains unable to consume maltose and maltotriose are frequently referred to as “maltose-negative” (MN) strains. Production of NA beers with MN yeasts does not require expensive or specialized equipment, therefore this type of arrested fermentation process is accessible to breweries of all sizes, however it has significant drawbacks. For example, non-alcoholic beers produced using currently available MN strains are often perceived as excessively sweet due to the high concentrations of unfermented sugars and lack beer-like flavors due to the reduced levels of flavor molecules produced by yeast during the arrested fermentation (Yabaci Karaoglan, S., Jung, R., Gauthier, M., Kinčl, T. & Dostálek, P. Maltose-Negative Yeast in Non-Alcoholic and Low-Alcoholic Beer Production. Fermentation 8, 273 (2022); Piornos, J. A. et al. Elucidating the Odor-Active Aroma Compounds in Alcohol-Free Beer and Their Contribution to the Worty Flavor. J. Agric. Food Chem. (2020) doi:10.1021 / acs.jafc.0c03902). Additionally, non-alcoholic beers produced using currently available MN strains have significant “worty” off-flavors and aromas that detract from the overall sensory profile. The genetically modified cells and methods of use thereof described herein are capable of producing non-alcoholic fermented products having reduced sensory detection of wort-associated off-flavors. In some embodiments, the genetically modified cells and methods of use thereof described herein result in production of molecules in the fermented product that mask the detection of the wort-associated off-flavors, e.g., increase the detection threshold of the off-flavors. As used herein, a “brewing yeast cell” or a “brewing yeast strain” refers to a yeast strain that has been selected by brewers to have certain properties that make it suitable for brewing alcoholic and non-alcoholic beverages, and that is genetically distinct from non- brewing yeast strains. Brewing yeast strains include strains of Saccharomyces cerevisiae whose genome sequence places them within the phylogenetic clades of “Beer 1”, “Beer 2”, or “Mixed” as defined in Gallone et al.2016 and Priess et al.2018. (PMIDs 27610566, 30258422). Alternatively, a brewing yeast strain can be a strain of the Saccharomyces pastorianus, a hybrid species that originated from a hybridization between strains of S. cerevisiae and S. eubayanus during brewing (PMID 26269586). In addition, brewing yeast strains have or are likely to have one or more of the following characteristics: 1) they are able to metabolize maltotriose, 2) their genomes contain alleles of PAD1 and FDC1 that have no / reduced function due to loss-of-function mutations, 3) their genomes encode the AGT1 allele of MAL11, and / or they display efficient growth on maltose and maltotriose media. In any of the embodiments of the present disclosure, a genetically modified yeast cell can be derived from a brewing yeast strain. Exemplary brewing yeast strains are disclosed further herein. As used herein, the term “wort -associated off-flavors” refers to undesired flavors and / or aromas that are associated with wort and limited fermentation of the wort with maltose negative yeast strains. For example, in some embodiments, wort-associated off-flavors may be described as cereal, potato, hay, stewed apples, or tomato. Without wishing to be bound by any particular theory, a collection of approximately 10 volatile aldehydes have been attributed with undesired wort-associated off-flavors in beer (Gernat, D. C., Brouwer, E. & Ottens, M. Aldehydes as Wort Off-Flavours in Alcohol-Free Beers—Origin and Control. Food Bioprocess Technol.13, 195–216 (2019); Piornos, J. A. et al. Elucidating the Odor- Active Aroma Compounds in Alcohol-Free Beer and Their Contribution to the Worty Flavor. J. Agric. Food Chem. (2020) doi:10.1021 / acs.jafc.0c03902). In some embodiments, the wort-associated off-flavors include aldehydes and non-aldehyde molecules. Examples of aldehydes and non-aldehyde molecules that contribute to the wort-associated off-flavors include, without limitation, 2-methylbutanal, 2-methylpropanal, hexanal, benzaldehyde, furfural, acetaldehyde, methional, phenylacetaldehyde, or 5-hydrox-methyl-furfural, (E)-beta- damascenone, or 5-ethyl-3-hydroxy-4-methyl-2(5H)-furanone. Maltose and / or maltotriose-negative (MN) yeast For the majority of Saccharomyces yeast strains, the ability to consume maltose and maltotriose is conferred by the expression of proteins that 1) transport maltose and maltotriose molecules into the cell, and 2) hydrolyze the glycosidic bond that joins individual glucose monomers within these di- and tri-saccharides (Needleman, R. B. Control of Maltase Synthesis in Yeast. (1975)). The result of these transport and hydrolytic activities is the release of glucose that can enter the yeast glycolytic pathway and be fermented. Most strains of Saccharomyces yeast express transport and glucosidase proteins that perform these two functions, and as a result most Saccharomyces yeasts are able to metabolize maltose, and to a slightly lesser extent, maltotriose (Gallone, B. et al. Domestication and Divergence of Saccharomyces cerevisiae Beer Yeasts. Cell 166, 1397–1410.e16 (2016); Warringer, J. et al. Trait variation in yeast is defined by population history. PLoS Genet.7, e1002111 (2011)). Brewing strains of Saccharomyces are, in fact, particularly adept at maltose and maltotriose consumption, owing to centuries of use in brewing during which these strains acquired adaptations – frequently duplications of maltose transport and glucosidase genes – that allowed them to rapidly ferment the maltose and maltotriose in brewing wort (Gallone, B. et al. Domestication and Divergence of Saccharomyces cerevisiae Beer Yeasts. Cell 166, 1397– 1410.e16 (2016)). Because most Saccharomyces yeast strains, and nearly all Saccharomyces strains used in brewing, are able to consume maltose and maltotriose, brewers have few brewing yeast strains available to choose from that are not capable of fermenting maltose and / or maltotriose to ethanol when producing non-alcoholic beers using arrested fermentation. This dearth of maltose-negative brewing strains creates a significant challenge for brewers, as non- Saccharomyces yeast and even non-brewing strains of Saccharomyces yeast have characteristics that make them poorly suited for beer fermentation, such as poor flocculation activity, and the production of undesirable flavor molecules. While there has been some interest in screening strains of non-brewing yeasts to identify potential strains that are both MN and well suited for beer production, few promising strains have been identified (Yabaci Karaoglan, S., Jung, R., Gauthier, M., Kinčl, T. & Dostálek, P. Maltose-Negative Yeast in Non-Alcoholic and Low-Alcoholic Beer Production. Fermentation 8, 273 (2022)). As a result, most arrested fermentation of non-alcoholic beer production with maltose-negative yeasts relies on non-brewing strains that have flavor or performance characteristics that negatively impact the quality of the resulting beer (Yabaci Karaoglan, S., Jung, R., Gauthier, M., Kinčl, T. & Dostálek, P. Maltose-Negative Yeast in Non-Alcoholic and Low-Alcoholic Beer Production. Fermentation 8, 273 (2022); Simões, J. et al. Exploiting Non-Conventional Yeasts for Low-Alcohol Beer Production. Microorganisms 11, (2023)). In some embodiments, the modified cell is naturally incapable of converting maltose and / or maltotriose to ethanol (e.g., a naturally maltose-negative strain). In some embodiments, the modified cell is incapable of or has a reduced capability of converting maltose and / or maltotriose to ethanol due to mating of the cell with a strain of yeast that is incapable of converting maltose and / or maltotriose to ethanol. In some embodiments, a genetically modified yeast cell incapable of or having a reduced capability of converting maltose and / or maltotriose to ethanol comprises a heterologous nucleic acid encoding an enzyme having alcohol acyltransferase (EC 2.3.1.84) activity. As used herein a “genetically modified yeast cell” is used interchangeably with “modified cell.” As used herein, a reduced capability of converting maltose and / or maltotriose to ethanol refers to a reduction in the conversion of maltose and / or maltotriose to ethanol. By way of example, but not limitation, such reduced capability can be a reduction of at least about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 98%, 99% or more as compared to the yeast cell strain from which the genetically modified yeast cell is derived fermented under the same conditions. In some embodiments, the genetically modified yeast cell is incapable of converting maltose and / or maltotriose to ethanol. In some embodiments, the modified cell comprises one or more genetic modifications to functionally disrupt one or more proteins associated with maltose and / or maltotriose transport into the modified cell. Genes encoding these maltose transporter proteins could include any one or more of MAL31, MAL11, MPH2, MPH3, MAL21, MAL41, MA61, and AGT1 (PMIDs 9925567, 16332759). While the nucleotide sequence of any of these genes may differ across distinct yeast strains, these genes can be identified by one skilled in the art by sequence homology search using well characterized reference sequences as queries. In some embodiments, the modified cell comprises one or more genetic modifications to functionally disrupt one or more proteins associated with maltose and / or maltotriose hydrolysis by the modified cell. Genes encoding proteins involved in maltose hydrolysis include MAL11, MAL12, MAL13, MAL14, MAL16 and STA1 (PMIDs 11598808, 31346683). While the nucleotide sequence of any of these genes may differ across distinct yeast strains, these genes can be identified by one skilled in the art by sequence homology search using well characterized reference sequences as queries. In some embodiments, the modified cell comprises one or more genetic modifications to functionally disrupt a maltose and / or maltotriose transporter. In some embodiments, the modified cell is genetically modified to be deficient in MAL31 and MAL11 (AGT1). Methods of functionally disrupting genes in yeast cells are known in the art. The amino acid sequence of MAL31, a maltose transporter from Saccharomyces cerevisiae is provided by the amino acid sequence set forth by SEQ ID NO: 1. The nucleic acid sequence of MAL31 is provided by the amino acid sequence set forth by SEQ ID NO: 2. The amino acid sequence of AGT1, also referred to as MAL11, a maltose transporter from Saccharomyces cerevisiae is provided by the amino acid sequence set forth by SEQ ID NO: 3. The nucleic acid sequence of AGT1 is provided by the amino acid sequence set forth by SEQ ID NO: 4. Production of acetate esters and / or ethyl esters Aspects of the present disclosure relate to modified cells comprising a genetic modification to reduce sensory detection of one or more wort-associated off-flavors that results in increased production of one or more acetate esters and / or ethyl esters as compared to a cell that does not comprise the genetic modification(s). Worty flavors in arrested fermentation beer are a result of the presence of a combination of aldehyde and non-aldehydic molecules. These aldehyde molecules are present in the unfermented wort, and during a normal alcoholic fermentation, the yeast either convert them into other molecules that do not impart flavor, or sufficiently alter the chemical composition of the beer through the production of ethanol and other flavor molecules such that these molecules are no longer perceptible. In contrast, in an arrested fermentation with maltose-negative strains, it is thought that one or both of these processes do not occur or occur at reduced levels, hence the aldehydes are present and very perceptible as off-flavors in the finished beer. Esters generally add a fresh fruity aroma to beverages. Ethyl acetate, isoamyl acetate, and phenethyl acetate are three acetate esters generally produced by yeast during the course of a typical beer fermentation and are thought to be major contributors to the “beer-like” aroma and flavor of alcoholic beer. In excessive amounts, they can also lead to undesirable off-flavors. During arrested fermentation, far lower (i.e. insufficient) levels of these acetate esters are produced due to the reduced levels of wort attenuation and yeast metabolic activity, thus exacerbating the increased presence and perception of aldehyde and non-aldehydic- based off-flavors. Accordingly, also provided herein are genetically modified yeast cell compositions and methods to genetically modify yeast cells to produce a well-balanced volatile ester profile, important for achieving a desirable sensory profile for NA beverages, even in an arrested fermentation where yeast metabolic activity is reduced relative to normal alcoholic fermentation. Non-limiting examples of acetate esters that may reduce sensory detection of one or more wort-associated off-flavors include ethyl acetate, isoamyl acetate, phenethyl acetate, and hexyl acetate. Non-limiting examples of ethyl esters that may reduce sensory detection of one or more wort-associated off-flavors include ethyl hexanoate, ethyl octanoate, and ethyl decanoate. In some embodiments, the modified cells overexpress an enzyme having alcohol acyltransferase (AAT) activity. In some embodiments, the modified cells express a heterologous gene encoding an enzyme having alcohol acetyltransferase (AAT) activity. The term “heterologous gene,” as used herein, refers to a sequence of nucleic acid (e.g., DNA) that contains the genetic instruction, which is introduced into and expressed by a host organism (e.g., a genetically modified cell) which does not naturally encode the introduced gene. The heterologous gene may encode an enzyme that is not typically expressed by the cell, a variant of an enzyme that the cell does not typically express (e.g., a mutated enzyme), an additional copy of a gene encoding an enzyme that is typically expressed in the cell, or a gene encoding an enzyme that is typically expressed by the cell but under different regulation. In some embodiments, the modified cells express an endogenous gene at a level that is increased as compared to expression in a counterpart cell that is not genetically modified. In some embodiments, the heterologous gene encoding an enzyme with glycosidase activity is a wild-type (naturally occurring) AAT (e.g., a gene isolated from an organism). The term “heterologous nucleic acid” as used herein refers to a nucleic acid wherein at least one of the following is true: (a) the nucleic acid is foreign (“exogenous”) to (that is, not naturally found in) a given host cell; (b) the nucleic acid comprises a nucleotide sequence that is naturally found in (that is, is “endogenous to”) a given host cell, but the nucleotide sequence is present in an unnatural amount in the cell (for example, greater than expected or greater than naturally found); (c) the nucleic acid comprises a nucleotide sequence that differs in sequence from an endogenous nucleotide sequence, but the nucleotide sequence encodes the same protein (having the same or substantially the same amino acid sequence) and is present in an unnatural amount in the cell (for example, greater than expected or greater than naturally found); or (d) the nucleic acid comprises two or more nucleotide sequences that are not found in the same relationship to each other in nature (for example, the nucleic acid is recombinant). In some embodiments, the enzyme having AAT activity is obtained from a yeast. In some embodiments, the enzyme having AAT activity is obtained from a bacterium. In some embodiments, the enzyme having AAT activity is obtained from a plant. In some embodiments, the enzyme having AAT activity is obtained from a yeast or fungus. In some embodiments, the enzyme having AAT activity is derived from Saccharomyces cerevisiae. In some embodiments, the genetically modified yeast cell produces an increased amount of one or more acetate esters and / or ethyl esters compared to a cell that does not comprise the heterologous nucleic acid. In some embodiments, the genetically modified yeast cell produces an increased amount of one or more acetate esters compared to a cell that does not comprise the heterologous nucleic acid. In some embodiments, the genetically modified yeast cell produces an increased amount of one or more ethyl esters compared to a cell that does not comprise the heterologous nucleic acid. In some embodiments, the genetically modified yeast cell produces an increased amount of one or more acetate esters and one or more ethyl esters compared to a cell that does not comprise the heterologous nucleic acid. In some embodiments, the one or more acetate esters are selected from the group consisting of ethyl acetate, isoamyl acetate, phenethyl acetate, hexyl acetate, and combinations thereof. In some embodiments, the one or more acetate esters comprise ethyl acetate, isoamyl acetate, and phenethyl acetate. In some embodiments, the one or more acetate esters comprise isoamyl acetate and phenethyl acetate. In some embodiments, the one or more acetate esters comprise isoamyl acetate. In some embodiments, the one or more acetate esters comprise phenethyl acetate. In some embodiments, the one or more ethyl esters are selected from the group consisting of ethyl hexanoate, ethyl octanoate, ethyl decanoate, and combinations thereof. In some embodiments, the one or more ethyl esters comprise ethyl hexanoate, ethyl octanoate and ethyl decanoate. In some embodiments, the one or more ethyl esters comprise ethyl hexanoate and ethyl octanoate. In some embodiments, the one or more ethyl esters comprise ethyl hexanoate and ethyl decanoate. In some embodiments, the one or more ethyl esters comprise ethyl octanoate and ethyl decanoate. In some embodiments, the one or more ethyl esters comprise ethyl hexanoate. In some embodiments, the one or more ethyl esters comprise ethyl octanoate. In some embodiments, the one or more ethyl esters comprise ethyl decanoate. An exemplary enzyme having AAT activity is ATF1 from Saccharomyces cerevisiae. The Saccharomyces cerevisiae ATF1 is provided by the amino acid sequence set forth by SEQ ID NO: 5. An exemplary nucleic acid sequence of ATF1 is provided by SEQ ID NO: 6. An exemplary enzyme having AAT activity is AAT1 from Cucumis melo. The Cucumis melo AAT1 is provided by the amino acid sequence set forth by SEQ ID NO: 7. An exemplary nucleic acid sequence of AAT1 of C. melo is provided by SEQ ID NO: 8. Other examples of enzymes having AAT activity useful for the compositions and methods provided herein include, but are not limited to those described by GenBank accession numbers: NP_001315675.1 (SEQ ID NO: 36), ABO21021.1 (SEQ ID NO: 37), WP_011783747.1 (SEQ ID NO: 38), XP_008462821.2 (SEQ ID NO: 39), EGA72844.1 (SEQ ID NO: 40), NP_011693.1 (SEQ ID NO: 41), NP_011529.1 (SEQ ID NO: 42), ADD16960.1 (SEQ ID NO: 43), AHY74654.1 (SEQ ID NO: 44), NP_001310384.1 (SEQ ID NO: 45), ACT82247.1 (SEQ ID NO: 46), AAG13130.1 (SEQ ID NO: 47), NP_001315389.1 (SEQ ID NO: 48), NP_001295454.1 (SEQ ID NO: 49), AAW31948.1 (SEQ ID NO: 50), XP_007209131.1 (SEQ ID NO: 51), A0A2R6Q326.2 (SEQ ID NO: 52), CAB4309439.1 (SEQ ID NO: 53), P0DO25.1 (SEQ ID NO: 54), WP_004922247.1 (SEQ ID NO: 55), and WP_004920769.1 (SEQ ID NO: 56). In some embodiments, the cell that expresses the AAT enzyme is capable of increased production of acetate esters and / or ethyl esters as compared to a cell that does not express the AAT or expresses the AAT at a lower level (e.g., a cell that has not been genetically modified). In some embodiments, the cell that expresses the AAT enzyme is capable of increased production of acetate esters and / or ethyl esters in a fermented product as compared to a fermented product that is not produced with the modified cells. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence set forth in any one of SEQ ID NOs: 5, 7 and 36-56. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 5. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 7. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 36. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 37. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 38. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 39. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 40. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 41. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 42. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 43. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 44. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 45. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 46. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 47. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 48. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 49. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 50. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 51. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 52. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 53. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 54. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 55. In some embodiments, the enzyme with AAT activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 56. The terms “percent identity,” “sequence identity,” “% identity,” “% sequence identity,” and % identical,” as they may be interchangeably used herein, refer to a quantitative measurement of the similarity between two sequences (e.g., nucleic acid or amino acid). Percent identity can be determined using the algorithms of Karlin and Altschul, Proc. Natl. Acad. Sci. USA 87:2264-68, 1990, modified as in Karlin and Altschul, Proc. Natl. Acad. Sci. USA 90:5873-77, 1993. Such algorithms are incorporated into the NBLAST and XBLAST programs (version 2.0) of Altschul et al., J. Mol. Biol.215:403-10, 1990. BLAST protein searches can be performed with the XBLAST program, score=50, word length=3, to obtain amino acid sequences homologous to the protein molecules of interest. Where gaps exist between two sequences, Gapped BLAST can be utilized as described in Altschul et al., Nucleic Acids Res.25(17):3389-3402, 1997. When utilizing BLAST and Gapped BLAST programs, the default parameters of the respective programs (e.g., XBLAST and NBLAST) can be used. When a percent identity is stated, or a range thereof (e.g., at least, more than, etc.), unless otherwise specified, the endpoints shall be inclusive and the range (e.g., at least 70% identity) shall include all ranges within the cited range (e.g., at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5% ,at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9% identity) and all increments thereof (e.g., tenths of a percent (i.e., 0.1%), hundredths of a percent (i.e., 0.01%), etc.). In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in any one of SEQ ID NO: 5, 7 or 36-56. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 5. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 7. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 36. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 37. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 38. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 39. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 40. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 41. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 42. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 43. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 44. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 45. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 46. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 47. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 48. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 49. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 50. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 51. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 52. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 53. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 54. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 55. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 56. In some embodiments, the enzyme with AAT activity comprises the amino acid sequence as set forth in SEQ ID NO: 5 or 7. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in any one of SEQ ID NO: 5, 7 or 36-56. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 5. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 7. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 36. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 37. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 38. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 39. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 40. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 41. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 42. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 43. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 44. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 45. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 46. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 47. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 48. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 49. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 50. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 51. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 52. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 53. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 54. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 55. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 56. In some embodiments, the enzyme with AAT activity consists of the amino acid sequence as set forth in SEQ ID NO: 5 or 7. In some embodiments, the gene encoding the enzyme with AAT activity comprises a nucleic acid sequence which encodes an enzyme comprising an amino acid sequence with at least 80% (e.g., at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9%) sequence identity to the sequence as set forth in any one of SEQ ID NOs: 5, 7 or 36-56. In some embodiments, the gene encoding the enzyme with AAT activity comprises a nucleic acid sequence which encodes an enzyme consisting of an amino acid sequence as set forth in any one of SEQ ID NOs: 5, 7 or 36-56. In some embodiments, the gene encoding the enzyme with AAT activity comprises a nucleic acid sequence with at least 80% (e.g., at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9%) sequence identity to the sequence as set forth in SEQ ID NO: 6 or 8. In some embodiments, the gene encoding the enzyme with AAT activity comprises a nucleic acid sequence consisting of an amino acid sequence as set forth in SEQ ID NO: 6 or 8. Identification of additional enzymes having AAT activity or predicted to have AAT activity may be performed, for example based on similarity or homology with one or more domains of an AAT, such as the AATs provided by any one of SEQ ID NOs: 5, 7 and 36-56. In some embodiments, an enzyme for use in the modified cells and methods described herein may be identified based on similarity or homology with an active domain, such as a catalytic domain, such as a catalytic domain associated with AAT activity. In some embodiments, an enzyme for use in the modified cells and methods described herein may have a relatively high level of sequence identity with a reference AAT, e.g., a wild-type AAT, such as any one of SEQ ID NOs: 5, 7 or 36-56, in the region of the catalytic domain but a relatively low level of sequence identity to the reference AAT based on analysis of a larger portion of the enzyme or across the full length of the enzyme. In some embodiments, the enzyme for use in the modified cells and methods described herein has at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9% sequence identity in the region of the catalytic domain of the enzyme relative to a reference AAT (e.g., SEQ ID NO: 5, 7 or 36-56). In some embodiments, an enzyme for use in the modified cells and methods described herein has a relatively high level of sequence identity in the region of the catalytic domain of the enzyme relative to a reference AAT (e.g., SEQ ID NO: 5, 7 or 36-56) and a relatively low level of sequence identity to the reference AAT based on analysis of a larger portion of the enzyme or across the full length of the enzyme. In some embodiments, the enzymes for use in the modified cells and methods described herein have at least 10%, at least 15%, at least 20%, at least 25%, least 30% at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9% sequence identity based on a portion of the enzyme or across the full length of the enzyme relative to a reference AAT (e.g., SEQ ID NO: 5, 7 or 36-56). Production of 3-mercaptohexanol Aspects of the present disclosure relate to modified cells comprising a genetic modification to reduce sensory detection of one or more wort-associated off-flavors results in increased production of 3-mercaptohexanol (3MH) as compared to a cell that does not comprise the genetic modification(s). 3MH is a volatile thiol molecule that is generally produced in yeast at very low levels (<50 ng / L) during beer fermentation. In some embodiments, the modified cell further comprises a heterologous nucleic acid encoding an enzyme having carbon-sulfur-lyase (EC 4.4) activity. In some embodiments, the modified cells overexpress an enzyme having carbon- sulfur lyase (CSL) activity. In some embodiments, the modified cells express a heterologous gene encoding an enzyme having CSL activity. In some embodiments, any of the modified cells described herein are genetically modified to express a heterologous gene encoding an enzyme having CSL activity. In some embodiments, the heterologous gene encoding an enzyme with CSL activity is a wild-type CSL gene (e.g., a gene isolated from an organism). In some embodiments, the CSL is obtained from a bacterium, a fungus, or a plant. In some embodiments, the CSL is obtained from a bacterium. In some embodiments, the enzyme having CSL activity is derived from Citrobacter freundii. The Citrobacter freundii derived CSL is provided by the amino acid sequence set forth by SEQ ID NO: 9. An exemplary nucleic acid sequence CSL of C. freundii is provided by SEQ ID NO: 10. Other examples of enzymes having CSL activity useful for the compositions and methods provided herein include, but are not limited to those referenced by GenBank accession numbers: WP_125339275.1 (SEQ ID NO: 57), WP_105310552.1 (SEQ ID NO: 58), WP_119633472.1 (SEQ ID NO: 59), EDN59205.1 (SEQ ID NO: 60), WP_094789495.1 (SEQ ID NO: 61), and XP_025427068.1 (SEQ ID NO: 62). In some embodiments, the heterologous gene encodes an enzyme with CSL activity such that a cell that expresses the enzyme is capable of increased production of 3- mercaptohexanol (3MH). In some embodiments, the heterologous gene encodes an enzyme with CSL activity such that a cell that expresses the enzyme is capable of increased production of 3MH as compared to a cell that does not express the heterologous gene. In some embodiments, the enzyme with CSL activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in any one of SEQ ID NOs: 9 and 57-62. In some embodiments, the enzyme with CSL activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 9. In some embodiments, the enzyme with CSL activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 57. In some embodiments, the enzyme with CSL activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 58. In some embodiments, the enzyme with CSL activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 59. In some embodiments, the enzyme with CSL activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 60. In some embodiments, the enzyme with CSL activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 61. In some embodiments, the enzyme with CSL activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 62. In some embodiments, the enzyme with CSL activity comprises the amino acid sequence as set forth in any one of SEQ ID NOs: 9 and 57-62. In some embodiments, the enzyme with CSL activity comprises the amino acid sequence as set forth in SEQ ID NO: 9. In some embodiments, the enzyme with CSL activity comprises the amino acid sequence as set forth in SEQ ID NO: 57. In some embodiments, the enzyme with CSL activity comprises the amino acid sequence as set forth in SEQ ID NO: 58. In some embodiments, the enzyme with CSL activity comprises the amino acid sequence as set forth in SEQ ID NO: 59. In some embodiments, the enzyme with CSL activity comprises the amino acid sequence as set forth in SEQ ID NO: 60. In some embodiments, the enzyme with CSL activity comprises the amino acid sequence as set forth in SEQ ID NO: 61. In some embodiments, the enzyme with CSL activity comprises the amino acid sequence as set forth in SEQ ID NO: 62. In some embodiments, the enzyme with CSL activity consists of the amino acid sequence as set forth in any one of SEQ ID NOs: 9 and 57-62. In some embodiments, the enzyme with CSL activity consists of the amino acid sequence as set forth in SEQ ID NO: 9. In some embodiments, the enzyme with CSL activity consists of the amino acid sequence as set forth in SEQ ID NO: 57. In some embodiments, the enzyme with CSL activity consists of the amino acid sequence as set forth in SEQ ID NO: 58. In some embodiments, the enzyme with CSL activity consists of the amino acid sequence as set forth in SEQ ID NO: 59. In some embodiments, the enzyme with CSL activity consists of the amino acid sequence as set forth in SEQ ID NO: 60. In some embodiments, the enzyme with CSL activity consists of the amino acid sequence as set forth in SEQ ID NO: 61. In some embodiments, the enzyme with CSL activity consists of the amino acid sequence as set forth in SEQ ID NO: 62. In some embodiments, the gene encoding the enzyme with CSL activity comprises a nucleic acid sequence which encodes an enzyme comprising an amino acid sequence with at least 80% (e.g., at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9%) sequence identity to the sequence as set forth in any one of SEQ ID NOs: 9 and 57-62. In some embodiments, the gene encoding the enzyme with CSL activity comprises a nucleic acid sequence which encodes an enzyme consisting of an amino acid sequence as set forth in any one of SEQ ID NOs: 9 and 57-62. In some embodiments, the gene encoding the enzyme with CSL activity comprises a nucleic acid sequence as set forth in SEQ ID NO: 10. Identification of additional enzymes having CSL activity or predicted to have CSL activity may be performed, for example based on similarity or homology with one or more domains of a CSL, such as the CSL provided by SEQ ID NO: 9 or 57-62. In some embodiments, an enzyme for use in the modified cells and methods described herein may be identified based on similarity or homology with an active domain, such as a catalytic domain, such as a catalytic domain associated with CSL activity. In some embodiments, an enzyme for use in the modified cells and methods described herein may have a relatively high level of sequence identity with a reference CSL, e.g., a wild-type CSL, such as SEQ ID NO: 9 or 57- 62, in the region of the catalytic domain but a relatively low level of sequence identity to the reference CSL based on analysis of a larger portion of the enzyme or across the full length of the enzyme. In some embodiments, the enzyme for use in the modified cells and methods described herein has at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9% sequence identity in the region of the catalytic domain of the enzyme relative to a reference CSL (e.g., SEQ ID NO: 9 or 57-62). In some embodiments, an enzyme for use in the modified cells and methods described herein have a relatively high level of sequence identity in the region of the catalytic domain of the enzyme relative to a reference CSL (e.g., SEQ ID NO: 9 or 57-62) and a relatively low level of sequence identity to the reference CSL based on analysis of a larger portion of the enzyme or across the full length of the enzyme. In some embodiments, the enzymes for use in the modified cells and methods described herein have at least 10%, at least 15%, at least 20%, at least 25%, least 30% at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9% sequence identity based on a portion of the enzyme or across the full length of the enzyme relative to a reference CSL (e.g., SEQ ID NO: 9 or 57-62). Production of monoterpenes Aspects of the present disclosure relate to modified cells comprising a genetic modification to reduce sensory detection of one or more wort-associated off-flavors results in increased production one or more monoterpenes as compared to a cell that does not comprise the genetic modification(s). In some embodiments, the one or more monoterpenes include linalool, geraniol, and / or citronellol. Genetic modification of brewing yeast to produce monoterpenes such as linalool, geraniol, and citronellol have been described, for example in PCT Publication No. WO 2017 / 100655A1, which is incorporated by reference herein in its entirety. In some embodiments, the modified cell is further genetically modified to produce one or more monoterpenes. In some embodiments, the monoterpene is selected from the group consisting of linalool, geraniol, and citronellol. In some embodiments, the modified cell expresses one or more (e.g., 1, 2, 3, or 4) of (a) a truncated variant of a yeast HMG1 enzyme; (b) a variant of ERG20 enzyme; (c) a linalool synthase; and / or (d) a geraniol synthase. In some embodiments, the modified cell expresses (a) a truncated variant of a yeast HMG1 enzyme; (b) a variant of ERG20 enzyme; (c) a linalool synthase; and (d) a geraniol synthase. In some embodiments, the modified cell comprises a heterologous nucleic acid encoding an enzyme selected from the group consisting of (a) a truncated variant of a yeast HMG1 enzyme, (b) a variant of ERG20 enzyme or enzyme having farnesyl diphosphate synthase activity, (c) a linalool synthase, (d) a geraniol synthase, and (e) combinations thereof. In some embodiments, the modified cell comprises a heterologous nucleic acid encoding: (a) a truncated variant of a yeast HMG1 enzyme, (b) a variant of ERG20 enzyme or enzyme having farnesyl diphosphate synthase activity, (c) a linalool synthase, and (d) a geraniol synthase. In some embodiments, the modified cell comprises a heterologous nucleic acid encoding an enzyme selected from the group consisting of (a) a truncated variant of a yeast HMG1 enzyme, (b) a variant of ERG20 enzyme, (c) a linalool synthase, (d) a geraniol synthase, and (e) combinations thereof. In some embodiments, the modified cell comprises a heterologous nucleic acid encoding: (a) a truncated variant of a yeast HMG1 enzyme, (b) a variant of ERG20 enzyme, (c) a linalool synthase, and (d) a geraniol synthase. Enzyme having HMG-CoA reductase activity In some embodiments, any of the modified cells described herein are genetically modified to express a heterologous gene encoding an enzyme having HMG-CoA reductase activity (3'-hydroxy- 3-methylglutaryl-coenzyme A reductase). In some embodiments, the heterologous gene encoding an enzyme with HMG-CoA reductase activity is a wild-type HMG1 gene (e.g., a gene isolated from an organism). In some embodiments, the enzyme with HMG-CoA reductase activity is obtained from a bacterium, a fungus, or a plant. In some embodiments, the enzyme with HMG-CoA reductase activity is obtained from a yeast. In some embodiments, the enzyme with HMG-CoA reductase activity is a truncated variant of an enzyme with HMG-CoA reductase activity. In some embodiments, the enzyme having HMG-CoA reductase activity is a truncated variant of a yeast HMG1 enzyme. As used herein “truncated” with respect to a HMG1 enzyme or HMG-CoA reductase enzyme refers to an enzyme that is truncated relative to the full enzyme sequence. For example, the truncated sequence can be shorter than the full reference sequence by about 5%, 10%, 20%, 30%, 40%, 50% or more. By way of further example, but not limitation, the truncated enzyme can be shortened by about 500 amino acids from the reference enzyme. In some embodiments, the truncation can be an N-terminal truncation. As used herein, a “variant” enzyme refers to an enzyme that has a different sequence than the original sequence within at least 85%, 90%, 95%, 98%, or 99% sequence identity to the reference sequence, but retains the functional property of the reference enzyme, albeit the level of activity may be increased or reduced. The truncated HMG-CoA reductase enzyme (referred to as tHMG) is provided by the amino acid sequence set forth by SEQ ID NO: 11. An exemplary nucleic acid sequence of a truncated HMG-CoA reductase enzyme is provided by SEQ ID NO: 12. In some embodiments, the heterologous gene encodes an enzyme with HMG-CoA reductase activity such that a cell that expresses the enzyme is capable of increased production of one or more monoterpenes. In some embodiments, the heterologous gene encodes an enzyme with HMG-CoA reductase activity such that a cell that expresses the enzyme is capable of increased production of one or more monoterpenes as compared to a cell that does not express the heterologous gene. In some embodiments, the enzyme with HMG-CoA reductase activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 11. In some embodiments, the enzyme with HMG-CoA reductase activity comprises the amino acid sequence as set forth in SEQ ID NO: 11. In some embodiments, the enzyme with HMG-CoA reductase activity consists of the amino acid sequence as set forth in SEQ ID NO: 11. In some embodiments, the gene encoding the enzyme with HMG-CoA reductase activity comprises a nucleic acid sequence which encodes an enzyme comprising an amino acid sequence with at least 80% (e.g., at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9%) sequence identity to the sequence as set forth in SEQ ID NO: 11. In some embodiments, the gene encoding the enzyme with HMG-CoA reductase activity comprises a nucleic acid sequence which encodes an enzyme consisting of an amino acid sequence as set forth in SEQ ID NO: 11. In some embodiments, the gene encoding the enzyme with HMG-CoA reductase activity comprises a nucleic acid sequence as set forth in SEQ ID NO: 12. Identification of additional enzymes having HMG-CoA reductase activity or predicted to have HMG-CoA reductase activity may be performed, for example based on similarity or homology with one or more domains of a HMG-CoA reductase, such as the HMG-CoA reductase provided by SEQ ID NO: 11. In some embodiments, an enzyme for use in the modified cells and methods described herein may be identified based on similarity or homology with an active domain, such as a catalytic domain, such as a catalytic domain associated with HMG-CoA reductase activity. In some embodiments, an enzyme for use in the modified cells and methods described herein may have a relatively high level of sequence identity with a reference HMG-CoA reductase, e.g., a wild-type HMG-CoA reductase in the region of the catalytic domain but a relatively low level of sequence identity to the reference HMG-CoA reductase based on analysis of a larger portion of the enzyme or across the full length of the enzyme. In some embodiments, the enzyme for use in the modified cells and methods described herein has at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9% sequence identity in the region of the catalytic domain of the enzyme relative to a reference HMG-CoA reductase (e.g., SEQ ID NO: 11). In some embodiments, an enzyme for use in the modified cells and methods described herein have a relatively high level of sequence identity in the region of the catalytic domain of the enzyme relative to a reference HMG-CoA reductase (e.g., SEQ ID NO: 11) and a relatively low level of sequence identity to the reference HMG-CoA reductase based on analysis of a larger portion of the enzyme or across the full length of the enzyme. In some embodiments, the enzymes for use in the modified cells and methods described herein have at least 10%, at least 15%, at least 20%, at least 25%, least 30% at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9% sequence identity based on a portion of the enzyme or across the full length of the enzyme relative to a reference HMG-CoA reductase (e.g., SEQ ID NO: 11). Enzyme having farnesyl diphosphate synthase (FPPS) activity In some embodiments, any of the modified cells described herein are genetically modified to express a heterologous gene encoding an enzyme having farnesyl diphosphate synthase activity. In some embodiments, the heterologous gene encoding an enzyme with farnesyl diphosphate synthase activity is a wild-type farnesyl diphosphate synthase gene (e.g., a gene isolated from an organism). In some embodiments, the enzyme with farnesyl diphosphate synthase reductase activity is obtained from a bacterium, a fungus, or a plant. In some embodiments, the enzyme with farnesyl diphosphate synthase reductase activity is obtained from a yeast. In some embodiments, the enzyme with farnesyl diphosphate synthase activity is a variant of an enzyme with farnesyl diphosphate synthase activity, e.g., a mutant that comprises one or more amino acid substitutions at any of positions F96, N127, and / or K197. In some embodiments, the enzyme having farnesyl diphosphate synthase activity is a variant of a farnesyl diphosphate synthase having a substitution mutation at positions F96 and N127, e.g., F96W and N127W. The farnesyl diphosphate synthase enzyme is provided by the amino acid sequence set forth by SEQ ID NO: 13, referred to as ERG20 (F96W,N127W). An exemplary nucleic acid sequence of a farnesyl diphosphate synthase enzyme (ERG20 (F96W,N127W)) is provided by SEQ ID NO: 14. In some embodiments, the heterologous gene encodes an enzyme with farnesyl diphosphate synthase activity such that a cell that expresses the enzyme is capable of increased production of one or more monoterpenes. In some embodiments, the heterologous gene encodes an enzyme with farnesyl diphosphate synthase activity such that a cell that expresses the enzyme is capable of increased production of one or more monoterpenes as compared to a cell that does not express the heterologous gene. In some embodiments, the enzyme with farnesyl diphosphate synthase activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 13. In some embodiments, the enzyme with farnesyl diphosphate synthase activity comprises the amino acid sequence as set forth in SEQ ID NO: 13. In some embodiments, the enzyme with farnesyl diphosphate synthase activity consists of the amino acid sequence as set forth in SEQ ID NO: 13. In some embodiments, the gene encoding the enzyme with farnesyl diphosphate synthase activity comprises a nucleic acid sequence which encodes an enzyme comprising an amino acid sequence with at least 80% (e.g., at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9%) sequence identity to the sequence as set forth in SEQ ID NO: 13. In some embodiments, the gene encoding the enzyme with farnesyl diphosphate synthase activity comprises a nucleic acid sequence which encodes an enzyme consisting of an amino acid sequence as set forth in SEQ ID NO: 13. In some embodiments, the gene encoding the enzyme with farnesyl diphosphate synthase activity comprises a nucleic acid sequence as set forth in SEQ ID NO: 14. Identification of additional enzymes having farnesyl diphosphate synthase activity or predicted to have farnesyl diphosphate synthase activity may be performed, for example based on similarity or homology with one or more domains of a farnesyl diphosphate synthase, such as the farnesyl diphosphate synthase provided by SEQ ID NO: 13. In some embodiments, an enzyme for use in the modified cells and methods described herein may be identified based on similarity or homology with an active domain, such as a catalytic domain, such as a catalytic domain associated with farnesyl diphosphate synthase activity. In some embodiments, an enzyme for use in the modified cells and methods described herein may have a relatively high level of sequence identity with a reference farnesyl diphosphate synthase, e.g., in the region of the catalytic domain but a relatively low level of sequence identity to the reference farnesyl diphosphate synthase based on analysis of a larger portion of the enzyme or across the full length of the enzyme. In some embodiments, the enzyme for use in the modified cells and methods described herein has at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9% sequence identity in the region of the catalytic domain of the enzyme relative to a reference farnesyl diphosphate synthase (e.g., SEQ ID NO: 13). In some embodiments, an enzyme for use in the modified cells and methods described herein have a relatively high level of sequence identity in the region of the catalytic domain of the enzyme relative to a reference farnesyl diphosphate synthase (e.g., SEQ ID NO: 13) and a relatively low level of sequence identity to the reference farnesyl diphosphate synthase based on analysis of a larger portion of the enzyme or across the full length of the enzyme. In some embodiments, the enzymes for use in the modified cells and methods described herein have at least 10%, at least 15%, at least 20%, at least 25%, least 30% at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9% sequence identity based on a portion of the enzyme or across the full length of the enzyme relative to a reference farnesyl diphosphate synthase (e.g., SEQ ID NO: 13). Enzyme having linalool synthase activity In some embodiments, any of the modified cells described herein are genetically modified to express a heterologous gene encoding an enzyme having linalool synthase activity. In some embodiments, the heterologous gene encoding an enzyme with linalool synthase activity is a wild-type linalool synthase gene (e.g., a gene isolated from an organism). In some embodiments, the enzyme with linalool synthase activity is obtained from a bacterium, a fungus, or a plant. In some embodiments, the enzyme with linalool synthase activity is obtained from a yeast. In some embodiments, the enzyme having linalool synthase activity is from Mentha citrate (referred to as McLIS). The linalool synthase enzyme is provided by the amino acid sequence set forth by SEQ ID NO: 15. An exemplary nucleic acid sequence of a linalool synthase enzyme is provided by SEQ ID NO: 16. Other examples of enzymes having linalool synthase activity useful for the compositions and methods provided herein include, but are not limited those referenced by the GenBank accession numbers: Q8H2B4.1 (SEQ ID NO: 63), Q6ZH94 (SEQ ID NO: 64), Q96376 (SEQ ID NO: 65), MN954676 (SEQ ID NO: 66), Q84ZW8.2 (SEQ ID NO: 67), A0A348B793.1 (SEQ ID NO: 68). In some embodiments, the heterologous gene encodes an enzyme with linalool synthase activity such that a cell that expresses the enzyme is capable of increased production of one or more monoterpenes. In some embodiments, the heterologous gene encodes an enzyme with linalool synthase activity such that a cell that expresses the enzyme is capable of increased production of one or more monoterpenes as compared to a cell that does not express the heterologous gene. In some embodiments, the enzyme with linalool synthase activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity a sequence selected from the group consisting of SEQ ID NOs: 15 and 63-68. In some embodiments, the enzyme with linalool synthase activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 15. In some embodiments, the enzyme with linalool synthase activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 63. In some embodiments, the enzyme with linalool synthase activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 64. In some embodiments, the enzyme with linalool synthase activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 65. In some embodiments, the enzyme with linalool synthase activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 66. In some embodiments, the enzyme with linalool synthase activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 67. In some embodiments, the enzyme with linalool synthase activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 68. In some embodiments, the enzyme with linalool synthase activity comprises the amino acid sequence as set forth in any one of SEQ ID NOs: 15 and 63-68. In some embodiments, the enzyme with linalool synthase activity comprises the amino acid sequence as set forth in SEQ ID NO: 15. In some embodiments, the enzyme with linalool synthase activity comprises the amino acid sequence as set forth in SEQ ID NO: 63. In some embodiments, the enzyme with linalool synthase activity comprises the amino acid sequence as set forth in SEQ ID NO: 64. In some embodiments, the enzyme with linalool synthase activity comprises the amino acid sequence as set forth in SEQ ID NO: 65. In some embodiments, the enzyme with linalool synthase activity comprises the amino acid sequence as set forth in SEQ ID NO: 66. In some embodiments, the enzyme with linalool synthase activity comprises the amino acid sequence as set forth in SEQ ID NO: 67. In some embodiments, the enzyme with linalool synthase activity comprises the amino acid sequence as set forth in SEQ ID NO: 68. In some embodiments, the enzyme with linalool synthase activity consists of the amino acid sequence as set forth in any one of SEQ ID NOs: 15 and 63-68. In some embodiments, the enzyme with linalool synthase activity consists of the amino acid sequence as set forth in SEQ ID NO: 15. In some embodiments, the enzyme with linalool synthase activity consists of the amino acid sequence as set forth in SEQ ID NO: 63. In some embodiments, the enzyme with linalool synthase activity consists of the amino acid sequence as set forth in SEQ ID NO: 64. In some embodiments, the enzyme with linalool synthase activity consists of the amino acid sequence as set forth in SEQ ID NO: 65. In some embodiments, the enzyme with linalool synthase activity consists of the amino acid sequence as set forth in SEQ ID NO: 66. In some embodiments, the enzyme with linalool synthase activity consists of the amino acid sequence as set forth in SEQ ID NO: 67. In some embodiments, the enzyme with linalool synthase activity consists of the amino acid sequence as set forth in SEQ ID NO: 68. In some embodiments, the gene encoding the enzyme with linalool synthase activity comprises a nucleic acid sequence which encodes an enzyme comprising an amino acid sequence with at least 80% (e.g., at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9%) sequence identity to the sequence as set forth in any one of SEQ ID NOs: 15 and 63-68. In some embodiments, the gene encoding the enzyme with linalool synthase activity comprises a nucleic acid sequence which encodes an enzyme consisting of an amino acid sequence as set forth in any one of SEQ ID NOs: 15 and 63-68. In some embodiments, the gene encoding the enzyme with linalool synthase activity comprises a nucleic acid sequence as set forth in SEQ ID NO: 16. Identification of additional enzymes having linalool synthase activity or predicted to have farnesyl diphosphate synthase activity may be performed, for example based on similarity or homology with one or more domains of a linalool synthase, such as the linalool synthase provided by any one of SEQ ID NOs: 15 and 63-68. In some embodiments, an enzyme for use in the modified cells and methods described herein may be identified based on similarity or homology with an active domain, such as a catalytic domain, such as a catalytic domain associated with linalool synthase activity. In some embodiments, an enzyme for use in the modified cells and methods described herein may have a relatively high level of sequence identity with a reference linalool synthase, e.g., in the region of the catalytic domain but a relatively low level of sequence identity to the reference linalool synthase based on analysis of a larger portion of the enzyme or across the full length of the enzyme. In some embodiments, the enzyme for use in the modified cells and methods described herein has at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9% sequence identity in the region of the catalytic domain of the enzyme relative to a reference linalool synthase (e.g., SEQ ID NO: 15 or 63-68). In some embodiments, an enzyme for use in the modified cells and methods described herein have a relatively high level of sequence identity in the region of the catalytic domain of the enzyme relative to a reference linalool synthase (e.g., SEQ ID NO: 15 or 63-68) and a relatively low level of sequence identity to the reference linalool synthase based on analysis of a larger portion of the enzyme or across the full length of the enzyme. In some embodiments, the enzymes for use in the modified cells and methods described herein have at least 10%, at least 15%, at least 20%, at least 25%, least 30% at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9% sequence identity based on a portion of the enzyme or across the full length of the enzyme relative to a reference linalool synthase (e.g., SEQ ID NO: 15 or 63-68). Enzyme having geraniol synthase activity In some embodiments, any of the modified cells described herein are genetically modified to express a heterologous gene encoding an enzyme having geraniol synthase activity. In some embodiments, the heterologous gene encoding an enzyme with geraniol synthase activity is a wild-type geraniol synthase gene (e.g., a gene isolated from an organism). In some embodiments, the enzyme with geraniol synthase activity is obtained from a bacterium, a fungus, or a plant. In some embodiments, the enzyme with geraniol synthase activity is obtained from a yeast. In some embodiments, the enzyme having geraniol synthase activity is from Ocimu basilicum (referred to as ObGES). The geraniol synthase enzyme is provided by the amino acid sequence set forth by SEQ ID NO: 17. An exemplary nucleic acid sequence of a geraniol synthase enzyme is provided by SEQ ID NO: 18. Other examples of enzymes having geraniol synthase activity useful for the compositions and methods provided herein include, but are not limited to those referenced by the GenBank accession numbers AHE41084.1 (SEQ ID NO: 69), AFD64744.1 (SEQ ID NO: 70), QNQ74216.1 (SEQ ID NO: 71). In some embodiments, the heterologous gene encodes an enzyme with geraniol synthase activity such that a cell that expresses the enzyme is capable of increased production of one or more monoterpenes. In some embodiments, the heterologous gene encodes an enzyme with geraniol synthase activity such that a cell that expresses the enzyme is capable of increased production of one or more monoterpenes as compared to a cell that does not express the heterologous gene. In some embodiments, the enzyme with geraniol synthase activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in any one of SEQ ID NOs: 17 and 69-71. In some embodiments, the enzyme with geraniol synthase activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 17. In some embodiments, the enzyme with geraniol synthase activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 69. In some embodiments, the enzyme with geraniol synthase activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 70. In some embodiments, the enzyme with geraniol synthase activity has an amino acid sequence with at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, or 99.9% sequence identity to the sequence as set forth in SEQ ID NO: 71. In some embodiments, the enzyme with geraniol synthase activity comprises the amino acid sequence as set forth in any one of SEQ ID NOs: 17 and 69-71. In some embodiments, the enzyme with geraniol synthase activity comprises the amino acid sequence as set forth in SEQ ID NO: 17. In some embodiments, the enzyme with geraniol synthase activity comprises the amino acid sequence as set forth in SEQ ID NO: 69. In some embodiments, the enzyme with geraniol synthase activity comprises the amino acid sequence as set forth in SEQ ID NO: 70. In some embodiments, the enzyme with geraniol synthase activity comprises the amino acid sequence as set forth in SEQ ID NO: 71. In some embodiments, the enzyme with geraniol synthase activity consists of the amino acid sequence as set forth in any one of SEQ ID NOs: 17 and 69-71. In some embodiments, the enzyme with geraniol synthase activity consists of the amino acid sequence as set forth in SEQ ID NO: 17. In some embodiments, the enzyme with geraniol synthase activity consists of the amino acid sequence as set forth in SEQ ID NO: 69. In some embodiments, the enzyme with geraniol synthase activity consists of the amino acid sequence as set forth in SEQ ID NO: 70. In some embodiments, the enzyme with geraniol synthase activity consists of the amino acid sequence as set forth in SEQ ID NO: 71. In some embodiments, the gene encoding the enzyme with geraniol synthase activity comprises a nucleic acid sequence which encodes an enzyme comprising an amino acid sequence with at least 80% (e.g., at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9%) sequence identity to the sequence as set forth in any one of SEQ ID NOs: 17 and 69-71. In some embodiments, the gene encoding the enzyme with geraniol synthase activity comprises a nucleic acid sequence which encodes an enzyme consisting of an amino acid sequence as set forth in any one of SEQ ID NOs: 17 and 69-71. In some embodiments, the gene encoding the enzyme with geraniol synthase activity comprises a nucleic acid sequence as set forth in SEQ ID NO: 18. Identification of additional enzymes having geraniol synthase activity or predicted to have farnesyl diphosphate synthase activity may be performed, for example based on similarity or homology with one or more domains of a geraniol synthase, such as the linalool synthase provided by SEQ ID NO: 17 or 69-71. In some embodiments, an enzyme for use in the modified cells and methods described herein may be identified based on similarity or homology with an active domain, such as a catalytic domain, such as a catalytic domain associated with geraniol synthase activity. In some embodiments, an enzyme for use in the modified cells and methods described herein may have a relatively high level of sequence identity with a reference geraniol synthase, e.g., in the region of the catalytic domain but a relatively low level of sequence identity to the reference geraniol synthase based on analysis of a larger portion of the enzyme or across the full length of the enzyme. In some embodiments, the enzyme for use in the modified cells and methods described herein has at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9% sequence identity in the region of the catalytic domain of the enzyme relative to a reference geraniol synthase (e.g., SEQ ID NO: 17 or 69- 71). In some embodiments, an enzyme for use in the modified cells and methods described herein have a relatively high level of sequence identity in the region of the catalytic domain of the enzyme relative to a reference geraniol synthase (e.g., SEQ ID NO: 17 or 69-71) and a relatively low level of sequence identity to the reference geraniol synthase based on analysis of a larger portion of the enzyme or across the full length of the enzyme. In some embodiments, the enzymes for use in the modified cells and methods described herein have at least 10%, at least 15%, at least 20%, at least 25%, least 30% at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9% sequence identity based on a portion of the enzyme or across the full length of the enzyme relative to a reference geraniol synthase (e.g., SEQ ID NO: 17 or 69-71). General methods of genetic engineering As will also be evident to one of ordinary skill in the art, the amino acid position number of a selected residue in a protein may have a different amino acid position number as compared to another protein (e.g., a reference protein). Generally, one may identify corresponding positions in other proteins using methods known in the art, for example by aligning the amino acid sequences of two or more proteins. Software programs and algorithms for aligning amino acid (or nucleotide) sequences are known in the art and readily available, e.g., Clustal Omega (Sievers et al.2011). The proteins described herein may further contain one or more modifications, for example to specifically alter a feature of the polypeptide unrelated to its desired physiological activity. Alternatively or in addition, the proteins described herein may contain one or more mutations to modulate expression and / or activity of the proteins in the cell. Mutations of a nucleic acid which encodes a protein preferably preserve the amino acid reading frame of the coding sequence, and preferably do not create regions in the nucleic acid which are likely to hybridize to form secondary structures, such a hairpins or loops, which can be deleterious to expression of the protein. Mutations can be made by selecting an amino acid substitution, or by random mutagenesis of a selected site in a nucleic acid which encodes the polypeptide. As described herein, variant polypeptides can be expressed and tested for one or more activities to determine which mutation provides a variant polypeptide with the desired properties. Further mutations can be made to variants (or to non-variant polypeptides) which are silent as to the amino acid sequence of the polypeptide, but which provide preferred codons for translation in a particular host (referred to as codon optimization). The preferred codons for translation of a nucleic acid in, e.g., S. cerevisiae, are well known to those of ordinary skill in the art. Still other mutations can be made to the noncoding sequences of a gene or cDNA clone to enhance expression of the polypeptide. The activity of a protein variant can be tested by cloning the gene encoding the protein variant into an expression vector, introducing the vector into an appropriate host cell, expressing the protein variant, and testing for a functional capability of the protein, as disclosed herein. The proteins described herein may contain an amino acid substitution of one or more positions corresponding to a reference protein, such as a wild-type protein. In some embodiments, the protein contains an amino acid substitution at 1, 2, 3, 4, 5, or more positions corresponding to a reference protein. In some embodiments, the protein is not a naturally occurring protein, e.g., is genetically modified. In some embodiments, the protein contains an amino acid substitution at 1, 2, 3, 4, 5, or more positions corresponding to a reference protein. In some embodiments, the protein is not a naturally occurring protein, e.g., is genetically modified. In some embodiments, the protein variant may also contain one or more amino acid substitutions that do not substantially affect the activity and / or structure of the protein. The skilled artisan will also realize that conservative amino acid substitutions may be made in the protein to provide functionally equivalent variants of the foregoing polypeptides, i.e., the variants retain the functional capabilities of the polypeptides. As used herein, a “conservative amino acid substitution” refers to an amino acid substitution which does not alter the relative charge or size characteristics of the protein in which the amino acid substitution is made. Variants can be prepared according to methods for altering polypeptide sequence known to one of ordinary skill in the art such as are found in references which compile such methods, e.g., Molecular Cloning: A Laboratory Manual, J. Sambrook, et al., eds., Fourth Edition, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 2012, or Current Protocols in Molecular Biology, F.M. Ausubel, et al., eds., John Wiley & Sons, Inc., New York. Exemplary functionally equivalent variants of polypeptides include conservative amino acid substitutions in the amino acid sequences of proteins disclosed herein. Conservative substitutions of amino acids include substitutions made amongst amino acids within the following groups: (a) M, I, L, V; (b) F, Y, W; (c) K, R, H; (d) A, G; (e) S, T; (f) Q, N; and (g) E, D. As one of ordinary skill in the art would be aware, homologous genes encoding a protein having a desired activity could be obtained from other species and could be identified by homology searches, for example through a protein BLAST search, available at the National Center for Biotechnology Information (NCBI) internet site (ncbi.nlm.nih.gov). By aligning the amino acid sequence of a protein with one or more reference proteins and / or by comparing the secondary or tertiary structure of a similar or homologous protein with one or more reference eta lyase, one can determine corresponding amino acid residues in similar or homologous proteins and can determine amino acid residues for mutation in the similar or homologous protein. Genes associated with the disclosure can be obtained (e.g., by PCR amplification) from DNA from any source of DNA which contains the given gene. In some embodiments, genes associated with the invention are synthetic, e.g., produced by chemical synthesis in vitro. Any means of obtaining a gene encoding the proteins described herein are compatible with the modified cells and methods described herein. The disclosure provided herein involves recombinant expression of genes encoding a protein having a desired activity, functional modifications, and variants of the foregoing, as well as uses relating thereto. Homologs and alleles of the nucleic acids associated with the invention can be identified by conventional techniques. Also encompassed by the invention are nucleic acids that hybridize under stringent conditions to the nucleic acids described herein. The term “stringent conditions” as used herein refers to parameters with which the art is familiar. Nucleic acid hybridization parameters may be found in references which compile such methods, e.g., Molecular Cloning: A Laboratory Manual, J. Sambrook, et al., eds., Fourth Edition, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 2012, or Current Protocols in Molecular Biology, F.M. Ausubel, et al., eds., John Wiley & Sons, Inc., New York. There are other conditions, reagents, and so forth which can be used, which result in a similar degree of stringency. The skilled artisan will be familiar with such conditions, and thus they are not given here. It will be understood, however, that the skilled artisan will be able to manipulate the conditions in a manner to permit the clear identification of homologs and alleles of nucleic acids of the invention (e.g., by using lower stringency conditions). The skilled artisan also is familiar with the methodology for screening cells and libraries for expression of such molecules which then are routinely isolated, followed by isolation of the pertinent nucleic acid molecule and sequencing. The invention also includes degenerate nucleic acids which include alternative codons to those present in the native materials. For example, serine residues are encoded by the codons TCA, AGT, TCC, TCG, TCT and AGC. Each of the six codons is equivalent for the purposes of encoding a serine residue. Thus, it will be apparent to one of ordinary skill in the art that any of the serine-encoding nucleotide triplets may be employed to direct the protein synthesis apparatus, in vitro or in vivo, to incorporate a serine residue into an elongating polypeptide. Similarly, nucleotide sequence triplets which encode other amino acid residues include, but are not limited to: CCA, CCC, CCG and CCT (proline codons); CGA, CGC, CGG, CGT, AGA and AGG (arginine codons); ACA, ACC, ACG and ACT (threonine codons); AAC and AAT (asparagine codons); and ATA, ATC and ATT (isoleucine codons). Other amino acid residues may be encoded similarly by multiple nucleotide sequences. Thus, the invention embraces degenerate nucleic acids that differ from the biologically isolated nucleic acids in codon sequence due to the degeneracy of the genetic code. The invention also embraces codon optimization to suit optimal codon usage of a host cell. The invention also provides modified nucleic acid molecules which include additions, substitutions and deletions of one or more nucleotides. In preferred embodiments, these modified nucleic acid molecules and / or the polypeptides they encode retain at least one activity or function of the unmodified nucleic acid molecule and / or the polypeptides, such as enzymatic activity. In certain embodiments, the modified nucleic acid molecules encode modified polypeptides, preferably polypeptides having conservative amino acid substitutions as are described elsewhere herein. The modified nucleic acid molecules are structurally related to the unmodified nucleic acid molecules and in preferred embodiments are sufficiently structurally related to the unmodified nucleic acid molecules so that the modified and unmodified nucleic acid molecules hybridize under stringent conditions known to one of skill in the art. For example, modified nucleic acid molecules which encode polypeptides having single amino acid changes can be prepared. Each of these nucleic acid molecules can have one, two or three nucleotide substitutions exclusive of nucleotide changes corresponding to the degeneracy of the genetic code as described herein. Likewise, modified nucleic acid molecules which encode polypeptides having two amino acid changes can be prepared which have, e.g., 2-6 nucleotide changes. Numerous modified nucleic acid molecules like these will be readily envisioned by one of skill in the art, including for example, substitutions of nucleotides in codons encoding amino acids 2 and 3, 2 and 4, 2 and 5, 2 and 6, and so on. In the foregoing example, each combination of two amino acids is included in the set of modified nucleic acid molecules, as well as all nucleotide substitutions which code for the amino acid substitutions. Additional nucleic acid molecules that encode polypeptides having additional substitutions (i.e., 3 or more), additions or deletions (e.g., by introduction of a stop codon or a splice site(s)) also can be prepared and are embraced by the invention as readily envisioned by one of ordinary skill in the art. Any of the foregoing nucleic acids or polypeptides can be tested by routine experimentation for retention of structural relation or activity to the nucleic acids and / or polypeptides disclosed herein. Mutations can be made by selecting an amino acid substitution, or by random mutagenesis of a selected site in a nucleic acid which encodes the polypeptide. As described herein, variant polypeptides can be expressed and tested for one or more activities to determine which mutation provides a variant polypeptide with the desired properties. Further mutations can be made to variants (or to non-variant polypeptides) which are silent as to the amino acid sequence of the polypeptide, but which provide preferred codons for translation in a particular host (referred to as codon optimization). The preferred codons for translation of a nucleic acid in, e.g., S. cerevisiae, are well known to those of ordinary skill in the art. Still other mutations can be made to the noncoding sequences of a gene or cDNA clone to enhance expression of the polypeptide. In one aspect of the present disclosure, one or more of the genes associated with the invention is expressed in a recombinant expression vector. As used herein, a “vector” may be any of a number of nucleic acids into which a desired sequence or sequences may be inserted by restriction and ligation for transport between different genetic environments or for expression in a host cell. Vectors are typically composed of DNA although RNA vectors are also available. Vectors include, but are not limited to: plasmids, fosmids, phagemids, virus genomes, and artificial chromosomes. A cloning vector is one which is able to replicate autonomously or integrated in the genome in a host cell. In the case of plasmids, replication of the desired sequence may occur many times as the plasmid increases in copy number within the host cell such as a host bacterium or just a single time per host before the host reproduces by mitosis. In the case of phage, replication may occur actively during a lytic phase or passively during a lysogenic phase. An expression vector is one into which a desired DNA sequence may be inserted by restriction and ligation such that it is operably joined to regulatory sequences and may be expressed as an RNA transcript. Vectors may further contain one or more marker sequences suitable for use in the identification of cells which have or have not been transformed or transfected with the vector. Markers include, for example, genes encoding proteins which increase or decrease either resistance or sensitivity to antibiotics or other compounds, genes which encode proteins whose activities are detectable by standard assays known in the art (e.g., β-galactosidase, luciferase, or alkaline phosphatase), and genes which visibly affect the phenotype of transformed or transfected cells, hosts, colonies or plaques (e.g., green fluorescent protein). Preferred vectors are those capable of autonomous replication and expression of the structural gene products present in the DNA segments to which they are operably joined. As used herein, a coding sequence and regulatory sequences are said to be “operably” joined or operably linked when they are covalently linked in such a way as to place the expression or transcription of the coding sequence under the influence or control of the regulatory sequences. If it is desired that the coding sequences be translated into a functional protein, two DNA sequences are said to be operably joined or operably linked if induction of a promoter in the 5’ regulatory sequences results in the transcription of the coding sequence and if the nature of the linkage between the two DNA sequences does not (1) result in the introduction of a frame-shift mutation, (2) interfere with the ability of the promoter region to direct the transcription of the coding sequences, or (3) interfere with the ability of the corresponding RNA transcript to be translated into a protein. Thus, a promoter region would be operably joined to a coding sequence if the promoter region were capable of effecting transcription of that DNA sequence such that the resulting transcript can be translated into the desired protein or polypeptide. When the nucleic acid molecule that encodes any of the proteins of the present disclosure is expressed in a cell, a variety of transcription control sequences (e.g., promoter / enhancer sequences) can be used to direct its expression. In some embodiments, each of the genes is operably linked to a promoter (e.g., each gene linked to a separate promoter). The promoter can be a native promoter, i.e., the promoter of the gene in its endogenous context, which provides normal regulation of expression of the gene. In some embodiments, the promoter can be constitutive, i.e., the promoter is unregulated allowing for continual transcription of its associated gene. A variety of conditional promoters also can be used, such as promoters controlled by the presence or absence of a molecule. The precise nature of the regulatory sequences needed for gene expression may vary between species or cell types, but shall in general include, as necessary, 5’ non-transcribed and 5’ non-translated sequences involved with the initiation of transcription and translation respectively, such as a TATA box, capping sequence, CAAT sequence, and the like. In particular, such 5’ non-transcribed regulatory sequences will include a promoter region which includes a promoter sequence for transcriptional control of the operably joined gene. Regulatory sequences may also include enhancer sequences or upstream activator sequences as desired. The vectors of the invention may optionally include 5' leader or signal sequences. The choice and design of an appropriate vector is within the ability and discretion of one of ordinary skill in the art. Expression vectors containing all the necessary elements for expression are commercially available and known to those skilled in the art. See, e.g., Sambrook et al., Molecular Cloning: A Laboratory Manual, Fourth Edition, Cold Spring Harbor Laboratory Press, 2012. Cells are genetically engineered by the introduction into the cells of heterologous DNA (RNA). That heterologous DNA (RNA) may be placed under operable control of transcriptional elements to permit the expression of the heterologous DNA in the host cell. As one of ordinary skill in the art would appreciate, any of the proteins described herein can also be expressed in other yeast cells, including yeast strains used for producing wine, mead, sake, cider, etc. A nucleic acid molecule that encodes a protein having a desired activity of the present disclosure can be introduced into a cell or cells using methods and techniques that are standard in the art. For example, nucleic acid molecules can be introduced by standard protocols such as transformation including chemical transformation and electroporation, transduction, particle bombardment, etc. Expressing the nucleic acid molecule encoding the proteins of the claimed invention also may be accomplished by integrating the nucleic acid molecule into the genome. The incorporation of genes can be accomplished either by incorporation of the nucleic acid encoding the protein(s) into the genome of the yeast cell, or by transient or stable maintenance of the new nucleic acid encoding the protein(s) as an episomal element. In eukaryotic cells, a permanent, inheritable genetic change is generally achieved by introduction of the DNA into the genome of the cell. The heterologous gene may also include various transcriptional elements required for expression of the encoded gene product (e.g., protein having a desired activity). For example, in some embodiments, any of the genes described herein may be operably linked to a promoter. In some embodiments, the promoter is an inducible promoter. In some embodiments, the promoter is active during a particular stage of a fermentation process. For example, in some embodiments, peak expression from the promoter is during an early stage of the fermentation process, e.g., before >50% of the fermentable sugars have been consumed. In some embodiments, peak expression from the promoter is during a late stage of the fermentation process e.g., after 50% of the fermentable sugars have been consumed. Conditions in the medium change during the course of the fermentation process, for example the availability of nutrients and oxygen tend to decrease over time during fermentation as sugar source and oxygen become depleted. Additionally, the presence of other factors, such as products produced by metabolism of the cells, may increase. In some embodiments, the promoter is regulated by one or more conditions in the fermentation process, such as presence or absence of one or more factors. In some embodiments, the promoter is regulated by hypoxic conditions. Examples of promoters of hypoxia activated genes are known in the art. See, e.g., Zitomer et al. Kidney Int. (1997) 51(2): 507-13; Gonzalez Siso et al. Biotechnol. Letters (2012) 34: 2161-2173. In some embodiments, the promoter is a constitutive promoter. Examples of constitutive promoters for use in yeast cells are known in the art and evident to one of ordinary skill in the art. In some embodiments, the promoter is a yeast promoter, e.g., a native promoter from the yeast cell in which the heterologous gene or the exogenous gene is expressed. Non-limiting examples of promoters for use in the genetically modified cells and methods described herein include, the NCP1 promoter (pNCP1), ERG11 promoter (pERG11), HEM13 promoter (pHEM13), SPG1 promoter (pSPG1), PRB1 promoter (pPRB1), QCR10 (pQCR10), PGK1 promoter (pPGK1), OLE1 promoter (pOLE1), ERG25 promoter (pERG25), the HHF2 promoter (pHHF2), the TDH1 promoter (pTDH1), the TDH2 promoter (pTDH2), the TDH3 promoter (pTDH3), the ENO2 promoter (pENO2), the ANT1 promoter (pANT1), the PEX11 promoter (pPEX11), or the HSP26 promoter (pHSP26). In some embodiments, the heterologous nucleic acid comprising a gene encoding the enzyme having alcohol acyltransferase activity can be operably linked to a promoter selected from the group consisting of SEQ ID NOs: 19-35 and 72-73. In some embodiments, the promoter is selected from the group consisting of pSPG1 (SEQ ID NO: 26), pHSP26 (SEQ ID NO: 20), pANT1 (SEQ ID NO: 34), pPEX11 (SEQ ID NO: 35), and pALD6 (SEQ ID NO: 73). In some embodiments, the promoter comprises or consists of SEQ ID NO: 19. In some embodiments, the promoter comprises or consists of SEQ ID NO: 20. In some embodiments, the promoter comprises or consists of SEQ ID NO: 21. In some embodiments, the promoter comprises or consists of SEQ ID NO: 22. In some embodiments, the promoter comprises or consists of SEQ ID NO: 23. In some embodiments, the promoter comprises or consists of SEQ ID NO: 24. In some embodiments, the promoter comprises or consists of SEQ ID NO: 25. In some embodiments, the promoter comprises or consists of SEQ ID NO: 26. In some embodiments, the promoter comprises or consists of SEQ ID NO: 27. In some embodiments, the promoter comprises or consists of SEQ ID NO: 28. In some embodiments, the promoter comprises or consists of SEQ ID NO: 29. In some embodiments, the promoter comprises or consists of SEQ ID NO: 30. In some embodiments, the promoter comprises or consists of SEQ ID NO: 31. In some embodiments, the promoter comprises or consists of SEQ ID NO: 32. In some embodiments, the promoter comprises or consists of SEQ ID NO: 33. In some embodiments, the promoter comprises or consists of SEQ ID NO: 34. In some embodiments, the promoter comprises or consists of SEQ ID NO: 35. In some embodiments, the promoter comprises or consists of SEQ ID NO: 72. In some embodiments, the promoter comprises or consists of SEQ ID NO: 73. Genetically modified yeast cells Aspects of the present disclosure relate to genetically modified yeast cells (modified cells) and use of such modified cells in methods of producing a fermented product (e.g., a fermented beverage). The genetically modified yeast cells described herein are genetically modified to reduce sensory detection of one or more wort-associated off-flavors of a fermented beverage. In some embodiments, the wort-associated off-flavors are aldehydic and / or non-aldehyde molecules. In some embodiments, the genetically modified yeast cells described herein are genetically modified to functionally disrupt one or more proteins associated with maltose and / or maltotriose transport into the modified cell and / or maltose and / or maltotriose hydrolysis by the modified cell. As used herein, to “functionally disrupt” or a “functional disruption” e.g., of a target gene, for example, one or more genes encoding one or more proteins associated with maltose and / or maltotriose transport, and / or maltose and / or maltotriose hydrolysis, means that the target gene is altered in such a way as to decrease in the host cell the activity of the protein encoded by the target gene. Similarly, to “functionally disrupt” or a “functional disruption” e.g., of a target protein, for example, one or more proteins associated with maltose and / or maltotriose transport, and / or maltose and / or maltotriose hydrolysis, means that the target protein is altered in such a way as to decrease in the host cell the activity of the protein. In some embodiments, the activity of the target protein encoded by the target gene is eliminated in the host cell. In other embodiments, the activity of the target protein encoded by the target gene is decreased in the host cell. Functional disruption of the target gene may be achieved by deleting all or a part of the gene so that gene expression is eliminated or reduced, or so that the activity of the gene product is eliminated or reduced. Functional disruption of the target gene may also be achieved by mutating a regulatory element of the gene, e.g., the promoter of the gene so that expression is eliminated or reduced, or by mutating the coding sequence of the gene so that the activity of the gene product is eliminated or reduced. In some embodiments, functional disruption of the target gene results in the removal of the complete open reading frame of the target gene. In other embodiments, functional disruption means introducing a premature stop codon into the ORF of the target gene. In other embodiments, functional disruption means inserting an exogenous nucleic acid sequence into the ORF or deleting an endogenous nucleic acid sequence from the ORF of the target gene. The terms “genetically modified cell,” “genetically modified yeast cell,” and “modified cell,” as may be used interchangeably herein, to refer to a eukaryotic cell (e.g., a yeast cell), which has been, or may be presently, modified by the introduction of a heterologous gene. The terms (e.g., modified cell) include the progeny of the original cell which has been genetically modified by the introduction of a heterologous gene. It shall be understood by the skilled artisan that the progeny of a single cell may not necessarily be completely identical in morphology or in genomic or total nucleic acid complement as the original parent, due to mutation (i.e., natural, accidental, or deliberate alteration of the nucleic acids of the modified cell). Yeast cells for use in the methods described herein are preferably capable of fermenting a sugar source (e.g., a fermentable sugar) and producing ethanol (ethyl alcohol) and carbon dioxide. In some embodiments, the yeast cell is of the genus Saccharomyces. The Saccharomyces genus includes nearly 500 distinct species, many of which are used in food production. One example species is Saccharomyces cerevisiae (S. cerevisiae), which is commonly referred to as “brewer’s yeast” or “baker’s yeast,” and is used in the production of wine, bread, beer, among other products. Other members of the Saccharomyces genus include, without limitation, the wild yeast Saccharomyces paradoxus, which is a close relative to S. cerevisiae; Saccharomyces bayanus, Saccharomyces pastorianus, Saccharomyces carlsbergensis, Saccharomyces uvarum, Saccharomyces cerevisiae var boulardii, Saccharomyces eubayanus. In some embodiments, the yeast is Saccharomyces cerevisiae (S. cerevisiae). Saccharomyces species may be haploid (i.e., having a single set of chromosomes), diploid (i.e., having a paired set of chromosomes), or polyploid (i.e., carrying or containing more than two homologous sets of chromosomes). Saccharomyces species used, for example for beer brewing, are typically classified into two groups: ale strains (e.g., S. cerevisiae), which are top fermenting, and lager strains (e.g., S. pastorianus, S. carlsbergensis, S. uvarum), which are bottom fermenting. These characterizations reflect their separation characteristics in open square fermentors, as well as other characteristics such as preferred fermentation temperatures and alcohol concentrations achieved. Although beer brewing and wine producing has traditionally focused on use of S. cerevisiae strains, other yeast species and genera have been appreciated in production of fermented beverages. In some embodiments, the yeast cell belongs to a non-Saccharomyces genus. See, e.g., Crauwels et al. Brewing Science (2015) 68: 110-121; Esteves et al. Microorganisms (2019) 7(11): 478. In some embodiments, the yeast cell is of the genus Kloeckera, Candida, Starmerella, Hanseniaspora, Kluyveromyces / Lachance, Metschnikowia, Saccharomycodes, Zygosaccharomyces, Dekkera (also referred to as Brettanomyces), Wickerhamomyces, or Torulaspora. Examples of non-Saccharomyces yeast include, without limitation, Hanseniaspora uvarum, Hanseniaspora guillermondii, Hanseniaspora vinae, Metschnikowia pulcherrima, Kluyveromyces / Lachancea thermotolerans, Starmerella bacillaris (previously referred to as Candida stellata / Candida zemplinina), Saccharomycodes ludwigii, Zygosaccharomyces rouxii, Dekkera bruxellensis, Dekkera anomala, Brettanomyces custersianus, Brettanomyces naardenensis, Brettanomyces nanus, Wickerhamomyces anomalus, and Torulaspora delbrueckii. In some embodiments, the methods described herein involve use of more than one genetically modified yeast. For example, in some embodiments, the methods may involve use of more than one genetically modified yeast belonging to the genus Saccharomyces. In some embodiments, the methods may involve use of more than one genetically modified yeast belonging to a non-Saccharomyces genus. In some embodiments, the methods may involve use of more than one genetically modified yeast belonging to the genus Saccharomyces and one genetically modified yeast belonging to a non-Saccharomyces genus. Alternatively, or in addition, any of the methods described herein may involve use of one or more genetically modified yeast and one or more non-genetically modified (wildtype) yeast. In some embodiments, the yeast is a hybrid strain. As will be evident to one of ordinary skill in the art, the term “hybrid strain” of yeast refers to a yeast strain that has resulted from the crossing of two different yeast strains, for example, to achieve one or more desired characteristics. For example, a hybrid strain may result from the crossing of two different yeast strains belonging to the same genus or the same species. In some embodiments, a hybrid strain results from the crossing of a Saccharomyces cerevisiae strain and a Saccharomyces eubayanus strain. See, e.g., Krogerus et al. Microbial Cell Factories (2017) 16: 66. In some embodiments, the yeast strain is a wild yeast strain, such as a yeast strain that is isolated from a natural source and subsequently propagated. Alternatively, in some embodiments, the yeast strain is a domesticated yeast strain. Domesticated yeast strains have been subjected to human selection and breeding to have desired characteristics. In some embodiments, the genetically modified yeast cells may be used in symbiotic matrices with other yeast or bacterial strains. Symbiotic matrices of yeast cells and bacterial strains may be used, for example, for the production of fermented beverages, such as kombucha, kefir, and ginger beers. Saccharomyces fragilis, for example, is part of kefir culture and is grown on the lactose contained in whey. Other bacterial strains that may be used in symbiotic matrices with the genetically modified yeast cells include Bifidobacterium animalis subsp. lactis, Bifidobacterium breve, bacteria in the genus Lactobacillus, and bacteria in the genus Pediococcus. Although many fermented beverages are produced using S. cerevisiae strains, other yeast genera have been appreciated in production of fermented beverages and may be used in symbiotic matrices with the modified yeast cells. In some embodiments, the other yeast cell belongs to a non-Saccharomyces genus. See, e.g., Crauwels et al. Brewing Science (2015) 68: 110-121; Esteves et al. Microorganisms (2019) 7(11): 478. In some embodiments, the other yeast cell is of the genus Kloeckera, Candida, Starmerella, Hanseniaspora, Kluyveromyces / Lachance, Metschnikowia, Saccharomycodes, Zygosaccharomyce, Dekkera (also referred to as Brettanomyces), Wickerhamomyces, or Torulaspora. Examples of non- Saccharomyces yeast include, without limitation, Hanseniaspora uvarum, Hanseniaspora guillermondii, Hanseniaspora vinae, Metschnikowia pulcherrima, Kluyveromyces / Lachancea thermotolerans, Starmerella bacillaris (previously referred to as Candida stellata / Candida zemplinina), Saccharomycodes ludwigii, Zygosaccharomyces rouxii, Dekkera bruxellensis, Dekkera anomala, Brettanomyces custersianus, Brettanomyces naardenensis, Brettanomyces nanus, Wickerhamomyces anomalus, and Torulaspora delbrueckii. Methods of genetically modifying yeast cells are known in the art. In some embodiments, the yeast cell is diploid and one copy of a heterologous gene encoding an enzyme with glycosidase activity as described herein is introduced into the yeast genome. In some embodiments, the yeast cell is diploid and one copy of a heterologous gene encoding an enzyme with a desired activity (e.g., an enzyme having AAT activity, an enzyme having carbon-sulfur-lyase (CSL) activity, a HMG1 enzyme, a ERG20 enzyme, a linalool synthase; and / or a geraniol synthase) as described herein is introduced into both copies of the yeast genome. In some embodiments, the copies of the heterologous gene are identical. In some embodiments, the copies of the heterologous gene are not identical, but the genes encode an identical enzyme having the desired activity. In some embodiments, the copies of the heterologous gene are not identical, and the genes encode enzymes having an activity that are different (e.g., mutants, variants, fragments thereof). In some embodiments, the cell contains a gene encoding an enzyme with a desired activity, referred to as an endogenous gene, and also contains a second gene encoding an enzyme with the same desired activity, which may be the same or different enzyme with the desired activity as that encoded by the endogenous gene. In some embodiments, the yeast cell is diploid and one copy of a gene encoding an enzyme with a desired activity (e.g., an enzyme having AAT activity, an enzyme having carbon-sulfur-lyase (CSL) activity, a HMG1 enzyme, a ERG20 enzyme, a linalool synthase; and / or a geraniol synthase) as described herein is introduced into both copies of the yeast genome. In some embodiments, the copies of the gene encoding an enzyme with a desired activity are identical. In some embodiments, the copies of the gene encoding an enzyme with the desired activity are not identical, but the genes encode an identical enzyme having the same or substantially similar activity. In some embodiments, the copies of the gene encoding an enzyme with a desired activity are not identical, and the genes encode enzymes having activity that are different (e.g., mutants, variants, fragments thereof). In some embodiments, the cell contains a gene encoding an enzyme with the desired activity, referred to as an endogenous gene, and also contains a second gene encoding an enzyme with the same or substantially similar activity, which may be the same or different enzyme with the activity as that encoded by the endogenous gene. In some embodiments, the yeast cell is tetraploid. Tetraploid yeast cells are cells which maintain four complete sets of chromosomes (i.e., a complete set of chromosomes in four copies). In some embodiments, the yeast cell is tetraploid and a copy of a heterologous gene encoding an enzyme with desired activity (e.g., an enzyme having AAT activity, an enzyme having carbon-sulfur-lyase (CSL) activity, a HMG1 enzyme, a ERG20 enzyme, a linalool synthase; and / or a geraniol synthase) as described herein is introduced into at least one copy of the genome. In some embodiments, the yeast cell is tetraploid and a copy of a heterologous gene encoding an enzyme with desired activity as described herein is introduced into more than one copy of the genome. In some embodiments, the yeast cell is tetraploid and a copy of a heterologous gene encoding an enzyme with the desired activity as described herein is introduced into all four copies of the genome. In some embodiments, the copies of the heterologous gene are identical. In some embodiments, the copies of the heterologous gene are not identical, but the genes encode an identical enzyme having the desired activity or substantially similar activity. In some embodiments, the copies of the heterologous gene are not identical, and the genes encode enzymes having the activity that are different (e.g., mutants, variants, fragments thereof). In some embodiments, the yeast cell is tetraploid and a copy of a gene encoding an enzyme with the desired activity as described herein is introduced into at least one copy of the genome. In some embodiments, the yeast cell is tetraploid and a copy of a gene encoding an enzyme with the desired activity as described herein is introduced into more than one copy of the genome. In some embodiments, the yeast cell is tetraploid and a copy of a gene encoding an enzyme with the desired activity as described herein is introduced into all four copies of the genome. In some embodiments, the copies of the gene encoding an enzyme with the desired activity are identical. In some embodiments, the copies of the gene encoding an enzyme with the desired activity are not identical, but the genes encode an identical enzyme having the activity or substantially similar activity. In some embodiments, the copies of the gene encoding an enzyme with the activity are not identical, and the genes encode enzymes having activities that are different (e.g., mutants, variants, fragments thereof). In some embodiments, the cell contains a gene encoding an enzyme, referred to as an endogenous gene, and also contains one or more additional copies of a gene encoding an enzyme with the desired activity or substantially similar activity, which may be the same or different enzyme with O-methyltransferase activity as that encoded by the endogenous gene. In some embodiments, the growth rate of the modified cell is not substantially impaired relative to a wild-type yeast cell that does not comprise a genetic modification. Methods of measuring and comparing the growth rates of two cells will be known to one of ordinary skill in the art. Non-limiting examples of growth rates that can be measured and compared between two types of cells are replication rate, budding rate, colony-forming units (CFUs) produced per unit of time, and amount of fermentable sugar reduced in a medium per unit of time. The growth rate of a modified cell is “not substantially impaired” relative to a wild-type cell if the growth rate, as measured, is at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 99%, or at least 100% of the growth rate of the wild-type cell. Strains of yeast cells that may be used with the methods described herein will be known to one of ordinary skill in the art and include yeast strains used for brewing desired fermented beverages as well as commercially available yeast strains. Examples of common beer strains include, without limitation, American ale strains, Belgian ale strains, British ale strains, Belgian lambic / sour ale strains, Barleywine / Imperial Stout strains, India Pale Ale strains, Brown Ale strains, Kolsch and Altbier strains, Stout and Porter strains, and Wheat beer strains. Non-limiting examples of strains for use with the genetically modified cells and methods described herein include Chico American Ale, Wyeast American Ale 1056, Wyeast American Ale II 1272, Wyeast Denny’s Favorite 501450, Wyeast Northwest Ale 1332, Wyeast Ringwood Ale 1187, Siebel Inst. American Ale BRY 96, White Labs American Ale Yeast Blend WLP060, White Labs California Ale V WLP051, White Labs California Ale WLP001, White Labs Old Sonoma Ale WLP076, White Labs Pacific Ale WLP041, White Labs East Coast Ale WLP008, White Labs East Midlands Ale WLP039, White Labs San Diego Super Yeast WLP090, White Labs San Francisco Lager WLP810, White Labs Neutral Grain WLP078, Lallemand American West Coast Ale BRY-97, Lallemand CBC-1 (Cask and Bottle Conditioning), Brewferm Top, Coopers Pure Brewers’ Yeast, Fermentis US-05, Real Brewers Yeast Lucky #7, Muntons Premium Gold, Muntons Standard Yeast, East Coast Yeast Northeast Ale ECY29, East Coast Yeast Old Newark Ale ECY10, East Coast Yeast Old Newark Beer ECY12, Fermentis Safale US-05, Fermentis Safbrew T-58, Real Brewers Yeast The One, Mangrove Jack US West Coast Yeast, Mangrove Jack Workhorse Beer Yeast, Lallemand Abbaye Belgian Ale, White Labs Abbey IV WLP540, White Labs American Farmhouse Blend WLP670, White Labs Antwerp Ale WLP515, East Coast Yeast Belgian Abbaye ECY09, White Labs Belgian Ale WLP550, Mangrove Jack Belgian Ale Yeast, Wyeast Belgian Dark Ale 3822-PC, Wyeast Belgian Saison 3724, White Labs Belgian Saison I WLP565, White Labs Belgian Saison II WLP566, White Labs Belgian Saison III WLP585, Wyeast Belgian Schelde Ale 3655-PC, Wyeast Belgian Stout 1581-PC, White Labs Belgian Style Ale Yeast Blend WLP575, White Labs Belgian Style Saison Ale Blend WLP568, East Coast Yeast Belgian White ECY11, Lallemand Belle Saison, Wyeast Biere de Garde 3725-PC, White Labs Brettanomyces Bruxellensis Trois Vrai WLP648, Brewferm Top, Wyeast Canadian / Belgian Ale 3864-PC, Lallemand CBC-1 (Cask and Bottle Conditioning), Wyeast Farmhouse Ale 3726-PC, East Coast Yeast Farmhouse Brett ECY03, Wyeast Flanders Golden Ale 3739-PC, White Labs Flemish Ale Blend WLP665, White Labs French Ale WLP072, Wyeast French Saison 3711, Wyeast Leuven Pale Ale 3538-PC, Fermentis Safbrew T-58, East Coast Yeast Saison Brasserie Blend ECY08, East Coast Yeast Saison Single-Strain ECY14, Real Brewers Yeast The Monk, Siebel Inst. Trappist Ale BRY 204, East Coast Yeast Trappist Ale ECY13, White Labs Trappist Ale WLP500, Wyeast Trappist Blend 3789-PC, Wyeast British Ale 1098, Wyeast British Ale II 1335, Wyeast British Cask Ale 1026-PC, Wyeast English Special Bitter 1768-PC, Wyeast Irish Ale 1084, London Ale, Wyeast London Ale 1028, Wyeast London Ale III 1318, Wyeast London ESB Ale 1968, Wyeast Ringwood Ale 1187, Wyeast Thames Valley Ale 1275, Wyeast Thames Valley Ale II 1882-PC, Wyeast West Yorkshire Ale 1469, Wyeast Whitbread Ale 1099, Mangrove Jack British Ale Yeast, Mangrove Jack Burton Union Yeast, Mangrove Jack Workhorse Beer Yeast, East Coast Yeast British Mild Ale ECY18, East Coast Yeast Northeast Ale ECY29, East Coast Yeast Burton Union ECY17, East Coast Yeast Old Newark Ale ECY10, White Labs Bedford British Ale WLP006, White Labs British Ale WLP005, White Labs Burton Ale WLP023, White Labs East Midlands Ale WLP039, White Labs English Ale Blend WLP085, White Labs English Ale WLP002, White Labs Essex Ale Yeast WLP022, White Labs Irish Ale WLP004, White Labs London Ale WLP013, White Labs Manchester Ale WLP038, White Labs Old Sonoma Ale WLP076, White Labs San Diego Super Yeast WLP090, White Labs Whitbread Ale WLP017, White Labs North Yorkshire Ale WLP037, Coopers Pure Brewers’ Yeast, Siebel Inst. English Ale BRY 264, Muntons Premium Gold, Muntons Standard Yeast, Lallemand Nottingham, Fermentis Safale S-04, Fermentis Safbrew T-58, Lallemand Windsor (British Ale), Real Brewers Yeast Ye Olde English, Brewferm Top, White Labs American Whiskey WLP065, White Labs Dry English Ale WLP007, White Labs Edinburgh Ale WLP028, Fermentis Safbrew S-33, Wyeast Scottish Ale 1728, East Coast Yeast Scottish Heavy ECY07, White Labs Super High Gravity WLP099, White Labs Whitbread Ale WLP017, Wyeast Belgian Lambic Blend 3278, Wyeast Belgian Schelde Ale 3655-PC, Wyeast Berliner-Weisse Blend 3191-PC, Wyeast Brettanomyces Bruxellensis 5112, Wyeast Brettanomyces Lambicus 5526, Wyeast Lactobacillus 5335, Wyeast Pediococcus Cerevisiae 5733, Wyeast Roeselare Ale Blend 3763, Wyeast Trappist Blend 3789-Pc, White Labs Belgian Sour Mix Wlp655, White Labs Berliner Weisse Blend Wlp630, White Labs Saccharomyces “Bruxellensis” Trois Wlp644, White Labs Brettanomyces Bruxellensis Wlp650, White Labs Brettanomyces Claussenii Wlp645, White Labs Brettanomyces Lambicus Wlp653, White Labs Flemish Ale Blend Wlp665, East Coast Yeast Berliner Blend Ecy06, East Coast Yeast Brett Anomala Ecy04, East Coast Yeast Brett Bruxelensis Ecy05, East Coast Yeast Brett Custersianus Ecy19, East Coast Yeast Brett Nanus Ecy16, Strain #2, East Coast Yeast BugCounty ECY20, East Coast Yeast BugFarm ECY01, East Coast Yeast Farmhouse Brett ECY03, East Coast Yeast Flemish Ale ECY02, East Coast Yeast Oud Brune ECY23, Wyeast American Ale 1056, Siebel Inst. American Ale BRY 96, White Labs American Ale Yeast Blend WLP060, White Labs Bourbon Yeast WLP070, White Labs California Ale V WLP051, White Labs California Ale WLP001, White Labs Dry English ale WLP007, White Labs East Coast Ale WLP008, White Labs Neutral Grain WLP078, White Labs Super High Gravity WLP099, White Labs Tennessee WLP050, Fermentis US-05, Real Brewers Yeast Lucky #7, Fermentis Safbrew S- 33, East Coast Yeast Scottish Heavy ECY07, Lallemand Windsor (British Ale), Wyeast American Ale 1056, Wyeast American Ale II 1272, Wyeast British Ale 1098, Wyeast British Ale II 1335, Wyeast Denny’s Favorite 501450, Wyeast London Ale 1028, Wyeast London Ale III 1318, Wyeast London ESB Ale 1968, Wyeast Northwest Ale 1332, Wyeast Ringwood Ale 1187, Siebel Inst. American Ale BRY 96, White Labs American Ale Yeast Blend WLP060, White Labs Bedford British Ale WLP006, White Labs British Ale WLP005, White Labs Burton Ale WLP023, White Labs California Ale V WLP051, White Labs California Ale WLP001, White Labs East Coast Ale WLP008, White Labs English Ale WLP002, White Labs London Ale WLP013, White Labs Essex Ale Yeast WLP022, White Labs Pacific Ale WLP041, White Labs San Diego Super Yeast WLP090, White Labs Whitbread Ale WLP017, Brewferm Top, Mangrove Jack Burton Union Yeast, Mangrove Jack US West Coast Yeast, Mangrove Jack Workhorse Beer Yeast, Coopers Pure Brewers’ Yeast, Fermentis US-05, Fermentis Safale S-04, Fermentis Safbrew T-58, Real Brewers Yeast Lucky #7, Real Brewers Yeast The One, Muntons Premium Gold, Muntons Standard Yeast, East Coast Yeast Northeast Ale ECY29, Lallemand Nottingham, Lallemand Windsor (British Ale), Wyeast American Ale 1056, Wyeast American Ale II 1272, Wyeast British Ale 1098, Wyeast British Ale II 1335, Wyeast Thames Valley Ale 1275, Wyeast Thames Valley Ale II 1882-PC, Wyeast West Yorkshire Ale 1469, Wyeast Whitbread Ale 1099, Wyeast British Cask Ale 1026-PC, Wyeast English Special Bitter 1768-PC, Wyeast London Ale 1028, Wyeast London Ale III 1318, Wyeast London ESB Ale 1968, Wyeast Northwest Ale 1332, Wyeast Ringwood Ale 1187, White Labs American Ale Yeast Blend WLP060, White Labs British Ale WLP005, White Labs Bedford British Ale WLP006, White Labs British Ale WLP005, White Labs Burton Ale WLP023, White Labs California Ale V WLP051, White Labs California Ale WLP001, White Labs East Coast Ale WLP008, White Labs English Ale WLP002, White Labs Essex Ale Yeast WLP022, White Labs French Ale WLP072, White Labs London Ale WLP013, White Labs Pacific Ale WLP041, White Labs Whitbread Ale WLP017, Brewferm Top, East Coast Yeast British Mild Ale ECY18, Coopers Pure Brewers’ Yeast, Muntons Premium Gold, Muntons Standard Yeast, Mangrove Jack Newcastle Dark Ale Yeast, Lallemand CBC-1 (Cask and Bottle Conditioning), Lallemand Nottingham, Lallemand Windsor (British Ale), Fermentis Safale S-04, Fermentis US-05, Siebel Inst. American Ale BRY 96, Wyeast American Wheat 1010, Wyeast German Ale 1007, Wyeast Kölsch 2565, Wyeast Kolsch II 2575-PC, White Labs Belgian Lager WLP815, White Labs Dusseldorf Alt WLP036, White Labs European Ale WLP011, White Labs German Ale / Kölsch WLP029, East Coast Yeast Kölschbier ECY21, Mangrove Jack Workhorse Beer Yeast, Siebel Inst. Alt Ale BRY 144, Wyeast American Ale 1056, Wyeast American Ale II 1272, Wyeast British Ale 1098, Wyeast British Ale II 1335, Wyeast Denny’s Favorite 501450, Wyeast English Special Bitter 1768-PC, Wyeast Irish Ale 1084, Wyeast London Ale 1028, Wyeast London Ale III 1318, Wyeast London ESB Ale 1968, Wyeast Northwest Ale 1332, Wyeast Ringwood Ale 1187, Wyeast Thames Valley Ale 1275, Wyeast Thames Valley Ale II 1882-PC, Wyeast West Yorkshire Ale 1469, Wyeast Whitbread Ale 1099, White Labs American Ale Yeast Blend WLP060, White Labs Bedford British Ale WLP006, White Labs British Ale WLP005, White Labs Burton Ale WLP023, White Labs California Ale V WLP051, White Labs California Ale WLP001, White Labs East Coast Ale WLP008, White Labs East Midlands Ale WLP039, White Labs English Ale WLP002, White Labs Essex Ale Yeast WLP022, White Labs Irish Ale WLP004, White Labs London Ale WLP013, White Labs Old Sonoma Ale WLP076, White Labs Pacific Ale WLP041, White Labs Whitbread Ale WLP017, Coopers Pure Brewers’ Yeast, Fermentis US-05, Muntons Premium Gold, Muntons Standard Yeast, Fermentis Safale S-04, Lallemand Nottingham, Lallemand Windsor (British Ale), Siebel Inst. American Ale BRY 96, White Labs American Hefeweizen Ale 320, White Labs Bavarian Weizen Ale 351, White Labs Belgian Wit Ale 400, White Labs Belgian Wit Ale II 410, White Labs Hefeweizen Ale 300, White Labs Hefeweizen IV Ale 380, Wyeast American Wheat 1010, Wyeast Bavarian Wheat 3638, Wyeast Bavarian Wheat Blend 3056, Wyeast Belgian Ardennes 3522, Wyeast Belgian Wheat 3942, Wyeast Belgian Witbier 3944, Wyeast Canadian / Belgian Ale 3864-PC, Wyeast Forbidden Fruit Yeast 3463, Wyeast German Wheat 3333, Wyeast Weihenstephan Weizen 3068, Siebel Institute Bavarian Weizen BRY 235, Fermentis Safbrew WB-06, Mangrove Jack Bavarian Wheat, Lallemand Munich (German Wheat Beer), Brewferm Blanche, Brewferm Lager, East Coast Yeast Belgian White ECY11, Augustiner, Augustiner Lager, W-34 / 70, Andechs, Andechs Lager, D254, RC212, BO213. In some embodiments, the yeast is S. cerevisiae strain Chico. Methods and Liquid Fermentation Compositions (and Fermented Products) Aspects of the present disclosure relate to methods of producing a fermented product using any of the genetically modified yeast cells described herein. The process of fermentation exploits a natural process of using microorganisms to convert carbohydrates into alcohol and carbon dioxide. It is a metabolic process that produces chemical changes in organic substrates through enzymatic action. In the context of food production, fermentation broadly refers to any process in which the activity of microorganisms brings about a desirable change to a food product or beverage. The conditions for fermentation and the carrying out of a fermentation is referred to herein as a “fermentation process.” In some aspects, the disclosure relates to a method of producing a fermented product, such as a fermented beverage, involving contacting any of the modified cells described herein with a medium comprising at least one fermentable sugar during a first fermentation process, to produce a fermented product. A “medium” as used herein, refers to liquid conducive to fermentation, meaning a liquid which does not inhibit or prevent the fermentation process. In some embodiments, the medium is water. In some embodiments, a method of producing a fermented beverage comprises: (a) providing a genetically modified yeast cell comprising a functional disruption in one or more enzymes associated with maltose and / or maltotriose transport, and / or maltose and / or maltotriose hydrolysis in the yeast cell, wherein the functional disruption(s) result in reduced growth of the yeast cell on maltose as a sole sugar source compared to a yeast cell not comprising the genetic modification, (b) providing a medium comprising a wort-derived sugar source, (c) combining the genetically modified yeast cell and the medium to form a fermentation composition, and (d) allowing the fermentation composition to ferment to produce the fermented beverage. In some embodiments, a method of producing a fermented beverage, comprising contacting a population of genetically modified yeast cells according to the present disclosure with a medium comprising a wort-derived sugar source during a fermentation process to produce the fermented beverage. In some embodiments, a fermented beverage produced by the methods disclosed herein is provided. In some embodiments, a fermented beverage comprising alcohol in an amount of no more than 1.0% (v / v) and nucleic acids from a genetically modified yeast cell of the present disclosure is provided. It should be understood that in the methods of the present disclosure, the modified cell of any aspect(s) of the present disclosure can be used. In some embodiments, the fermented beverage is a reduced alcohol fermented beverage. As used herein, “reduced alcohol fermented beverage” refers to a beverage containing less than if the same fermentation was performed with a strain that could metabolize maltose and maltotriose. In some embodiments, the fermented beverage has an alcohol content of less than or equal to about 1.0% (v / v) alcohol. In some embodiments, the fermented beverage has an alcohol content of less than or equal to about 0.5% (v / v) alcohol. In some embodiments, the method does not include a step of physically removing alcohol from the beverage or prematurely halting fermentation. In some embodiments, at least one fermentable sugar is provided in the wort-derived sugar source. In some embodiments, the fermentation process results in a reduction in the level of wort-derived sugar by at least 15% but not more than 25%. In some embodiments, the fermented beverage is beer. As also used herein, the term “fermentable sugar” refers to a carbohydrate that may be converted into an alcohol and carbon dioxide by a microorganism, such as any of the cells described herein. In some embodiments, the fermentable sugar is converted into an alcohol and carbon dioxide by an enzyme, such as a recombinant enzyme or a cell that expresses the enzyme. The genetically modified yeast cells described herein are not capable of converting maltose and / or maltotriose to ethanol (not capable of fermenting maltose and / or maltotriose). Accordingly, although maltose and / or maltotriose may be present in the medium (e.g., wort), the genetically modified yeast cells do not ferment these sugars to ethanol. Examples of fermentable sugars that may be utilized by the genetically modified yeast cells described herein include, without limitation, glucose, fructose, lactose, and sucrose. In some embodiments, the fermentable sugar is provided in a sugar source. The sugar source for use in the claimed methods may depend, for example, on the type of fermented product and the fermentable sugar. Examples of sugar sources include, without limitation, wort, grains / cereals, fruit juice (e.g., grape juice and apple juice / cider), honey, cane sugar, rice, and koji. Examples of fruits from which fruit juice can be obtained include, without limitation, grapes, apples, blueberries, blackberries, raspberries, currants, strawberries, cherries, pears, peaches, nectarines, oranges, pineapples, mangoes, and passionfruit. In some embodiments, the modified cells described herein are cultured in an anaerobic or semi-anaerobic environment. Anaerobic cell culture refers to the technique of culturing a microorganism, such as a modified yeast cell, in an environment without available oxygen. Semi-anaerobic cell culture refers to the technique of culturing a microorganism, such as a modified yeast cell, in an environment with limited oxygen availability, such as in a medium that has been pre-oxygenated. As will be evident to one of ordinary skill in the art, in some instances, it may be necessary to process the sugar source in order to make available the fermentable sugar for fermentation. Using beer production as an example fermented beverage, grains (cereal, barley) are steeped in water, which hydrates the grain and activates the malt enzymes that convert the starches to fermentable sugars, a process referred to as “mashing.” The grains are then boiled to concentrate the sugars and sterilize the solution. As used herein, the term “wort” refers to the liquid produced by the process of mashing and boiling, which contains the fermentable sugars. The wort is then exposed to a fermenting organism (e.g., any of the cells described herein), which allows enzymes of the fermenting organism to convert the sugars in the wort to alcohol and carbon dioxide. In some embodiments, the grains are malted, unmalted, or comprise a combination of malted and unmalted grains. Examples of grains for use in the methods described herein include, without limitation, barley, oats, maize, rice, rye, sorghum, wheat, karasumugi, and hatomugi. In the example of producing sake, the sugar source is rice, which is incubated with koji mold (Aspergillus oryzae) converting the rice starch to fermentable sugar, producing koji. The koji then is exposed to a fermenting organism (e.g., any of the cells described herein), which allows enzymes of the fermenting organism to convert the sugars in the koji to alcohol and carbon dioxide. In some embodiments, the methods described herein involve producing the medium, which may involve heating or steeping a sugar source, for example in water. In some embodiments, the water has a temperature of at least 50 degrees Celsius (50°C) and is incubated with a sugar source for a period of time. In some embodiments, the water has a temperature of at least 75°C and is incubated with a sugar source for a period of time. In some embodiments, the water has a temperature of at least 100°C and is incubated with a sugar source for a period of time. Preferably, the medium is cooled prior to addition of any of the cells described herein. In some embodiments, the methods described herein further comprise adding at least one (e.g., 1, 2, 3, 4, 5, or more) hop variety, for example to the medium, to a wort during a fermentation process. Hops are the flowers of the hops plant (Humulus lupulus) and are often used in fermentation to impart various flavors and aromas to the fermented product. Hops are considered to impart bitter flavoring in addition to floral, fruity, and / or citrus flavors and aromas and may be characterized based on the intended purpose. For example, bittering hops impart a level of bitterness to the fermented product due to the presence of alpha acids in the hop flowers, whereas aroma hops have lower lowers of alpha acids and contribute desirable aromas and flavor to the fermented product. Whether one or more variety of hops is added to the medium and / or the wort and stage during which the hops are added may be based on various factors, such as the intended purpose of the hops. For example, hops that are intended to impart a bitterness to the fermented product are typically added during preparation of the wort, for example during boiling of the wort. In some embodiments, hops that are intended to impart a bitterness to the fermented product are added to the wort and boiled with the wort for a period of time, for example, for about 15-60 minutes. In contrast, hops that are intended to impart desired aromas to the fermented product are typically added later than hops used for bitterness. In some embodiments, hops that are intended to impart desired aromas to the fermented product are added to at the end of the boil or after the wort is boiled (i.e., “dry hopping”). In some embodiments, one or more varieties of hops may be added at multiple times (e.g., at least twice, at least three times, or more) during the method. In some embodiments, the hops are added in the form of either wet or dried hops and may optionally be boiled with the wort. In some embodiments, the hops are in the form of dried hop pellets. In some embodiments, at least one variety of hops is added to the medium. In some embodiments, the hops are wet (i.e., undried). In some embodiments, the hops are dried, and optionally may be further processed prior to use. In some embodiments, the hops are added to the wort prior to the fermentation process. In some embodiments, the hops are boiled in the wort. In some embodiments, the hops are boiled with the wort and then cooled with the wort. Many varieties of hops are known in the art and may be used in the methods described herein. Examples of hop varieties include, without limitation, Ahtanum, Amarillo, Apollo, Cascade, Centennial, Chinook, Citra, Cluster, Columbus, Crystal / Chrystal, Eroica, Galena, Glacier, Greenburg, Horizon, Liberty, Millennium, Mosaic, Mount Hood, Mount Rainier, Newport, Nugget, Palisade, Santiam, Simcoe, Sterling, Summit, Tomahawk, Ultra, Vanguard, Warrior, Willamette, Zeus, Admiral, Brewer's Gold, Bullion, Challenger, First Gold, Fuggles, Goldings, Herald, Northdown, Northern Brewer, Phoenix, Pilot, Pioneer, Progress, Target, Whitbread Golding Variety (WGV), Hallertau, Hersbrucker, Saaz, Tettnang, Spalt, Feux-Coeur Francais, Galaxy, Green Bullet, Motueka, Nelson Sauvin, Pacific Gem, Pacific Jade, Pacifica, Pride of Ringwood, Riwaka, Southern Cross, Lublin, Magnum, Perle, Polnischer Lublin, Saphir, Satus, Select, Strisselspalt, Styrian Goldings, Tardif de Bourgogne, Tradition, Bravo, Calypso, Chelan, Comet, El Dorado, San Juan Ruby Red, Sonnet Golding, Super Galena, Tillicum, Bramling Cross, Pilgrim, Hallertauer Herkules, Hallertauer Magnum, Hallertauer Taurus, Merkur, Opal, Smaragd, Halleratau Aroma, Kohatu, Rakau, Stella, Sticklebract, Summer Saaz, Super Alpha, Super Pride, Topaz, Wai-iti, Bor, Junga, Marynka, Premiant, Sladek, Styrian Atlas, Styrian Aurora, Styrian Bobek, Styrian Celeia, Sybilla Sorachi Ace, Hallertauer Mittelfrueh, Hallertauer Tradition, Tettnanger, Tahoma, Triple Pearl, Yakima Gold, and Michigan Copper. In some embodiments, the fermentation process of at least one sugar source comprising at least one fermentable sugar may be carried out for about 1 day to about 31 days. In some embodiments, the fermentation process is performed for about 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 30 days, 31 days or longer. In some embodiments, the fermentation process of the one or more fermentable sugars may be performed at a temperature of about 4°C to about 30°C. In some embodiments, the fermentation process of one or more fermentable sugars may be carried out at temperature of about 8°C to about 14°C or about 18°C to about 24°C. In some embodiments, the fermentation process of one or more fermentable sugars may be performed at a temperature of about 4°C, 5°C, 6°C, 7°C, 8°C, 9°C, 10°C, 11°C, 12°C, 13°C, 14°C, 15°C, 16°C, 17°C, 18°C, 19°C, 20°C, 21°C, 22°C, 23°C, 24°C, 25°C, 26°C, 27°C, 28°C, 29°C, or 30°C. In some embodiments, fermentation results in the reduction of the amount of fermentable sugar present in a medium, referred to as attenuation. In some embodiments, the reduction in the amount of fermentable sugar occurs within 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 15 days, 16 days, 17 days, 18 days, 19 days, 20 days, 21 days, 22 days, 23 days, 24 days, 25 days, 26 days, 27 days, 28 days, 29 days, 30 days, 31 days, or longer, from the start of fermentation. In some embodiments, fermentation methods using the genetically modified yeast cells described herein result in a reduction of the amount of fermentable sugar by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, or at least 35%. In some embodiments, the modified cell or cells ferment a reduced amount of fermentable sugar relative to the amount of fermentable sugar fermented by wild-type yeast cells in the same amount of time or during a fermentation process. In some embodiments, the modified cell or cells ferment an amount of fermentable sugar that is up to 90% (e.g., 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, or 90%) relative to the amount of fermentable sugar fermented by wild-type yeast cells in the same amount of time or during a fermentation process. In some embodiments, fermentation results in a level of acetate esters in the fermented product (e.g. beer). In some embodiments, the fermented product comprises isoamyl acetate in an amount from about 10 µg / L to about 4000 µg / L. In some embodiments, the fermented product comprises isoamyl acetate in an amount from about 9.1 µg / L to about 4000 µg / L, about 9.2 µg / L to about 4000 µg / L, about 10 µg / L to about 4000 µg / L, about 20 µg / L to about 4000 µg / L, about 30 µg / L to about 4000 µg / L, about 40 µg / L to about 4000 µg / L, about 50 µg / L to about 4000 µg / L, about 60 µg / L to about 4000 µg / L, about 69.6 µg / L to about 4000 µg / L, about 70 µg / L to about 4000 µg / L, about 80 µg / L to about 4000 µg / L, about 90 µg / L to about 4000 µg / L, about 100 µg / L to about 4000 µg / L, about 150 µg / L to about 4000 µg / L, about 200 µg / L to about 4000 µg / L, about 250 µg / L to about 4000 µg / L, about 300 µg / L to about 4000 µg / L, about 400 µg / L to about 4000 µg / L, about 500 µg / L to about 4000 µg / L, about 600 µg / L to about 4000 µg / L, about 750 µg / L to about 4000 µg / L, about 800 µg / L to about 4000 µg / L, about 1000 µg / L to about 4000 µg / L, about 2000 µg / L to about 4000 µg / L, about 9.1 µg / L to about 3000 µg / L, about 9.2 µg / L to about 3000 µg / L, about 10 µg / L to about 3000 µg / L, about 20 µg / L to about 3000 µg / L, about 30 µg / L to about 3000 µg / L, about 40 µg / L to about 3000 µg / L, about 50 µg / L to about 3000 µg / L, about 60 µg / L to about 3000 µg / L, about 69.6 µg / L to about 3000 µg / L, about 70 µg / L to about 3000 µg / L, about 80 µg / L to about 3000 µg / L, about 90 µg / L to about 3000 µg / L, about 100 µg / L to about 3000 µg / L, about 150 µg / L to about 3000 µg / L, about 200 µg / L to about 3000 µg / L, about 250 µg / L to about 3000 µg / L, about 300 µg / L to about 3000 µg / L, about 400 µg / L to about 3000 µg / L, about 500 µg / L to about 3000 µg / L, about 600 µg / L to about 3000 µg / L, about 750 µg / L to about 3000 µg / L, about 800 µg / L to about 3000 µg / L, about 1000 µg / L to about 3000 µg / L, about 2000 µg / L to about 3000 µg / L, about 9.1 µg / L to about 2000 µg / L, about 9.2 µg / L to about 2000 µg / L, about 10 µg / L to about 2000 µg / L, about 20 µg / L to about 2000 µg / L, about 30 µg / L to about 2000 µg / L, about 40 µg / L to about 2000 µg / L, about 50 µg / L to about 2000 µg / L, about 60 µg / L to about 2000 µg / L, about 69.6 µg / L to about 2000 µg / L, about 70 µg / L to about 2000 µg / L, about 80 µg / L to about 2000 µg / L, about 90 µg / L to about 2000 µg / L, about 100 µg / L to about 2000 µg / L, about 150 µg / L to about 2000 µg / L, about 200 µg / L to about 2000 µg / L, about 250 µg / L to about 2000 µg / L, about 300 µg / L to about 2000 µg / L, about 400 µg / L to about 2000 µg / L, about 500 µg / L to about 2000 µg / L, about 600 µg / L to about 2000 µg / L, about 750 µg / L to about 2000 µg / L, about 800 µg / L to about 2000 µg / L, about 1000 µg / L to about 2000 µg / L, about 9.1 µg / L to about 1250 µg / L, about 9.2 µg / L to about 1250 µg / L, about 10 µg / L to about 1250 µg / L, about 20 µg / L to about 1250 µg / L, about 30 µg / L to about 1250 µg / L, about 40 µg / L to about 1250 µg / L, about 50 µg / L to about 1250 µg / L, about 60 µg / L to about 1250 µg / L, about 69.6 µg / L to about 1250 µg / L, about 70 µg / L to about 1250 µg / L, about 80 µg / L to about 1250 µg / L, about 90 µg / L to about 1250 µg / L, about 100 µg / L to about 1250 µg / L, about 150 µg / L to about 1250 µg / L, about 200 µg / L to about 1250 µg / L, about 250 µg / L to about 1250 µg / L, about 300 µg / L to about 1250 µg / L, about 400 µg / L to about 1250 µg / L, about 500 µg / L to about 1250 µg / L, about 600 µg / L to about 1250 µg / L, about 750 µg / L to about 1250 µg / L, about 800 µg / L to about 1250 µg / L, about 1000 µg / L to about 1250 µg / L, about 9.1 µg / L to about 1100 µg / L, about 9.2 µg / L to about 1100 µg / L, about 10 µg / L to about 1100 µg / L, about 20 µg / L to about 1100 µg / L, about 30 µg / L to about 1100 µg / L, about 40 µg / L to about 1100 µg / L, about 50 µg / L to about 1100 µg / L, about 60 µg / L to about 1100 µg / L, about 69.6 µg / L to about 1100 µg / L, about 70 µg / L to about 1100 µg / L, about 80 µg / L to about 1100 µg / L, about 90 µg / L to about 1100 µg / L, about 100 µg / L to about 1100 µg / L, about 150 µg / L to about 1100 µg / L, about 200 µg / L to about 1100 µg / L, about 250 µg / L to about 1100 µg / L, about 300 µg / L to about 1100 µg / L, about 400 µg / L to about 1100 µg / L, about 500 µg / L to about 1100 µg / L, about 600 µg / L to about 1100 µg / L, about 750 µg / L to about 1100 µg / L, about 800 µg / L to about 1100 µg / L, about 1000 µg / L to about 1100 µg / L, about 9.1 µg / L to about 1023.3 µg / L, about 9.2 µg / L to about 1023.3 µg / L, about 10 µg / L to about 1023.3 µg / L, about 20 µg / L to about 1023.3 µg / L, about 30 µg / L to about 1023.3 µg / L, about 40 µg / L to about 1023.3 µg / L, about 50 µg / L to about 1023.3 µg / L, about 60 µg / L to about 1023.3 µg / L, about 69.6 µg / L to about 1023.3 µg / L, about 70 µg / L to about 1023.3 µg / L, about 80 µg / L to about 1023.3 µg / L, about 90 µg / L to about 1023.3 µg / L, about 100 µg / L to about 1023.3 µg / L, about 150 µg / L to about 1023.3 µg / L, about 200 µg / L to about 1023.3 µg / L, about 250 µg / L to about 1023.3 µg / L, about 300 µg / L to about 1023.3 µg / L, about 400 µg / L to about 1023.3 µg / L, about 500 µg / L to about 1023.3 µg / L, about 600 µg / L to about 1023.3 µg / L, about 750 µg / L to about 1023.3 µg / L, about 800 µg / L to about 1023.3 µg / L, about 1000 µg / L to about 1023.3 µg / L, about 9.1 µg / L to about 1000 µg / L, about 9.2 µg / L to about 1000 µg / L, about 10 µg / L to about 1000 µg / L, about 20 µg / L to about 1000 µg / L, about 30 µg / L to about 1000 µg / L, about 40 µg / L to about 1000 µg / L, about 50 µg / L to about 1000 µg / L, about 60 µg / L to about 1000 µg / L, about 69.6 µg / L to about 1000 µg / L, about 70 µg / L to about 1000 µg / L, about 80 µg / L to about 1000 µg / L, about 90 µg / L to about 1000 µg / L, about 100 µg / L to about 1000 µg / L, about 150 µg / L to about 1000 µg / L, about 200 µg / L to about 1000 µg / L, about 250 µg / L to about 1000 µg / L, about 300 µg / L to about 1000 µg / L, about 400 µg / L to about 1000 µg / L, about 500 µg / L to about 1000 µg / L, about 600 µg / L to about 1000 µg / L, about 750 µg / L to about 1000 µg / L, about 800 µg / L to about 1000 µg / L, about 9.1 µg / L to about 812.8 µg / L, about 9.2 µg / L to about 812.8 µg / L, about 10 µg / L to about 812.8 µg / L, about 20 µg / L to about 812.8 µg / L, about 30 µg / L to about 812.8 µg / L, about 40 µg / L to about 812.8 µg / L, about 50 µg / L to about 812.8 µg / L, about 60 µg / L to about 812.8 µg / L, about 69.6 µg / L to about 812.8 µg / L, about 70 µg / L to about 812.8 µg / L, about 80 µg / L to about 812.8 µg / L, about 90 µg / L to about 812.8 µg / L, about 100 µg / L to about 812.8 µg / L, about 150 µg / L to about 812.8 µg / L, about 200 µg / L to about 812.8 µg / L, about 250 µg / L to about 812.8 µg / L, about 300 µg / L to about 812.8 µg / L, about 400 µg / L to about 812.8 µg / L, about 500 µg / L to about 812.8 µg / L, about 600 µg / L to about 812.8 µg / L, about 9.1 µg / L to about 800 µg / L, about 9.2 µg / L to about 800 µg / L, about 10 µg / L to about 800 µg / L, about 20 µg / L to about 800 µg / L, about 30 µg / L to about 800 µg / L, about 40 µg / L to about 800 µg / L, about 50 µg / L to about 800 µg / L, about 60 µg / L to about 800 µg / L, about 69.6 µg / L to about 800 µg / L, about 70 µg / L to about 800 µg / L, about 80 µg / L to about 800 µg / L, about 90 µg / L to about 800 µg / L, about 100 µg / L to about 800 µg / L, about 150 µg / L to about 800 µg / L, about 200 µg / L to about 800 µg / L, about 250 µg / L to about 800 µg / L, about 300 µg / L to about 800 µg / L, about 400 µg / L to about 800 µg / L, about 500 µg / L to about 800 µg / L, about 600 µg / L to about 800 µg / L, about 750 µg / L to about 800 µg / L, about 9.1 µg / L to about 766 µg / L, about 9.2 µg / L to about 766 µg / L, about 10 µg / L to about 766 µg / L, about 20 µg / L to about 766 µg / L, about 30 µg / L to about 766 µg / L, about 40 µg / L to about 766 µg / L, about 50 µg / L to about 766 µg / L, about 60 µg / L to about 766 µg / L, about 69.6 µg / L to about 766 µg / L, about 70 µg / L to about 766 µg / L, about 80 µg / L to about 766 µg / L, about 90 µg / L to about 766 µg / L, about 100 µg / L to about 766 µg / L, about 150 µg / L to about 766 µg / L, about 200 µg / L to about 766 µg / L, about 250 µg / L to about 766 µg / L, about 300 µg / L to about 766 µg / L, about 400 µg / L to about 766 µg / L, about 500 µg / L to about 766 µg / L, about 600 µg / L to about 766 µg / L, about 750 µg / L to about 766 µg / L, about 9.1 µg / L to about 750 µg / L, about 9.2 µg / L to about 750 µg / L, about 10 µg / L to about 750 µg / L, about 20 µg / L to about 750 µg / L, about 30 µg / L to about 750 µg / L, about 40 µg / L to about 750 µg / L, about 50 µg / L to about 750 µg / L, about 60 µg / L to about 750 µg / L, about 69.6 µg / L to about 750 µg / L, about 70 µg / L to about 750 µg / L, about 80 µg / L to about 750 µg / L, about 90 µg / L to about 750 µg / L, about 100 µg / L to about 750 µg / L, about 150 µg / L to about 750 µg / L, about 200 µg / L to about 750 µg / L, about 250 µg / L to about 750 µg / L, about 300 µg / L to about 750 µg / L, about 400 µg / L to about 750 µg / L, about 500 µg / L to about 750 µg / L, about 600 µg / L to about 750 µg / L, about 9.1 µg / L to about 600 µg / L, about 9.2 µg / L to about 600 µg / L, about 10 µg / L to about 600 µg / L, about 20 µg / L to about 600 µg / L, about 30 µg / L to about 600 µg / L, about 40 µg / L to about 600 µg / L, about 50 µg / L to about 600 µg / L, about 60 µg / L to about 600 µg / L, about 69.6 µg / L to about 600 µg / L, about 70 µg / L to about 600 µg / L, about 80 µg / L to about 600 µg / L, about 90 µg / L to about 600 µg / L, about 100 µg / L to about 600 µg / L, about 150 µg / L to about 600 µg / L, about 200 µg / L to about 600 µg / L, about 250 µg / L to about 600 µg / L, about 300 µg / L to about 600 µg / L, about 400 µg / L to about 600 µg / L, about 500 µg / L to about 600 µg / L, about 9.1 µg / L to about 500 µg / L, about 9.2 µg / L to about 500 µg / L, about 10 µg / L to about 500 µg / L, about 20 µg / L to about 500 µg / L, about 30 µg / L to about 500 µg / L, about 40 µg / L to about 500 µg / L, about 50 µg / L to about 500 µg / L, about 60 µg / L to about 500 µg / L, about 69.6 µg / L to about 500 µg / L, about 70 µg / L to about 500 µg / L, about 80 µg / L to about 500 µg / L, about 90 µg / L to about 500 µg / L, about 100 µg / L to about 500 µg / L, about 150 µg / L to about 500 µg / L, about 200 µg / L to about 500 µg / L, about 250 µg / L to about 500 µg / L, about 300 µg / L to about 500 µg / L, about 400 µg / L to about 500 µg / L, about 9.1 µg / L to about 400 µg / L, about 9.2 µg / L to about 400 µg / L, about 10 µg / L to about 400 µg / L, about 20 µg / L to about 400 µg / L, about 30 µg / L to about 400 µg / L, about 40 µg / L to about 400 µg / L, about 50 µg / L to about 400 µg / L, about 60 µg / L to about 400 µg / L, about 69.6 µg / L to about 400 µg / L, about 70 µg / L to about 400 µg / L, about 80 µg / L to about 400 µg / L, about 90 µg / L to about 400 µg / L, about 100 µg / L to about 400 µg / L, about 150 µg / L to about 400 µg / L, about 200 µg / L to about 400 µg / L, about 250 µg / L to about 400 µg / L, about 300 µg / L to about 400 µg / L, about 9.1 µg / L to about 300 µg / L, about 9.2 µg / L to about 300 µg / L, about 10 µg / L to about 300 µg / L, about 20 µg / L to about 300 µg / L, about 30 µg / L to about 300 µg / L, about 40 µg / L to about 300 µg / L, about 50 µg / L to about 300 µg / L, about 60 µg / L to about 300 µg / L, about 69.6 µg / L to about 300 µg / L, about 70 µg / L to about 300 µg / L, about 80 µg / L to about 300 µg / L, about 90 µg / L to about 300 µg / L, about 100 µg / L to about 300 µg / L, about 150 µg / L to about 300 µg / L, about 200 µg / L to about 300 µg / L, about 250 µg / L to about 300 µg / L, about 9.1 µg / L to about 250 µg / L, about 9.2 µg / L to about 250 µg / L, about 10 µg / L to about 250 µg / L, about 20 µg / L to about 250 µg / L, about 30 µg / L to about 250 µg / L, about 40 µg / L to about 250 µg / L, about 50 µg / L to about 250 µg / L, about 60 µg / L to about 250 µg / L, about 69.6 µg / L to about 250 µg / L, about 70 µg / L to about 250 µg / L, about 80 µg / L to about 250 µg / L, about 90 µg / L to about 250 µg / L, about 100 µg / L to about 250 µg / L, about 150 µg / L to about 250 µg / L, about 200 µg / L to about 250 µg / L, about 9.1 µg / L to about 200 µg / L, about 9.2 µg / L to about 200 µg / L, about 10 µg / L to about 200 µg / L, about 20 µg / L to about 200 µg / L, about 30 µg / L to about 200 µg / L, about 40 µg / L to about 200 µg / L, about 50 µg / L to about 200 µg / L, about 60 µg / L to about 200 µg / L, about 69.6 µg / L to about 200 µg / L, about 80 µg / L to about 200 µg / L, about 90 µg / L to about 200 µg / L, about 100 µg / L to about 200 µg / L, about 150 µg / L to about 200 µg / L, about 9.1 µg / L to about 150 µg / L, about 9.2 µg / L to about 150 µg / L, about 10 µg / L to about 150 µg / L, about 20 µg / L to about 150 µg / L, about 30 µg / L to about 150 µg / L, about 40 µg / L to about 150 µg / L, about 50 µg / L to about 150 µg / L, about 60 µg / L to about 150 µg / L, about 69.6 µg / L to about 150 µg / L, about 70 µg / L to about 200 µg / L, about 80 µg / L to about 150 µg / L, about 90 µg / L to about 150 µg / L, about 100 µg / L to about 150 µg / L, about 9.1 µg / L to about 100 µg / L, about 9.2 µg / L to about 100 µg / L, about 10 µg / L to about 100 µg / L, about 20 µg / L to about 100 µg / L, about 30 µg / L to about 100 µg / L, about 40 µg / L to about 100 µg / L, about 50 µg / L to about 100 µg / L, about 60 µg / L to about 100 µg / L, about 69.6 µg / L to about 100 µg / L, about 70 µg / L to about 100 µg / L, about 80 µg / L to about 100 µg / L, about 90 µg / L to about 100 µg / L, about 9.1 µg / L to about 90 µg / L, about 9.2 µg / L to about 90 µg / L, about 10 µg / L to about 90 µg / L, about 20 µg / L to about 90 µg / L, about 30 µg / L to about 90 µg / L, about 40 µg / L to about 90 µg / L, about 50 µg / L to about 90 µg / L, about 60 µg / L to about 90 µg / L, about 69.6 µg / L to about 90 µg / L, about 70 µg / L to about 90 µg / L, about 80 µg / L to about 90 µg / L, about 9.1 µg / L to about 80 µg / L, about 9.2 µg / L to about 80 µg / L, about 10 µg / L to about 80 µg / L, about 20 µg / L to about 80 µg / L, about 30 µg / L to about 80 µg / L, about 40 µg / L to about 80 µg / L, about 50 µg / L to about 80 µg / L, about 60 µg / L to about 80 µg / L, about 69.6 µg / L to about 80 µg / L, about 70 µg / L to about 80 µg / L, about 9.1 µg / L to about 70 µg / L, about 9.2 µg / L to about 70 µg / L, about 10 µg / L to about 70 µg / L, about 20 µg / L to about 70 µg / L, about 30 µg / L to about 70 µg / L, about 40 µg / L to about 70 µg / L, about 50 µg / L to about 70 µg / L, about 60 µg / L to about 70 µg / L, about 69.6 µg / L to about 70 µg / L, about 9.1 µg / L to about 60 µg / L, about 9.2 µg / L to about 60 µg / L, about 10 µg / L to about 60 µg / L, about 20 µg / L to about 60 µg / L, about 30 µg / L to about 60 µg / L, about 40 µg / L to about 60 µg / L, about 50 µg / L to about 60 µg / L, about 9.1 µg / L to about 50 µg / L, about 9.2 µg / L to about 50 µg / L, about 10 µg / L to about 50 µg / L, about 20 µg / L to about 50 µg / L, about 30 µg / L to about 50 µg / L, about 40 µg / L to about 50 µg / L, about 9.1 µg / L to about 40 µg / L, about 9.2 µg / L to about 40 µg / L, about 10 µg / L to about 40 µg / L, about 20 µg / L to about 40 µg / L, about 30 µg / L to about 40 µg / L, about 9.1 µg / L to about 30 µg / L, about 9.2 µg / L to about 30 µg / L, about 10 µg / L to about 30 µg / L, about 20 µg / L to about 30 µg / L, about 9.1 µg / L to about 20 µg / L, about 9.2 µg / L to about 20 µg / L, about 10 µg / L to about 20 µg / L, or about 9.1, 9.2, 10, 20, 30, 40, 50, 60, 69.6, 70, 80, 90, 100, 150, 200, 250, 300, 400, 500, 600, 750, 766, 800, 812.8, 1000, 1100, 1023.3, 1250, 2000, 3000 or 4000 µg / L or any range or value therebetween. In some embodiments, the fermented product comprises isoamyl acetate in an amount from about 69.6 µg / L to about 766 µg / L. In some embodiments, the fermented product comprises isoamyl acetate in an amount from about 9.2 µg / L to about 812.8 µg / L. In some embodiments, the fermented product comprises phenethyl acetate in an amount from about 2.3 µg / L to about 1500 µg / L. In some embodiments, the fermented product comprises phenethyl acetate in an amount from about 2.3 µg / L to about 1500 µg / L, 5 µg / L to about 1500 µg / L, about 10 µg / L to about 1500 µg / L, about 20 µg / L to about 1500 µg / L, about 25 µg / L to about 1500 µg / L, about 30 µg / L to about 1500 µg / L, about 40 µg / L to about 1500 µg / L, about 47.2 µg / L to about 1500 µg / L, about 50 µg / L to about 1500 µg / L, about 60 µg / L to about 1500 µg / L, about 70 µg / L to about 1500 µg / L, about 80 µg / L to about 1500 µg / L, about 89.2 µg / L to about 1500 µg / L, about 90 µg / L to about 1500 µg / L, about 100 µg / L to about 1500 µg / L, about 150 µg / L to about 1500 µg / L, about 200 µg / L to about 1500 µg / L, about 250 µg / L to about 1500 µg / L, about 300 µg / L to about 1500 µg / L, about 400 µg / L to about 1500 µg / L, about 500 µg / L to about 1500 µg / L, about 600 µg / L to about 1500 µg / L, about 750 µg / L to about 1500 µg / L, about 800 µg / L to about 1500 µg / L, about 900 µg / L to about 1500 µg / L, about 1000 µg / L to about 1500 µg / L, about 1100 µg / L to about 1500 µg / L, about 1200 µg / L to about 1500 µg / L, about 1250 µg / L to about 1500 µg / L, about 1300 µg / L to about 1500 µg / L, about 1400 µg / L to about 1500 µg / L, about 2.3 µg / L to about 1400 µg / L, about 5 µg / L to about 1400 µg / L, about 10 µg / L to about 1400 µg / L, about 20 µg / L to about 1400 µg / L, about 25 µg / L to about 1400 µg / L, about 30 µg / L to about 1400 µg / L, about 40 µg / L to about 1400 µg / L, about 47.2 µg / L to about 1400 µg / L, about 50 µg / L to about 1400 µg / L, about 60 µg / L to about 1400 µg / L, about 70 µg / L to about 1400 µg / L, about 80 µg / L to about 1400 µg / L, about 89.2 µg / L to about 1400 µg / L, about 90 µg / L to about 1400 µg / L, about 100 µg / L to about 1400 µg / L, about 150 µg / L to about 1400 µg / L, about 200 µg / L to about 1400 µg / L, about 250 µg / L to about 1400 µg / L, about 300 µg / L to about 1400 µg / L, about 400 µg / L to about 1400 µg / L, about 500 µg / L to about 1400 µg / L, about 600 µg / L to about 1400 µg / L, about 750 µg / L to about 1400 µg / L, about 800 µg / L to about 1400 µg / L, about 900 µg / L to about 1400 µg / L, about 1000 µg / L to about 1400 µg / L, about 1100 µg / L to about 1400 µg / L, about 1200 µg / L to about 1400 µg / L, about 1250 µg / L to about 1400 µg / L, about 1300 µg / L to about 1400 µg / L, about 2.3 µg / L to about 1300 µg / L, about 5 µg / L to about 1300 µg / L, about 10 µg / L to about 1300 µg / L, about 20 µg / L to about 1300 µg / L, about 25 µg / L to about 1300 µg / L, about 30 µg / L to about 1300 µg / L, about 40 µg / L to about 1300 µg / L, about 47.2 µg / L to about 1300 µg / L, about 50 µg / L to about 1300 µg / L, about 60 µg / L to about 1300 µg / L, about 70 µg / L to about 1300 µg / L, about 80 µg / L to about 1300 µg / L, about 89.2 µg / L to about 1300 µg / L, about 90 µg / L to about 1300 µg / L, about 100 µg / L to about 1300 µg / L, about 150 µg / L to about 1300 µg / L, about 200 µg / L to about 1300 µg / L, about 250 µg / L to about 1300 µg / L, about 300 µg / L to about 1300 µg / L, about 400 µg / L to about 1300 µg / L, about 500 µg / L to about 1300 µg / L, about 600 µg / L to about 1300 µg / L, about 750 µg / L to about 1300 µg / L, about 800 µg / L to about 1300 µg / L, about 900 µg / L to about 1300 µg / L, about 1000 µg / L to about 1300 µg / L, about 1100 µg / L to about 1300 µg / L, about 1200 µg / L to about 1300 µg / L, about 1250 µg / L to about 1300 µg / L, about 2.3 µg / L to about 1250 µg / L, about 5 µg / L to about 1250 µg / L, about 10 µg / L to about 1250 µg / L, about 20 µg / L to about 1250 µg / L, about 25 µg / L to about 1250 µg / L, about 30 µg / L to about 1250 µg / L, about 40 µg / L to about 1250 µg / L, about 47.2 µg / L to about 1250 µg / L, about 50 µg / L to about 1250 µg / L, about 60 µg / L to about 1250 µg / L, about 70 µg / L to about 1250 µg / L, about 80 µg / L to about 1250 µg / L, about 89.2 µg / L to about 1250 µg / L, about 90 µg / L to about 1250 µg / L, about 100 µg / L to about 1250 µg / L, about 150 µg / L to about 1250 µg / L, about 200 µg / L to about 1250 µg / L, about 250 µg / L to about 1250 µg / L, about 300 µg / L to about 1250 µg / L, about 400 µg / L to about 1250 µg / L, about 500 µg / L to about 1250 µg / L, about 600 µg / L to about 1250 µg / L, about 750 µg / L to about 1250 µg / L, about 800 µg / L to about 1250 µg / L, about 900 µg / L to about 1250 µg / L, about 1000 µg / L to about 1250 µg / L, about 1100 µg / L to about 1250 µg / L, about 1200 µg / L to about 1250 µg / L, about 2.3 µg / L to about 1200 µg / L, about 5 µg / L to about 1200 µg / L, about 10 µg / L to about 1200 µg / L, about 20 µg / L to about 1200 µg / L, about 25 µg / L to about 1200 µg / L, about 30 µg / L to about 1200 µg / L, about 40 µg / L to about 1200 µg / L, about 47.2 µg / L to about 1200 µg / L, about 50 µg / L to about 1200 µg / L, about 60 µg / L to about 1200 µg / L, about 70 µg / L to about 1200 µg / L, about 80 µg / L to about 1200 µg / L, about 89.2 µg / L to about 1200 µg / L, about 90 µg / L to about 1200 µg / L, about 100 µg / L to about 1200 µg / L, about 150 µg / L to about 1200 µg / L, about 200 µg / L to about 1200 µg / L, about 250 µg / L to about 1200 µg / L, about 300 µg / L to about 1200 µg / L, about 400 µg / L to about 1200 µg / L, about 500 µg / L to about 1200 µg / L, about 600 µg / L to about 1200 µg / L, about 750 µg / L to about 1200 µg / L, about 800 µg / L to about 1200 µg / L, about 900 µg / L to about 1200 µg / L, about 1000 µg / L to about 1200 µg / L, about 1100 µg / L to about 1200 µg / L, about 2.3 µg / L to about 1100 µg / L, about 5 µg / L to about 1100 µg / L, about 10 µg / L to about 1100 µg / L, about 20 µg / L to about 1100 µg / L, about 25 µg / L to about 1100 µg / L, about 30 µg / L to about 1100 µg / L, about 40 µg / L to about 1100 µg / L, about 47.2 µg / L to about 1100 µg / L, about 50 µg / L to about 1100 µg / L, about 60 µg / L to about 1100 µg / L, about 70 µg / L to about 1100 µg / L, about 80 µg / L to about 1100 µg / L, about 89.2 µg / L to about 1100 µg / L, about 90 µg / L to about 1100 µg / L, about 100 µg / L to about 1100 µg / L, about 150 µg / L to about 1100 µg / L, about 200 µg / L to about 1100 µg / L, about 250 µg / L to about 1100 µg / L, about 300 µg / L to about 1100 µg / L, about 400 µg / L to about 1100 µg / L, about 500 µg / L to about 1100 µg / L, about 600 µg / L to about 1100 µg / L, about 750 µg / L to about 1100 µg / L, about 800 µg / L to about 1100 µg / L, about 900 µg / L to about 1100 µg / L, about 1000 µg / L to about 1100 µg / L, about 2.3 µg / L to about 1000 µg / L, about 5 µg / L to about 1000 µg / L, about 10 µg / L to about 1000 µg / L, about 20 µg / L to about 1000 µg / L, about 25 µg / L to about 1000 µg / L, about 30 µg / L to about 1000 µg / L, about 40 µg / L to about 1000 µg / L, about 47.2 µg / L to about 1000 µg / L, about 50 µg / L to about 1000 µg / L, about 60 µg / L to about 1000 µg / L, about 70 µg / L to about 1000 µg / L, about 80 µg / L to about 1000 µg / L, about 89.2 µg / L to about 1000 µg / L, about 90 µg / L to about 1000 µg / L, about 100 µg / L to about 1000 µg / L, about 150 µg / L to about 1000 µg / L, about 200 µg / L to about 1000 µg / L, about 250 µg / L to about 1000 µg / L, about 300 µg / L to about 1000 µg / L, about 400 µg / L to about 1000 µg / L, about 500 µg / L to about 1000 µg / L, about 600 µg / L to about 1000 µg / L, about 750 µg / L to about 1000 µg / L, about 800 µg / L to about 1000 µg / L, about 900 µg / L to about 1000 µg / L, about 2.3 µg / L to about 900 µg / L, about 5 µg / L to about 900 µg / L, about 10 µg / L to about 900 µg / L, about 20 µg / L to about 900 µg / L, about 25 µg / L to about 900 µg / L, about 30 µg / L to about 900 µg / L, about 40 µg / L to about 900 µg / L, about 47.2 µg / L to about 900 µg / L, about 50 µg / L to about 900 µg / L, about 60 µg / L to about 900 µg / L, about 70 µg / L to about 900 µg / L, about 80 µg / L to about 900 µg / L, about 89.2 µg / L to about 900 µg / L, about 90 µg / L to about 900 µg / L, about 100 µg / L to about 900 µg / L, about 150 µg / L to about 900 µg / L, about 200 µg / L to about 900 µg / L, about 250 µg / L to about 900 µg / L, about 300 µg / L to about 900 µg / L, about 400 µg / L to about 900 µg / L, about 500 µg / L to about 900 µg / L, about 600 µg / L to about 900 µg / L, about 750 µg / L to about 900 µg / L, about 800 µg / L to about 900 µg / L, about 2.3 µg / L to about 800 µg / L, about 5 µg / L to about 800 µg / L, about 10 µg / L to about 800 µg / L, about 20 µg / L to about 800 µg / L, about 25 µg / L to about 800 µg / L, about 30 µg / L to about 800 µg / L, about 40 µg / L to about 800 µg / L, about 47.2 µg / L to about 800 µg / L, about 50 µg / L to about 800 µg / L, about 60 µg / L to about 800 µg / L, about 70 µg / L to about 800 µg / L, about 80 µg / L to about 800 µg / L, about 89.2 µg / L to about 800 µg / L, about 90 µg / L to about 800 µg / L, about 100 µg / L to about 800 µg / L, about 150 µg / L to about 800 µg / L, about 200 µg / L to about 800 µg / L, about 250 µg / L to about 800 µg / L, about 300 µg / L to about 800 µg / L, about 400 µg / L to about 800 µg / L, about 500 µg / L to about 800 µg / L, about 600 µg / L to about 800 µg / L, about 750 µg / L to about 800 µg / L, about 2.3 µg / L to about 750 µg / L, about 5 µg / L to about 750 µg / L, about 10 µg / L to about 750 µg / L, about 20 µg / L to about 750 µg / L, about 25 µg / L to about 750 µg / L, about 30 µg / L to about 750 µg / L, about 40 µg / L to about 750 µg / L, about 47.2 µg / L to about 750 µg / L, about 50 µg / L to about 750 µg / L, about 60 µg / L to about 750 µg / L, about 70 µg / L to about 750 µg / L, about 80 µg / L to about 750 µg / L, about 89.2 µg / L to about 750 µg / L, about 90 µg / L to about 750 µg / L, about 100 µg / L to about 750 µg / L, about 150 µg / L to about 750 µg / L, about 200 µg / L to about 750 µg / L, about 250 µg / L to about 750 µg / L, about 300 µg / L to about 750 µg / L, about 400 µg / L to about 750 µg / L, about 500 µg / L to about 750 µg / L, about 600 µg / L to about 750 µg / L, about 2.3 µg / L to about 600 µg / L, about 5 µg / L to about 600 µg / L, about 10 µg / L to about 600 µg / L, about 20 µg / L to about 600 µg / L, about 25 µg / L to about 600 µg / L, about 30 µg / L to about 600 µg / L, about 40 µg / L to about 600 µg / L, about 47.2 µg / L to about 600 µg / L, about 50 µg / L to about 600 µg / L, about 60 µg / L to about 600 µg / L, about 70 µg / L to about 600 µg / L, about 80 µg / L to about 600 µg / L, about 89.2 µg / L to about 600 µg / L, about 90 µg / L to about 600 µg / L, about 100 µg / L to about 600 µg / L, about 150 µg / L to about 600 µg / L, about 200 µg / L to about 600 µg / L, about 250 µg / L to about 600 µg / L, about 300 µg / L to about 600 µg / L, about 400 µg / L to about 600 µg / L, about 500 µg / L to about 600 µg / L, about 2.3 µg / L to about 594 µg / L, about 5 µg / L to about 594 µg / L, about 10 µg / L to about 594 µg / L, about 20 µg / L to about 594 µg / L, about 25 µg / L to about 594 µg / L, about 30 µg / L to about 594 µg / L, about 40 µg / L to about 594 µg / L, about 47.2 µg / L to about 594 µg / L, about 50 µg / L to about 594 µg / L, about 60 µg / L to about 594 µg / L, about 70 µg / L to about 594 µg / L, about 80 µg / L to about 594 µg / L, about 89.2 µg / L to about 594 µg / L, about 90 µg / L to about 594 µg / L, about 100 µg / L to about 594 µg / L, about 150 µg / L to about 594 µg / L, about 200 µg / L to about 594 µg / L, about 250 µg / L to about 594 µg / L, about 300 µg / L to about 594 µg / L, about 400 µg / L to about 594 µg / L, about 500 µg / L to about 594 µg / L, about 2.3 µg / L to about 500 µg / L, about 5 µg / L to about 500 µg / L, about 10 µg / L to about 500 µg / L, about 20 µg / L to about 500 µg / L, about 25 µg / L to about 500 µg / L, about 30 µg / L to about 500 µg / L, about 40 µg / L to about 500 µg / L, about 47.2 µg / L to about 500 µg / L, about 50 µg / L to about 500 µg / L, about 60 µg / L to about 500 µg / L, about 70 µg / L to about 500 µg / L, about 80 µg / L to about 500 µg / L, about 89.2 µg / L to about 500 µg / L, about 90 µg / L to about 500 µg / L, about 100 µg / L to about 500 µg / L, about 150 µg / L to about 500 µg / L, about 200 µg / L to about 500 µg / L, about 250 µg / L to about 500 µg / L, about 300 µg / L to about 500 µg / L, about 400 µg / L to about 500 µg / L, about 2.3 µg / L to about 400 µg / L, about 5 µg / L to about 400 µg / L, about 10 µg / L to about 400 µg / L, about 20 µg / L to about 400 µg / L, about 25 µg / L to about 400 µg / L, about 30 µg / L to about 400 µg / L, about 40 µg / L to about 400 µg / L, about 47.2 µg / L to about 400 µg / L, about 50 µg / L to about 400 µg / L, about 60 µg / L to about 400 µg / L, about 70 µg / L to about 400 µg / L, about 80 µg / L to about 400 µg / L, about 89.2 µg / L to about 400 µg / L, about 90 µg / L to about 400 µg / L, about 100 µg / L to about 400 µg / L, about 150 µg / L to about 400 µg / L, about 200 µg / L to about 400 µg / L, about 250 µg / L to about 400 µg / L, about 300 µg / L to about 400 µg / L, about 2.3 µg / L to about 363.1 µg / L, about 5 µg / L to about 363.1 µg / L, about 10 µg / L to about 363.1 µg / L, about 20 µg / L to about 363.1 µg / L, about 25 µg / L to about 363.1 µg / L, about 30 µg / L to about 363.1 µg / L, about 40 µg / L to about 363.1 µg / L, about 47.2 µg / L to about 363.1 µg / L, about 50 µg / L to about 363.1 µg / L, about 60 µg / L to about 363.1 µg / L, about 70 µg / L to about 363.1 µg / L, about 80 µg / L to about 363.1 µg / L, about 89.2 µg / L to about 363.1 µg / L, about 90 µg / L to about 363.1 µg / L, about 100 µg / L to about 363.1 µg / L, about 150 µg / L to about 363.1 µg / L, about 200 µg / L to about 363.1 µg / L, about 250 µg / L to about 363.1 µg / L, about 300 µg / L to about 363.1 µg / L, about 400 µg / L to about 363.1 µg / L, about 500 µg / L to about 363.1 µg / L, about 2.3 µg / L to about 300 µg / L, about 5 µg / L to about 300 µg / L, about 10 µg / L to about 300 µg / L, about 20 µg / L to about 300 µg / L, about 25 µg / L to about 300 µg / L, about 30 µg / L to about 300 µg / L, about 40 µg / L to about 300 µg / L, about 47.2 µg / L to about 300 µg / L, about 50 µg / L to about 300 µg / L, about 60 µg / L to about 300 µg / L, about 70 µg / L to about 300 µg / L, about 80 µg / L to about 300 µg / L, about 89.2 µg / L to about 300 µg / L, about 90 µg / L to about 300 µg / L, about 100 µg / L to about 300 µg / L, about 150 µg / L to about 300 µg / L, about 200 µg / L to about 300 µg / L, about 250 µg / L to about 300 µg / L, about 2.3 µg / L to about 281.1 µg / L, about 5 µg / L to about 281.1 µg / L, about 10 µg / L to about 281.1 µg / L, about 20 µg / L to about 281.1 µg / L, about 25 µg / L to about 281.1 µg / L, about 30 µg / L to about 281.1 µg / L, about 40 µg / L to about 281.1 µg / L, about 47.2 µg / L to about 281.1 µg / L, about 50 µg / L to about 281.1 µg / L, about 60 µg / L to about 281.1 µg / L, about 70 µg / L to about 281.1 µg / L, about 80 µg / L to about 281.1 µg / L, about 89.2 µg / L to about 281.1 µg / L, about 90 µg / L to about 281.1 µg / L, about 100 µg / L to about 281.1 µg / L, about 150 µg / L to about 281.1 µg / L, about 200 µg / L to about 281.1 µg / L, about 250 µg / L to about 281.1 µg / L, about 2.3 µg / L to about 250 µg / L, about 5 µg / L to about 250 µg / L, about 10 µg / L to about 250 µg / L, about 20 µg / L to about 250 µg / L, about 25 µg / L to about 250 µg / L, about 30 µg / L to about 250 µg / L, about 40 µg / L to about 250 µg / L, about 47.2 µg / L to about 250 µg / L, about 50 µg / L to about 250 µg / L, about 60 µg / L to about 250 µg / L, about 70 µg / L to about 250 µg / L, about 80 µg / L to about 250 µg / L, about 89.2 µg / L to about 250 µg / L, about 90 µg / L to about 250 µg / L, about 100 µg / L to about 250 µg / L, about 150 µg / L to about 250 µg / L, about 200 µg / L to about 250 µg / L, about 2.3 µg / L to about 200 µg / L, about 5 µg / L to about 200 µg / L, about 10 µg / L to about 200 µg / L, about 20 µg / L to about 200 µg / L, about 25 µg / L to about 200 µg / L, about 30 µg / L to about 200 µg / L, about 40 µg / L to about 200 µg / L, about 47.2 µg / L to about 200 µg / L, about 50 µg / L to about 200 µg / L, about 60 µg / L to about 200 µg / L, about 70 µg / L to about 200 µg / L, about 80 µg / L to about 200 µg / L, about 89.2 µg / L to about 200 µg / L, about 90 µg / L to about 200 µg / L, about 100 µg / L to about 200 µg / L, about 150 µg / L to about 200 µg / L, about 2.3 µg / L to about 150 µg / L, about 5 µg / L to about 150 µg / L, about 10 µg / L to about 150 µg / L, about 20 µg / L to about 150 µg / L, about 25 µg / L to about 150 µg / L, about 30 µg / L to about 150 µg / L, about 40 µg / L to about 150 µg / L, about 47.2 µg / L to about 150 µg / L, about 50 µg / L to about 150 µg / L, about 60 µg / L to about 150 µg / L, about 70 µg / L to about 150 µg / L, about 80 µg / L to about 150 µg / L, about 89.2 µg / L to about 150 µg / L, about 90 µg / L to about 150 µg / L, about 100 µg / L to about 150 µg / L, about 2.3 µg / L to about 100 µg / L, about 5 µg / L to about 100 µg / L, about 10 µg / L to about 100 µg / L, about 20 µg / L to about 100 µg / L, about 25 µg / L to about 100 µg / L, about 30 µg / L to about 100 µg / L, about 40 µg / L to about 100 µg / L, about 47.2 µg / L to about 100 µg / L, about 50 µg / L to about 100 µg / L, about 60 µg / L to about 100 µg / L, about 70 µg / L to about 100 µg / L, about 80 µg / L to about 100 µg / L, about 89.2 µg / L to about 100 µg / L, about 90 µg / L to about 100 µg / L, about 2.3 µg / L to about 90 µg / L, about 5 µg / L to about 90 µg / L, about 10 µg / L to about 90 µg / L, about 20 µg / L to about 90 µg / L, about 25 µg / L to about 90 µg / L, about 30 µg / L to about 90 µg / L, about 40 µg / L to about 90 µg / L, about 47.2 µg / L to about 90 µg / L, about 50 µg / L to about 90 µg / L, about 60 µg / L to about 90 µg / L, about 70 µg / L to about 90 µg / L, about 80 µg / L to about 90 µg / L, about 89.2 µg / L to about 90 µg / L, about 2.3 µg / L to about 80 µg / L, about 5 µg / L to about 80 µg / L, about 10 µg / L to about 80 µg / L, about 20 µg / L to about 80 µg / L, about 25 µg / L to about 80 µg / L, about 30 µg / L to about 80 µg / L, about 40 µg / L to about 80 µg / L, about 47.2 µg / L to about 80 µg / L, about 50 µg / L to about 80 µg / L, about 60 µg / L to about 80 µg / L, about 70 µg / L to about 80 µg / L, about 2.3 µg / L to about 70 µg / L, about 5 µg / L to about 70 µg / L, about 10 µg / L to about 70 µg / L, about 20 µg / L to about 70 µg / L, about 25 µg / L to about 70 µg / L, about 30 µg / L to about 70 µg / L, about 40 µg / L to about 70 µg / L, about 47.2 µg / L to about 70 µg / L, about 50 µg / L to about 70 µg / L, about 60 µg / L to about 70 µg / L, about 2.3 µg / L to about 60 µg / L, about 5 µg / L to about 60 µg / L, about 10 µg / L to about 60 µg / L, about 20 µg / L to about 60 µg / L, about 25 µg / L to about 60 µg / L, about 30 µg / L to about 60 µg / L, about 40 µg / L to about 60 µg / L, about 47.2 µg / L to about 60 µg / L, about 50 µg / L to about 60 µg / L, about 2.3 µg / L to about 50 µg / L, about 5 µg / L to about 50 µg / L, about 10 µg / L to about 50 µg / L, about 20 µg / L to about 50 µg / L, about 25 µg / L to about 50 µg / L, about 30 µg / L to about 50 µg / L, about 40 µg / L to about 50 µg / L, about 47.2 µg / L to about 50 µg / L, about 2.3 µg / L to about 40 µg / L, about 5 µg / L to about 40 µg / L, about 10 µg / L to about 40 µg / L, about 20 µg / L to about 40 µg / L, about 25 µg / L to about 40 µg / L, about 30 µg / L to about 40 µg / L, about 2.3 µg / L to about 30 µg / L, about 5 µg / L to about 30 µg / L, about 10 µg / L to about 30 µg / L, about 20 µg / L to about 30 µg / L, about 25 µg / L to about 30 µg / L, about 2.3 µg / L to about 20 µg / L, about 5 µg / L to about 20 µg / L, about 10 µg / L to about 20 µg / L, about 2.3 µg / L to about 10 µg / L, about 5 µg / L to about 10 µg / L, about 2.3 µg / L to about 5 µg / L, or about 2.3, 5, 10, 20, 25, 30, 40, 47.2, 50, 60, 70, 75, 80, 89.2, 90, 100, 150, 200, 250, 281.1, 300, 363.1, 400, 500, 594, 600, 750, 800, 900, 1000, 1100, 1200, 1250, 1300, 1400, or 1500 µg / L or any range or value therebetween. In some embodiments, the fermented product comprises phenethyl acetate in an amount from about 89.2 µg / L to about 594 µg / L. In some embodiments, the fermented product comprises phenethyl acetate in an amount from about 2.3 µg / L to about 281.1 µg / L. In some embodiments, the fermented product comprises ethyl acetate in an amount from about 500 µg / L to about 4500 µg / L. In some embodiments, the fermented product comprises ethyl acetate in an amount from about 500 µg / L to about 4500 µg / L, about 524.8 µg / L to about 4500 µg / L, about 562 µg / L to about 4500 µg / L, about 600 µg / L to about 4500 µg / L, about 700 µg / L to about 4500 µg / L, about 800 µg / L to about 4500 µg / L, about 900 µg / L to about 4500 µg / L, about 1000 µg / L to about 4500 µg / L, about 1250 µg / L to about 4500 µg / L, about 1500 µg / L to about 4500 µg / L, about 1750 µg / L to about 4500 µg / L, about 2000 µg / L to about 4500 µg / L, about 2500 µg / L to about 4500 µg / L, about 3000 µg / L to about 4500 µg / L, about 3500 µg / L to about 4500 µg / L, about 4000 µg / L to about 4500 µg / L, about 500 µg / L to about 4073.8 µg / L, about 524.8 µg / L to about 4073.8 µg / L, about 562 µg / L to about 4073.8 µg / L, about 600 µg / L to about 4073.8 µg / L, about 700 µg / L to about 4073.8 µg / L, about 800 µg / L to about 4073.8 µg / L, about 900 µg / L to about 4073.8 µg / L, about 1000 µg / L to about 4073.8 µg / L, about 1250 µg / L to about 4073.8 µg / L, about 1500 µg / L to about 4073.8 µg / L, about 1750 µg / L to about 4073.8 µg / L, about 2000 µg / L to about 4073.8 µg / L, about 2500 µg / L to about 4073.8 µg / L, about 3000 µg / L to about 4073.8 µg / L, about 3500 µg / L to about 4073.8 µg / L, about 4000 µg / L to about 4073.8 µg / L, about 500 µg / L to about 4000 µg / L, about 524.8 µg / L to about 4000 µg / L, about 562 µg / L to about 4000 µg / L, about 600 µg / L to about 4000 µg / L, about 700 µg / L to about 4000 µg / L, about 800 µg / L to about 4000 µg / L, about 900 µg / L to about 4000 µg / L, about 1000 µg / L to about 4000 µg / L, about 1250 µg / L to about 4000 µg / L, about 1500 µg / L to about 4000 µg / L, about 1750 µg / L to about 4000 µg / L, about 2000 µg / L to about 4000 µg / L, about 2500 µg / L to about 4000 µg / L, about 3000 µg / L to about 4000 µg / L, about 3500 µg / L to about 4000 µg / L, about 500 µg / L to about 3800 µg / L, about 524.8 µg / L to about 3800 µg / L, about 562 µg / L to about 3800 µg / L, about 600 µg / L to about 3800 µg / L, about 700 µg / L to about 3800 µg / L, about 800 µg / L to about 3800 µg / L, about 900 µg / L to about 3800 µg / L, about 1000 µg / L to about 3800 µg / L, about 1250 µg / L to about 3800 µg / L, about 1500 µg / L to about 3800 µg / L, about 1750 µg / L to about 3800 µg / L, about 2000 µg / L to about 3800 µg / L, about 2500 µg / L to about 3800 µg / L, about 3000 µg / L to about 3800 µg / L, about 3500 µg / L to about 3800 µg / L, about 500 µg / L to about 3630.8 µg / L, about 524.8 µg / L to about 3630.8 µg / L, about 562 µg / L to about 3630.8 µg / L, about 600 µg / L to about 3630.8 µg / L, about 700 µg / L to about 3630.8 µg / L, about 800 µg / L to about 3630.8 µg / L, about 900 µg / L to about 3630.8 µg / L, about 1000 µg / L to about 3630.8 µg / L, about 1250 µg / L to about 3630.8 µg / L, about 1500 µg / L to about 3630.8 µg / L, about 1750 µg / L to about 3630.8 µg / L, about 2000 µg / L to about 3630.8 µg / L, about 2500 µg / L to about 3630.8 µg / L, about 3000 µg / L to about 3630.8 µg / L, about 3500 µg / L to about 3630.8 µg / L, about 500 µg / L to about 3500 µg / L, about 524.8 µg / L to about 3500 µg / L, about 562 µg / L to about 3500 µg / L, about 600 µg / L to about 3500 µg / L, about 700 µg / L to about 3500 µg / L, about 800 µg / L to about 3500 µg / L, about 900 µg / L to about 3500 µg / L, about 1000 µg / L to about 3500 µg / L, about 1250 µg / L to about 3500 µg / L, about 1500 µg / L to about 3500 µg / L, about 1750 µg / L to about 3500 µg / L, about 2000 µg / L to about 3500 µg / L, about 2500 µg / L to about 3500 µg / L, about 3000 µg / L to about 3500 µg / L, about 500 µg / L to about 3000 µg / L, about 524.8 µg / L to about 3000 µg / L, about 562 µg / L to about 3000 µg / L, about 600 µg / L to about 3000 µg / L, about 700 µg / L to about 3000 µg / L, about 800 µg / L to about 3000 µg / L, about 900 µg / L to about 3000 µg / L, about 1000 µg / L to about 3000 µg / L, about 1250 µg / L to about 3000 µg / L, about 1500 µg / L to about 3000 µg / L, about 1750 µg / L to about 3000 µg / L, about 2000 µg / L to about 3000 µg / L, about 2500 µg / L to about 3000 µg / L, about 500 µg / L to about 2500 µg / L, about 524.8 µg / L to about 2500 µg / L, about 562 µg / L to about 2500 µg / L, about 600 µg / L to about 2500 µg / L, about 700 µg / L to about 2500 µg / L, about 800 µg / L to about 2500 µg / L, about 900 µg / L to about 2500 µg / L, about 1000 µg / L to about 2500 µg / L, about 1250 µg / L to about 2500 µg / L, about 1500 µg / L to about 2500 µg / L, about 1750 µg / L to about 2500 µg / L, about 2000 µg / L to about 2500 µg / L, about 500 µg / L to about 2000 µg / L, about 524.8 µg / L to about 2000 µg / L, about 562 µg / L to about 2000 µg / L, about 600 µg / L to about 2000 µg / L, about 700 µg / L to about 2000 µg / L, about 800 µg / L to about 2000 µg / L, about 900 µg / L to about 2000 µg / L, about 1000 µg / L to about 2000 µg / L, about 1250 µg / L to about 2000 µg / L, about 1500 µg / L to about 2000 µg / L, about 1750 µg / L to about 2000 µg / L, about 500 µg / L to about 1750 µg / L, about 524.8 µg / L to about 1750 µg / L, about 562 µg / L to about 1750 µg / L, about 600 µg / L to about 1750 µg / L, about 700 µg / L to about 1750 µg / L, about 800 µg / L to about 1750 µg / L, about 900 µg / L to about 1750 µg / L, about 1000 µg / L to about 1750 µg / L, about 1250 µg / L to about 1750 µg / L, about 1500 µg / L to about 1750 µg / L, about 500 µg / L to about 1500 µg / L, about 524.8 µg / L to about 1500 µg / L, about 562 µg / L to about 1500 µg / L, about 600 µg / L to about 1500 µg / L, about 700 µg / L to about 1500 µg / L, about 800 µg / L to about 1500 µg / L, about 900 µg / L to about 1500 µg / L, about 1000 µg / L to about 1500 µg / L, about 1250 µg / L to about 1500 µg / L, about 500 µg / L to about 1250 µg / L, about 524.8 µg / L to about 1250 µg / L, about 562 µg / L to about 1250 µg / L, about 600 µg / L to about 1250 µg / L, about 700 µg / L to about 1250 µg / L, about 800 µg / L to about 1250 µg / L, about 900 µg / L to about 1250 µg / L, about 1000 µg / L to about 1250 µg / L, about 500 µg / L to about 1000 µg / L, about 524.8 µg / L to about 1000 µg / L, about 562 µg / L to about 1000 µg / L, about 600 µg / L to about 1000 µg / L, about 700 µg / L to about 1000 µg / L, about 800 µg / L to about 1000 µg / L, about 900 µg / L to about 1000 µg / L, about 500 µg / L to about 900 µg / L, about 524.8 µg / L to about 900 µg / L, about 562 µg / L to about 900 µg / L, about 600 µg / L to about 900 µg / L, about 700 µg / L to about 900 µg / L, about 800 µg / L to about 900 µg / L, about 500 µg / L to about 800 µg / L, about 524.8 µg / L to about 800 µg / L, about 562 µg / L to about 800 µg / L, about 600 µg / L to about 800 µg / L, about 700 µg / L to about 800 µg / L, about 500 µg / L to about 700 µg / L, about 524.8 µg / L to about 700 µg / L, about 562 µg / L to about 700 µg / L, about 600 µg / L to about 700 µg / L, about 500 µg / L to about 600 µg / L, about 524.8 µg / L to about 600 µg / L, about 562 µg / L to about 600 µg / L, or 500, 524.8, 600, 700, 800, 900, 1000, 1250, 1500, 1750, 2000, 2500, 3000, 3500, 3630.8, 3800, 4000, 4073.8, 4500 µg / L or any range or value therebetween. In some embodiments, the fermented product comprises ethyl acetate in an amount from about 600 µg / L to about 3800 µg / L. In some embodiments, the fermented product comprises ethyl acetate in an amount from about 524.8 µg / L to about 3630.8 µg / L. In some embodiments, the fermented product comprises phenethyl acetate and isoamyl acetate in a combined amount from about 10 µg / L to about 5500 µg / L. In some embodiments, the fermented product comprises phenethyl acetate and isoamyl acetate in a combined amount from about 10 µg / L to about 5500 µg / L, about 11.4 µg / L to about 5500 µg / L, about 11.5 µg / L to about 5500 µg / L, about 12.5 µg / L to about 5500 µg / L, about 20 µg / L to about 5500 µg / L, about 25 µg / L to about 5500 µg / L, about 30 µg / L to about 5500 µg / L, about 40 µg / L to about 5500 µg / L, about 50 µg / L to about 5500 µg / L, about 60 µg / L to about 5500 µg / L, about 70 µg / L to about 5500 µg / L, about 75 µg / L to about 5500 µg / L, about 80 µg / L to about 5500 µg / L, about 90 µg / L to about 5500 µg / L, about 100 µg / L to about 5500 µg / L, about 125 µg / L to about 5500 µg / L, about 150 µg / L to about 5500 µg / L, about 158.8 µg / L to about 5500 µg / L, about 175 µg / L to about 5500 µg / L, about 200 µg / L to about 5500 µg / L, about 250 µg / L to about 5500 µg / L, about 300 µg / L to about 5500 µg / L, about 400 µg / L to about 5500 µg / L, about 500 µg / L to about 5500 µg / L, about 600 µg / L to about 5500 µg / L, about 700 µg / L to about 5500 µg / L, about 800 µg / L to about 5500 µg / L, about 900 µg / L to about 5500 µg / L, about 1000 µg / L to about 5500 µg / L, about 1100 µg / L to about 5500 µg / L, about 1200 µg / L to about 5500 µg / L, about 1250 µg / L to about 5500 µg / L, about 1300 µg / L to about 5500 µg / L, about 1400 µg / L to about 5500 µg / L, about 1500 µg / L to about 5500 µg / L, about 2000 µg / L to about 5500 µg / L, about 3000 µg / L to about 5500 µg / L, about 4000 µg / L to about 5500 µg / L, about 5000 µg / L to about 5500 µg / L, about 10 µg / L to about 5000 µg / L, about 11.4 µg / L to about 5000 µg / L, about 11.5 µg / L to about 5000 µg / L, about 12.5 µg / L to about 5000 µg / L, about 20 µg / L to about 5000 µg / L, about 25 µg / L to about 5000 µg / L, about 30 µg / L to about 5000 µg / L, about 40 µg / L to about 5000 µg / L, about 50 µg / L to about 5000 µg / L, about 60 µg / L to about 5000 µg / L, about 70 µg / L to about 5000 µg / L, about 75 µg / L to about 5000 µg / L, about 80 µg / L to about 5000 µg / L, about 90 µg / L to about 5000 µg / L, about 100 µg / L to about 5000 µg / L, about 125 µg / L to about 5000 µg / L, about 150 µg / L to about 5000 µg / L, about 158.8 µg / L to about 5000 µg / L, about 175 µg / L to about 5000 µg / L, about 200 µg / L to about 5000 µg / L, about 250 µg / L to about 5000 µg / L, about 300 µg / L to about 5000 µg / L, about 400 µg / L to about 5000 µg / L, about 500 µg / L to about 5000 µg / L, about 600 µg / L to about 5000 µg / L, about 700 µg / L to about 5000 µg / L, about 800 µg / L to about 5000 µg / L, about 900 µg / L to about 5000 µg / L, about 1000 µg / L to about 5000 µg / L, about 1100 µg / L to about 5000 µg / L, about 1200 µg / L to about 5000 µg / L, about 1250 µg / L to about 5000 µg / L, about 1300 µg / L to about 5000 µg / L, about 1400 µg / L to about 5000 µg / L, about 1500 µg / L to about 5000 µg / L, about 2000 µg / L to about 5000 µg / L, about 3000 µg / L to about 5000 µg / L, about 4000 µg / L to about 5000 µg / L, about 10 µg / L to about 4000 µg / L, about 11.4 µg / L to about 4000 µg / L, about 11.5 µg / L to about 4000 µg / L, about 12.5 µg / L to about 4000 µg / L, about 20 µg / L to about 4000 µg / L, about 25 µg / L to about 4000 µg / L, about 30 µg / L to about 4000 µg / L, about 40 µg / L to about 4000 µg / L, about 50 µg / L to about 4000 µg / L, about 60 µg / L to about 4000 µg / L, about 70 µg / L to about 4000 µg / L, about 75 µg / L to about 4000 µg / L, about 80 µg / L to about 4000 µg / L, about 90 µg / L to about 4000 µg / L, about 100 µg / L to about 4000 µg / L, about 125 µg / L to about 4000 µg / L, about 150 µg / L to about 4000 µg / L, about 158.8 µg / L to about 4000 µg / L, about 175 µg / L to about 4000 µg / L, about 200 µg / L to about 4000 µg / L, about 250 µg / L to about 4000 µg / L, about 300 µg / L to about 4000 µg / L, about 400 µg / L to about 4000 µg / L, about 500 µg / L to about 4000 µg / L, about 600 µg / L to about 4000 µg / L, about 700 µg / L to about 4000 µg / L, about 800 µg / L to about 4000 µg / L, about 900 µg / L to about 4000 µg / L, about 1000 µg / L to about 4000 µg / L, about 1100 µg / L to about 4000 µg / L, about 1200 µg / L to about 4000 µg / L, about 1250 µg / L to about 4000 µg / L, about 1300 µg / L to about 4000 µg / L, about 1400 µg / L to about 4000 µg / L, about 1500 µg / L to about 4000 µg / L, about 2000 µg / L to about 4000 µg / L, about 3000 µg / L to about 4000 µg / L, about 10 µg / L to about 3000 µg / L, about 11.4 µg / L to about 3000 µg / L, about 11.5 µg / L to about 3000 µg / L, about 12.5 µg / L to about 3000 µg / L, about 20 µg / L to about 3000 µg / L, about 25 µg / L to about 3000 µg / L, about 30 µg / L to about 3000 µg / L, about 40 µg / L to about 3000 µg / L, about 50 µg / L to about 3000 µg / L, about 60 µg / L to about 3000 µg / L, about 70 µg / L to about 3000 µg / L, about 75 µg / L to about 3000 µg / L, about 80 µg / L to about 3000 µg / L, about 90 µg / L to about 3000 µg / L, about 100 µg / L to about 3000 µg / L, about 125 µg / L to about 3000 µg / L, about 150 µg / L to about 3000 µg / L, about 158.8 µg / L to about 3000 µg / L, about 175 µg / L to about 3000 µg / L, about 200 µg / L to about 3000 µg / L, about 250 µg / L to about 3000 µg / L, about 300 µg / L to about 3000 µg / L, about 400 µg / L to about 3000 µg / L, about 500 µg / L to about 3000 µg / L, about 600 µg / L to about 3000 µg / L, about 700 µg / L to about 3000 µg / L, about 800 µg / L to about 3000 µg / L, about 900 µg / L to about 3000 µg / L, about 1000 µg / L to about 3000 µg / L, about 1100 µg / L to about 3000 µg / L, about 1200 µg / L to about 3000 µg / L, about 1250 µg / L to about 3000 µg / L, about 1300 µg / L to about 3000 µg / L, about 1400 µg / L to about 3000 µg / L, about 1500 µg / L to about 3000 µg / L, about 2000 µg / L to about 3000 µg / L, about 10 µg / L to about 2000 µg / L, about 11.4 µg / L to about 2000 µg / L, about 11.5 µg / L to about 2000 µg / L, about 12.5 µg / L to about 2000 µg / L, about 20 µg / L to about 2000 µg / L, about 25 µg / L to about 2000 µg / L, about 30 µg / L to about 2000 µg / L, about 40 µg / L to about 2000 µg / L, about 50 µg / L to about 2000 µg / L, about 60 µg / L to about 2000 µg / L, about 70 µg / L to about 2000 µg / L, about 75 µg / L to about 2000 µg / L, about 80 µg / L to about 2000 µg / L, about 90 µg / L to about 2000 µg / L, about 100 µg / L to about 2000 µg / L, about 125 µg / L to about 2000 µg / L, about 150 µg / L to about 2000 µg / L, about 158.8 µg / L to about 2000 µg / L, about 175 µg / L to about 2000 µg / L, about 200 µg / L to about 2000 µg / L, about 250 µg / L to about 2000 µg / L, about 300 µg / L to about 2000 µg / L, about 400 µg / L to about 2000 µg / L, about 500 µg / L to about 2000 µg / L, about 600 µg / L to about 2000 µg / L, about 700 µg / L to about 2000 µg / L, about 800 µg / L to about 2000 µg / L, about 900 µg / L to about 2000 µg / L, about 1000 µg / L to about 2000 µg / L, about 1100 µg / L to about 2000 µg / L, about 1200 µg / L to about 2000 µg / L, about 1250 µg / L to about 2000 µg / L, about 1300 µg / L to about 2000 µg / L, about 1400 µg / L to about 2000 µg / L, about 1500 µg / L to about 2000 µg / L, about 10 µg / L to about 1753 µg / L, about 11.4 µg / L to about 1753 µg / L, about 11.5 µg / L to about 1753 µg / L, about 12.5 µg / L to about 1753 µg / L, about 20 µg / L to about 1753 µg / L, about 25 µg / L to about 1753 µg / L, about 30 µg / L to about 1753 µg / L, about 40 µg / L to about 1753 µg / L, about 50 µg / L to about 1753 µg / L, about 60 µg / L to about 1753 µg / L, about 70 µg / L to about 1753 µg / L, about 75 µg / L to about 1753 µg / L, about 80 µg / L to about 1753 µg / L, about 90 µg / L to about 1753 µg / L, about 100 µg / L to about 1753 µg / L, about 125 µg / L to about 1753 µg / L, about 150 µg / L to about 1753 µg / L, about 158.8 µg / L to about 1753 µg / L, about 175 µg / L to about 1753 µg / L, about 200 µg / L to about 1753 µg / L, about 250 µg / L to about 1753 µg / L, about 300 µg / L to about 1753 µg / L, about 400 µg / L to about 1753 µg / L, about 500 µg / L to about 1753 µg / L, about 600 µg / L to about 1753 µg / L, about 700 µg / L to about 1753 µg / L, about 800 µg / L to about 1753 µg / L, about 900 µg / L to about 1753 µg / L, about 1000 µg / L to about 1753 µg / L, about 1100 µg / L to about 1753 µg / L, about 1200 µg / L to about 1753 µg / L, about 1250 µg / L to about 1753 µg / L, about 1300 µg / L to about 1753 µg / L, about 1400 µg / L to about 1753 µg / L, about 10 µg / L to about 1500 µg / L, about 11.4 µg / L to about 1500 µg / L, about 11.5 µg / L to about 1500 µg / L, about 12.5 µg / L to about 1500 µg / L, about 20 µg / L to about 1500 µg / L, about 25 µg / L to about 1500 µg / L, about 30 µg / L to about 1500 µg / L, about 35 µg / L to about 1500 µg / L, about 40 µg / L to about 1500 µg / L, about 50 µg / L to about 1500 µg / L, about 60 µg / L to about 1500 µg / L, about 70 µg / L to about 1500 µg / L, about 75 µg / L to about 1500 µg / L, about 80 µg / L to about 1500 µg / L, about 90 µg / L to about 1500 µg / L, about 100 µg / L to about 1500 µg / L, about 125 µg / L to about 1500 µg / L, about 150 µg / L to about 1500 µg / L, about 158.8 µg / L to about 1500 µg / L, about 175 µg / L to about 1500 µg / L, about 200 µg / L to about 1500 µg / L, about 250 µg / L to about 1500 µg / L, about 300 µg / L to about 1500 µg / L, about 400 µg / L to about 1500 µg / L, about 500 µg / L to about 1500 µg / L, about 600 µg / L to about 1500 µg / L, about 700 µg / L to about 1500 µg / L, about 800 µg / L to about 1500 µg / L, about 900 µg / L to about 1500 µg / L, about 1000 µg / L to about 1500 µg / L, about 1100 µg / L to about 1500 µg / L, about 1200 µg / L to about 1500 µg / L, about 1250 µg / L to about 1500 µg / L, about 1300 µg / L to about 1500 µg / L, about 1400 µg / L to about 1500 µg / L, about 10 µg / L to about 1400 µg / L, about 11.4 µg / L to about 1400 µg / L, about 11.5 µg / L to about 1400 µg / L, about 12.5 µg / L to about 1400 µg / L, about 20 µg / L to about 1400 µg / L, about 25 µg / L to about 1400 µg / L, about 30 µg / L to about 1400 µg / L, about 40 µg / L to about 1400 µg / L, about 50 µg / L to about 1400 µg / L, about 60 µg / L to about 1400 µg / L, about 70 µg / L to about 1400 µg / L, about 75 µg / L to about 1400 µg / L, about 80 µg / L to about 1400 µg / L, about 90 µg / L to about 1400 µg / L, about 100 µg / L to about 1400 µg / L, about 125 µg / L to about 1400 µg / L, about 150 µg / L to about 1400 µg / L, about 158.8 µg / L to about 1400 µg / L, about 175 µg / L to about 1400 µg / L, about 200 µg / L to about 1400 µg / L, about 250 µg / L to about 1400 µg / L, about 300 µg / L to about 1400 µg / L, about 400 µg / L to about 1400 µg / L, about 500 µg / L to about 1400 µg / L, about 600 µg / L to about 1400 µg / L, about 700 µg / L to about 1400 µg / L, about 800 µg / L to about 1400 µg / L, about 900 µg / L to about 1400 µg / L, about 1000 µg / L to about 1400 µg / L, about 1100 µg / L to about 1400 µg / L, about 1200 µg / L to about 1400 µg / L, about 1250 µg / L to about 1400 µg / L, about 1300 µg / L to about 1400 µg / L, about 10 µg / L to about 1360 µg / L, about 11.4 µg / L to about 1360 µg / L, about 11.5 µg / L to about 1360 µg / L, about 12.5 µg / L to about 1360 µg / L, about 20 µg / L to about 1360 µg / L, about 25 µg / L to about 1360 µg / L, about 30 µg / L to about 1360 µg / L, about 40 µg / L to about 1360 µg / L, about 50 µg / L to about 1360 µg / L, about 60 µg / L to about 1360 µg / L, about 70 µg / L to about 1360 µg / L, about 75 µg / L to about 1360 µg / L, about 80 µg / L to about 1360 µg / L, about 90 µg / L to about 1360 µg / L, about 100 µg / L to about 1360 µg / L, about 125 µg / L to about 1360 µg / L, about 150 µg / L to about 1360 µg / L, about 158.8 µg / L to about 1360 µg / L, about 175 µg / L to about 1360 µg / L, about 200 µg / L to about 1360 µg / L, about 250 µg / L to about 1360 µg / L, about 300 µg / L to about 1360 µg / L, about 400 µg / L to about 1360 µg / L, about 500 µg / L to about 1360 µg / L, about 600 µg / L to about 1360 µg / L, about 700 µg / L to about 1360 µg / L, about 800 µg / L to about 1360 µg / L, about 900 µg / L to about 1360 µg / L, about 1000 µg / L to about 1360 µg / L, about 1100 µg / L to about 1360 µg / L, about 1200 µg / L to about 1360 µg / L, about 1250 µg / L to about 1360 µg / L, about 1300 µg / L to about 1360 µg / L, about 10 µg / L to about 1300 µg / L, about 11.4 µg / L to about 1300 µg / L, about 11.5 µg / L to about 1300 µg / L, about 12.5 µg / L to about 1300 µg / L, about 20 µg / L to about 1300 µg / L, about 25 µg / L to about 1300 µg / L, about 30 µg / L to about 1300 µg / L, about 40 µg / L to about 1300 µg / L, about 50 µg / L to about 1300 µg / L, about 60 µg / L to about 1300 µg / L, about 70 µg / L to about 1300 µg / L, about 75 µg / L to about 1300 µg / L, about 80 µg / L to about 1300 µg / L, about 90 µg / L to about 1300 µg / L, about 100 µg / L to about 1300 µg / L, about 125 µg / L to about 1300 µg / L, about 150 µg / L to about 1300 µg / L, about 158.8 µg / L to about 1300 µg / L, about 175 µg / L to about 1300 µg / L, about 200 µg / L to about 1300 µg / L, about 250 µg / L to about 1300 µg / L, about 300 µg / L to about 1300 µg / L, about 400 µg / L to about 1300 µg / L, about 500 µg / L to about 1300 µg / L, about 600 µg / L to about 1300 µg / L, about 700 µg / L to about 1300 µg / L, about 800 µg / L to about 1300 µg / L, about 900 µg / L to about 1300 µg / L, about 1000 µg / L to about 1300 µg / L, about 1100 µg / L to about 1300 µg / L, about 1200 µg / L to about 1300 µg / L, about 1250 µg / L to about 1300 µg / L, about 10 µg / L to about 1250 µg / L, about 11.4 µg / L to about 1250 µg / L, about 11.5 µg / L to about 1250 µg / L, about 12.5 µg / L to about 1250 µg / L, about 20 µg / L to about 1250 µg / L, about 25 µg / L to about 1250 µg / L, about 30 µg / L to about 1250 µg / L, about 40 µg / L to about 1250 µg / L, about 50 µg / L to about 1250 µg / L, about 60 µg / L to about 1250 µg / L, about 70 µg / L to about 1250 µg / L, about 75 µg / L to about 1250 µg / L, about 80 µg / L to about 1250 µg / L, about 90 µg / L to about 1250 µg / L, about 100 µg / L to about 1250 µg / L, about 125 µg / L to about 1250 µg / L, about 150 µg / L to about 1250 µg / L, about 158.8 µg / L to about 1250 µg / L, about 175 µg / L to about 1250 µg / L, about 200 µg / L to about 1250 µg / L, about 250 µg / L to about 1250 µg / L, about 300 µg / L to about 1250 µg / L, about 400 µg / L to about 1250 µg / L, about 500 µg / L to about 1250 µg / L, about 600 µg / L to about 1250 µg / L, about 700 µg / L to about 1250 µg / L, about 800 µg / L to about 1250 µg / L, about 900 µg / L to about 1250 µg / L, about 1000 µg / L to about 1250 µg / L, about 1100 µg / L to about 1250 µg / L, about 1200 µg / L to about 1250 µg / L, about 10 µg / L to about 1200 µg / L, about 11.4 µg / L to about 1200 µg / L, about 11.5 µg / L to about 1200 µg / L, about 12.5 µg / L to about 1200 µg / L, about 20 µg / L to about 1200 µg / L, about 25 µg / L to about 1200 µg / L, about 30 µg / L to about 1200 µg / L, about 40 µg / L to about 1200 µg / L, about 50 µg / L to about 1200 µg / L, about 60 µg / L to about 1200 µg / L, about 70 µg / L to about 1200 µg / L, about 75 µg / L to about 1200 µg / L, about 80 µg / L to about 1200 µg / L, about 90 µg / L to about 1200 µg / L, about 100 µg / L to about 1200 µg / L, about 125 µg / L to about 1200 µg / L, about 150 µg / L to about 1200 µg / L, about 158.8 µg / L to about 1200 µg / L, about 175 µg / L to about 1200 µg / L, about 200 µg / L to about 1200 µg / L, about 250 µg / L to about 1200 µg / L, about 300 µg / L to about 1200 µg / L, about 400 µg / L to about 1200 µg / L, about 500 µg / L to about 1200 µg / L, about 600 µg / L to about 1200 µg / L, about 700 µg / L to about 1200 µg / L, about 800 µg / L to about 1200 µg / L, about 900 µg / L to about 1200 µg / L, about 1000 µg / L to about 1200 µg / L, about 1100 µg / L to about 1200 µg / L, about 10 µg / L to about 1100 µg / L, about 11.4 µg / L to about 1100 µg / L, about 11.5 µg / L to about 1100 µg / L, about 12.5 µg / L to about 1100 µg / L, about 20 µg / L to about 1100 µg / L, about 25 µg / L to about 1100 µg / L, about 30 µg / L to about 1100 µg / L, about 40 µg / L to about 1100 µg / L, about 50 µg / L to about 1100 µg / L, about 60 µg / L to about 1100 µg / L, about 70 µg / L to about 1100 µg / L, about 75 µg / L to about 1100 µg / L, about 80 µg / L to about 1100 µg / L, about 90 µg / L to about 1100 µg / L, about 100 µg / L to about 1100 µg / L, about 125 µg / L to about 1100 µg / L, about 150 µg / L to about 1100 µg / L, about 158.8 µg / L to about 1100 µg / L, about 175 µg / L to about 1100 µg / L, about 200 µg / L to about 1100 µg / L, about 250 µg / L to about 1100 µg / L, about 300 µg / L to about 1100 µg / L, about 400 µg / L to about 1100 µg / L, about 500 µg / L to about 1100 µg / L, about 600 µg / L to about 1100 µg / L, about 700 µg / L to about 1100 µg / L, about 800 µg / L to about 1100 µg / L, about 900 µg / L to about 1100 µg / L, about 1000 µg / L to about 1100 µg / L, about 10 µg / L to about 1094.7 µg / L, about 11.4 µg / L to about 1094.7 µg / L, about 11.5 µg / L to about 1094.7 µg / L, about 12.5 µg / L to about 1094.7 µg / L, about 20 µg / L to about 1094.7 µg / L, about 25 µg / L to about 1094.7 µg / L, about 30 µg / L to about 1094.7 µg / L, about 40 µg / L to about 1094.7 µg / L, about 50 µg / L to about 1094.7 µg / L, about 60 µg / L to about 1094.7 µg / L, about 70 µg / L to about 1094.7 µg / L, about 75 µg / L to about 1094.7 µg / L, about 80 µg / L to about 1094.7 µg / L, about 90 µg / L to about 1094.7 µg / L, about 100 µg / L to about 1094.7 µg / L, about 125 µg / L to about 1094.7 µg / L, about 150 µg / L to about 1094.7 µg / L, about 158.8 µg / L to about 1094.7 µg / L, about 175 µg / L to about 1094.7 µg / L, about 200 µg / L to about 1094.7 µg / L, about 250 µg / L to about 1094.7 µg / L, about 300 µg / L to about 1094.7 µg / L, about 400 µg / L to about 1094.7 µg / L, about 500 µg / L to about 1094.7 µg / L, about 600 µg / L to about 1094.7 µg / L, about 700 µg / L to about 1094.7 µg / L, about 800 µg / L to about 1094.7 µg / L, about 900 µg / L to about 1094.7 µg / L, about 1000 µg / L to about 1094.7 µg / L, about 10 µg / L to about 1000 µg / L, about 11.4 µg / L to about 1000 µg / L, about 11.5 µg / L to about 1000 µg / L, about 12.5 µg / L to about 1000 µg / L, about 20 µg / L to about 1000 µg / L, about 25 µg / L to about 1000 µg / L, about 30 µg / L to about 1000 µg / L, about 40 µg / L to about 1000 µg / L, about 50 µg / L to about 1000 µg / L, about 60 µg / L to about 1000 µg / L, about 70 µg / L to about 1000 µg / L, about 75 µg / L to about 1000 µg / L, about 80 µg / L to about 1000 µg / L, about 90 µg / L to about 1000 µg / L, about 100 µg / L to about 1000 µg / L, about 125 µg / L to about 1000 µg / L, about 150 µg / L to about 1000 µg / L, about 158.8 µg / L to about 1000 µg / L, about 175 µg / L to about 1000 µg / L, about 200 µg / L to about 1000 µg / L, about 250 µg / L to about 1000 µg / L, about 300 µg / L to about 1000 µg / L, about 400 µg / L to about 1000 µg / L, about 500 µg / L to about 1000 µg / L, about 600 µg / L to about 1000 µg / L, about 700 µg / L to about 1000 µg / L, about 800 µg / L to about 1000 µg / L, about 900 µg / L to about 1000 µg / L, about 10 µg / L to about 900 µg / L, about 11.4 µg / L to about 900 µg / L, about 11.5 µg / L to about 900 µg / L, about 12.5 µg / L to about 900 µg / L, about 20 µg / L to about 900 µg / L, about 25 µg / L to about 900 µg / L, about 30 µg / L to about 900 µg / L, about 40 µg / L to about 900 µg / L, about 50 µg / L to about 900 µg / L, about 60 µg / L to about 900 µg / L, about 70 µg / L to about 900 µg / L, about 75 µg / L to about 900 µg / L, about 80 µg / L to about 900 µg / L, about 90 µg / L to about 900 µg / L, about 100 µg / L to about 900 µg / L, about 125 µg / L to about 900 µg / L, about 150 µg / L to about 900 µg / L, about 158.8 µg / L to about 900 µg / L, about 175 µg / L to about 900 µg / L, about 200 µg / L to about 900 µg / L, about 250 µg / L to about 900 µg / L, about 300 µg / L to about 900 µg / L, about 400 µg / L to about 900 µg / L, about 500 µg / L to about 900 µg / L, about 600 µg / L to about 900 µg / L, about 700 µg / L to about 900 µg / L, about 800 µg / L to about 900 µg / L, about 10 µg / L to about 800 µg / L, about 11.4 µg / L to about 800 µg / L, about 11.5 µg / L to about 800 µg / L, about 12.5 µg / L to about 800 µg / L, about 20 µg / L to about 800 µg / L, about 25 µg / L to about 800 µg / L, about 30 µg / L to about 800 µg / L, about 40 µg / L to about 800 µg / L, about 50 µg / L to about 800 µg / L, about 60 µg / L to about 800 µg / L, about 70 µg / L to about 800 µg / L, about 75 µg / L to about 800 µg / L, about 80 µg / L to about 800 µg / L, about 90 µg / L to about 800 µg / L, about 100 µg / L to about 800 µg / L, about 125 µg / L to about 800 µg / L, about 150 µg / L to about 800 µg / L, about 158.8 µg / L to about 800 µg / L, about 175 µg / L to about 800 µg / L, about 200 µg / L to about 800 µg / L, about 250 µg / L to about 800 µg / L, about 300 µg / L to about 800 µg / L, about 400 µg / L to about 800 µg / L, about 500 µg / L to about 800 µg / L, about 600 µg / L to about 800 µg / L, about 700 µg / L to about 800 µg / L, about 10 µg / L to about 700 µg / L, about 11.4 µg / L to about 700 µg / L, about 11.5 µg / L to about 700 µg / L, about 12.5 µg / L to about 700 µg / L, about 20 µg / L to about 700 µg / L, about 25 µg / L to about 700 µg / L, about 30 µg / L to about 700 µg / L, about 40 µg / L to about 700 µg / L, about 50 µg / L to about 700 µg / L, about 60 µg / L to about 700 µg / L, about 70 µg / L to about 700 µg / L, about 75 µg / L to about 700 µg / L, about 80 µg / L to about 700 µg / L, about 90 µg / L to about 700 µg / L, about 100 µg / L to about 700 µg / L, about 125 µg / L to about 700 µg / L, about 150 µg / L to about 700 µg / L, about 158.8 µg / L to about 700 µg / L, about 175 µg / L to about 700 µg / L, about 200 µg / L to about 700 µg / L, about 250 µg / L to about 700 µg / L, about 300 µg / L to about 700 µg / L, about 400 µg / L to about 700 µg / L, about 500 µg / L to about 700 µg / L, about 600 µg / L to about 700 µg / L, about 10 µg / L to about 600 µg / L, about 11.4 µg / L to about 600 µg / L, about 11.5 µg / L to about 600 µg / L, about 12.5 µg / L to about 600 µg / L, about 20 µg / L to about 600 µg / L, about 25 µg / L to about 600 µg / L, about 30 µg / L to about 600 µg / L, about 40 µg / L to about 600 µg / L, about 50 µg / L to about 600 µg / L, about 60 µg / L to about 600 µg / L, about 70 µg / L to about 600 µg / L, about 75 µg / L to about 600 µg / L, about 80 µg / L to about 600 µg / L, about 90 µg / L to about 600 µg / L, about 100 µg / L to about 600 µg / L, about 125 µg / L to about 600 µg / L, about 150 µg / L to about 600 µg / L, about 158.8 µg / L to about 600 µg / L, about 175 µg / L to about 600 µg / L, about 200 µg / L to about 600 µg / L, about 250 µg / L to about 600 µg / L, about 300 µg / L to about 600 µg / L, about 400 µg / L to about 600 µg / L, about 500 µg / L to about 600 µg / L, about 10 µg / L to about 500 µg / L, about 11.4 µg / L to about 500 µg / L, about 11.5 µg / L to about 500 µg / L, about 12.5 µg / L to about 500 µg / L, about 20 µg / L to about 500 µg / L, about 25 µg / L to about 500 µg / L, about 30 µg / L to about 500 µg / L, about 40 µg / L to about 500 µg / L, about 50 µg / L to about 500 µg / L, about 60 µg / L to about 500 µg / L, about 70 µg / L to about 500 µg / L, about 75 µg / L to about 500 µg / L, about 80 µg / L to about 500 µg / L, about 90 µg / L to about 500 µg / L, about 100 µg / L to about 500 µg / L, about 125 µg / L to about 500 µg / L, about 150 µg / L to about 500 µg / L, about 158.8 µg / L to about 500 µg / L, about 175 µg / L to about 500 µg / L, about 200 µg / L to about 500 µg / L, about 250 µg / L to about 500 µg / L, about 300 µg / L to about 500 µg / L, about 400 µg / L to about 500 µg / L, about 10 µg / L to about 400 µg / L, about 11.4 µg / L to about 400 µg / L, about 11.5 µg / L to about 400 µg / L, about 12.5 µg / L to about 40 µg / L, about 20 µg / L to about 400 µg / L, about 25 µg / L to about 400 µg / L, about 30 µg / L to about 400 µg / L, about 40 µg / L to about 400 µg / L, about 50 µg / L to about 400 µg / L, about 60 µg / L to about 400 µg / L, about 70 µg / L to about 400 µg / L, about 75 µg / L to about 400 µg / L, about 80 µg / L to about 400 µg / L, about 90 µg / L to about 400 µg / L, about 100 µg / L to about 400 µg / L, about 125 µg / L to about 400 µg / L, about 150 µg / L to about 400 µg / L, about 158.8 µg / L to about 400 µg / L, about 175 µg / L to about 400 µg / L, about 200 µg / L to about 400 µg / L, about 250 µg / L to about 400 µg / L, about 300 µg / L to about 400 µg / L, about 10 µg / L to about 300 µg / L, about 11.4 µg / L to about 300 µg / L, about 11.5 µg / L to about 300 µg / L, about 12.5 µg / L to about 300 µg / L, about 20 µg / L to about 300 µg / L, about 25 µg / L to about 300 µg / L, about 30 µg / L to about 300 µg / L, about 40 µg / L to about 300 µg / L, about 50 µg / L to about 300 µg / L, about 60 µg / L to about 300 µg / L, about 70 µg / L to about 300 µg / L, about 75 µg / L to about 300 µg / L, about 80 µg / L to about 300 µg / L, about 90 µg / L to about 300 µg / L, about 100 µg / L to about 300 µg / L, about 125 µg / L to about 300 µg / L, about 150 µg / L to about 300 µg / L, about 158.8 µg / L to about 300 µg / L, about 175 µg / L to about 300 µg / L, about 200 µg / L to about 300 µg / L, about 250 µg / L to about 300 µg / L, about 10 µg / L to about 250 µg / L, about 11.4 µg / L to about 250 µg / L, about 11.5 µg / L to about 250 µg / L, about 12.5 µg / L to about 250 µg / L, about 20 µg / L to about 250 µg / L, about 25 µg / L to about 250 µg / L, about 30 µg / L to about 250 µg / L, about 40 µg / L to about 250 µg / L, about 50 µg / L to about 250 µg / L, about 60 µg / L to about 250 µg / L, about 70 µg / L to about 250 µg / L, about 75 µg / L to about 250 µg / L, about 80 µg / L to about 250 µg / L, about 90 µg / L to about 250 µg / L, about 100 µg / L to about 250 µg / L, about 125 µg / L to about 250 µg / L, about 150 µg / L to about 250 µg / L, about 158.8 µg / L to about 250 µg / L, about 175 µg / L to about 250 µg / L, about 200 µg / L to about 250 µg / L, about 10 µg / L to about 200 µg / L, about 11.4 µg / L to about 200 µg / L, about 11.5 µg / L to about 200 µg / L, about 12.5 µg / L to about 200 µg / L, about 20 µg / L to about 200 µg / L, about 25 µg / L to about 200 µg / L, about 30 µg / L to about 200 µg / L, about 40 µg / L to about 200 µg / L, about 50 µg / L to about 200 µg / L, about 60 µg / L to about 200 µg / L, about 70 µg / L to about 200 µg / L, about 75 µg / L to about 200 µg / L, about 80 µg / L to about 200 µg / L, about 90 µg / L to about 200 µg / L, about 100 µg / L to about 200 µg / L, about 125 µg / L to about 200 µg / L, about 150 µg / L to about 200 µg / L, about 158.8 µg / L to about 200 µg / L, about 175 µg / L to about 200 µg / L, about 10 µg / L to about 175 µg / L, about 11.4 µg / L to about 175 µg / L, about 11.5 µg / L to about 175 µg / L, about 12.5 µg / L to about 175 µg / L, about 20 µg / L to about 175 µg / L, about 25 µg / L to about 175 µg / L, about 30 µg / L to about 175 µg / L, about 40 µg / L to about 175 µg / L, about 50 µg / L to about 175 µg / L, about 60 µg / L to about 175 µg / L, about 70 µg / L to about 175 µg / L, about 75 µg / L to about 175 µg / L, about 80 µg / L to about 175 µg / L, about 90 µg / L to about 175 µg / L, about 100 µg / L to about 175 µg / L, about 125 µg / L to about 175 µg / L, about 150 µg / L to about 175 µg / L, about 158.8 µg / L to about 175 µg / L, about 10 µg / L to about 150 µg / L, about 11.4 µg / L to about 150 µg / L, about 11.5 µg / L to about 150 µg / L, about 12.5 µg / L to about 150 µg / L, about 20 µg / L to about 150 µg / L, about 25 µg / L to about 150 µg / L, about 30 µg / L to about 150 µg / L, about 40 µg / L to about 150 µg / L, about 50 µg / L to about 150 µg / L, about 60 µg / L to about 150 µg / L, about 70 µg / L to about 150 µg / L, about 75 µg / L to about 150 µg / L, about 80 µg / L to about 150 µg / L, about 90 µg / L to about 150 µg / L, about 100 µg / L to about 150 µg / L, about 125 µg / L to about 150 µg / L, about 10 µg / L to about 125 µg / L, about 11.4 µg / L to about 125 µg / L, about 11.5 µg / L to about 125 µg / L, about 12.5 µg / L to about 125 µg / L, about 20 µg / L to about 125 µg / L, about 25 µg / L to about 125 µg / L, about 30 µg / L to about 125 µg / L, about 40 µg / L to about 125 µg / L, about 50 µg / L to about 125 µg / L, about 60 µg / L to about 125 µg / L, about 70 µg / L to about 125 µg / L, about 75 µg / L to about 125 µg / L, about 80 µg / L to about 125 µg / L, about 90 µg / L to about 125 µg / L, about 100 µg / L to about 125 µg / L, about 10 µg / L to about 100 µg / L, about 11.4 µg / L to about 100 µg / L, about 11.5 µg / L to about 100 µg / L, about 12.5 µg / L to about 100 µg / L, about 20 µg / L to about 100 µg / L, about 25 µg / L to about 100 µg / L, about 30 µg / L to about 100 µg / L, about 40 µg / L to about 100 µg / L, about 50 µg / L to about 100 µg / L, about 60 µg / L to about 100 µg / L, about 70 µg / L to about 100 µg / L, about 75 µg / L to about 100 µg / L, about 80 µg / L to about 100 µg / L, about 90 µg / L to about 100 µg / L, about 10 µg / L to about 90 µg / L, about 11.4 µg / L to about 90 µg / L, about 11.5 µg / L to about 90 µg / L, about 12.5 µg / L to about 90 µg / L, about 20 µg / L to about 90 µg / L, about 25 µg / L to about 90 µg / L, about 30 µg / L to about 90 µg / L, about 40 µg / L to about 90 µg / L, about 50 µg / L to about 90 µg / L, about 60 µg / L to about 90 µg / L, about 70 µg / L to about 90 µg / L, about 75 µg / L to about 90 µg / L, about 80 µg / L to about 90 µg / L, about 10 µg / L to about 80 µg / L, about 11.4 µg / L to about 80 µg / L, about 11.5 µg / L to about 80 µg / L, about 12.5 µg / L to about 80 µg / L, about 20 µg / L to about 80 µg / L, about 25 µg / L to about 80 µg / L, about 30 µg / L to about 80 µg / L, about 40 µg / L to about 80 µg / L, about 50 µg / L to about 80 µg / L, about 60 µg / L to about 80 µg / L, about 70 µg / L to about 80 µg / L, about 75 µg / L to about 80 µg / L, about 10 µg / L to about 75 µg / L, about 11.4 µg / L to about 75 µg / L, about 11.5 µg / L to about 75 µg / L, about 12.5 µg / L to about 75 µg / L, about 20 µg / L to about 75 µg / L, about 25 µg / L to about 75 µg / L, about 30 µg / L to about 75 µg / L, about 40 µg / L to about 75 µg / L, about 50 µg / L to about 75 µg / L, about 60 µg / L to about 75 µg / L, about 70 µg / L to about 75 µg / L, about 10 µg / L to about 70 µg / L, about 11.4 µg / L to about 70 µg / L, about 11.5 µg / L to about 70 µg / L, about 12.5 µg / L to about 70 µg / L, about 20 µg / L to about 70 µg / L, about 25 µg / L to about 70 µg / L, about 30 µg / L to about 70 µg / L, about 40 µg / L to about 70 µg / L, about 50 µg / L to about 70 µg / L, about 60 µg / L to about 70 µg / L, about 10 µg / L to about 60 µg / L, about 11.4 µg / L to about 60 µg / L, about 11.5 µg / L to about 60 µg / L, about 12.5 µg / L to about 60 µg / L, about 20 µg / L to about 60 µg / L, about 25 µg / L to about 60 µg / L, about 30 µg / L to about 60 µg / L, about 40 µg / L to about 60 µg / L, about 50 µg / L to about 60 µg / L, about 10 µg / L to about 50 µg / L, about 11.4 µg / L to about 50 µg / L, about 11.5 µg / L to about 50 µg / L, about 12.5 µg / L to about 50 µg / L, about 20 µg / L to about 50 µg / L, about 25 µg / L to about 50 µg / L, about 30 µg / L to about 50 µg / L, about 40 µg / L to about 50 µg / L, about 10 µg / L to about 40 µg / L, about 11.4 µg / L to about 40 µg / L, about 11.5 µg / L to about 40 µg / L, about 12.5 µg / L to about 40 µg / L, about 20 µg / L to about 40 µg / L, about 25 µg / L to about 40 µg / L, about 30 µg / L to about 40 µg / L, about 10 µg / L to about 30 µg / L, about 11.4 µg / L to about 30 µg / L, about 11.5 µg / L to about 30 µg / L, about 12.5 µg / L to about 30 µg / L, about 20 µg / L to about 30 µg / L, about 25 µg / L to about 30 µg / L, about 10 µg / L to about 25 µg / L, about 11.4 µg / L to about 25 µg / L, about 11.5 µg / L to about 25 µg / L, about 12.5 µg / L to about 25 µg / L, about 20 µg / L to about 25 µg / L, about 10 µg / L to about 20 µg / L, about 11.4 µg / L to about 20 µg / L, about 11.5 µg / L to about 20 µg / L, about 12.5 µg / L to about 20 µg / L, or about 10, 11.4, 11.5, 12.5, 20, 25, 30, 40, 45, 50, 60, 70, 75, 80, 90, 100, 125, 150, 158.8, 175, 200, 250, 300, 400, 500, 529.2, 600, 700, 800, 900, 1000, 1094.7, 1100, 1200, 1300, 1360, 1386.4, 1400, 1500, 1753, 2000, 3000, 4000, 5000, 5500 µg / L or any range or value therebetween. In some embodiments, the fermented product comprises phenethyl acetate and isoamyl acetate in an amount from about 11.4 µg / L to about 1094.7 µg / L. In some embodiments, the fermented product comprises acetate esters (total phenethyl acetate, isoamyl acetate and ethyl acetate) in an amount from about 500 µg / L to about 6500 µg / L. In some embodiments, the fermented product comprises acetate esters (total phenethyl acetate, isoamyl acetate and ethyl acetate) in an amount from about 500 µg / L to about 6500 µg / L, about 536.2 µg / L to about 6500 µg / L, about 536.3 µg / L to about 6500 µg / L, about 574.5 µg / L to about 6500 µg / L, about 600 µg / L to about 6500 µg / L, about 700 µg / L to about 6500 µg / L, about 800 µg / L to about 6500 µg / L, about 900 µg / L to about 6500 µg / L, about 1000 µg / L to about 6500 µg / L, about 1500 µg / L to about 6500 µg / L, about 2000 µg / L to about 6500 µg / L, about 2500 µg / L to about 6500 µg / L, about 3000 µg / L to about 6500 µg / L, about 3500 µg / L to about 6500 µg / L, about 4000 µg / L to about 6500 µg / L, about 4500 µg / L to about 6500 µg / L, about 5000 µg / L to about 6500 µg / L, about 5500 µg / L to about 6500 µg / L, about 6000 µg / L to about 6500 µg / L, about 500 µg / L to about 6219 µg / L, about 536.2 µg / L to about 6219 µg / L, about 536.3 µg / L to about 6219 µg / L, about 574.5 µg / L to about 6219 µg / L, about 600 µg / L to about 6219 µg / L, about 700 µg / L to about 6219 µg / L, about 800 µg / L to about 6219 µg / L, about 900 µg / L to about 6219 µg / L, about 1000 µg / L to about 6219 µg / L, about 1500 µg / L to about 6219 µg / L, about 2000 µg / L to about 6219 µg / L, about 2500 µg / L to about 6219 µg / L, about 3000 µg / L to about 6219 µg / L, about 3500 µg / L to about 6219 µg / L, about 4000 µg / L to about 6219 µg / L, about 4500 µg / L to about 6219 µg / L, about 5000 µg / L to about 6219 µg / L, about 5500 µg / L to about 6219 µg / L, about 6000 µg / L to about 6219 µg / L, about 500 µg / L to about 6000 µg / L, about 536.2 µg / L to about 6000 µg / L, about 536.3 µg / L to about 6000 µg / L, about 574.5 µg / L to about 6000 µg / L, about 600 µg / L to about 6000 µg / L, about 700 µg / L to about 6000 µg / L, about 800 µg / L to about 6000 µg / L, about 900 µg / L to about 6000 µg / L, about 1000 µg / L to about 6000 µg / L, about 1500 µg / L to about 6000 µg / L, about 2000 µg / L to about 6000 µg / L, about 2500 µg / L to about 6000 µg / L, about 3000 µg / L to about 6000 µg / L, about 3500 µg / L to about 6000 µg / L, about 4000 µg / L to about 6000 µg / L, about 4500 µg / L to about 6000 µg / L, about 5000 µg / L to about 6000 µg / L, about 5500 µg / L to about 6000 µg / L, about 500 µg / L to about 5500 µg / L, about 536.2 µg / L to about 5500 µg / L, about 536.3 µg / L to about 5500 µg / L, about 574.5 µg / L to about 5500 µg / L, about 600 µg / L to about 5500 µg / L, about 700 µg / L to about 5500 µg / L, about 800 µg / L to about 5500 µg / L, about 900 µg / L to about 5500 µg / L, about 1000 µg / L to about 5500 µg / L, about 1500 µg / L to about 5500 µg / L, about 2000 µg / L to about 5500 µg / L, about 2500 µg / L to about 5500 µg / L, about 3000 µg / L to about 5500 µg / L, about 3500 µg / L to about 5500 µg / L, about 4000 µg / L to about 5500 µg / L, about 4500 µg / L to about 5500 µg / L, about 5000 µg / L to about 5500 µg / L, about 500 µg / L to about 5000 µg / L, about 536.2 µg / L to about 5000 µg / L, about 536.3 µg / L to about 5000 µg / L, about 574.5 µg / L to about 5000 µg / L, about 600 µg / L to about 5000 µg / L, about 700 µg / L to about 5000 µg / L, about 800 µg / L to about 5000 µg / L, about 900 µg / L to about 5000 µg / L, about 1000 µg / L to about 5000 µg / L, about 1500 µg / L to about 5000 µg / L, about 2000 µg / L to about 5000 µg / L, about 2500 µg / L to about 5000 µg / L, about 3000 µg / L to about 5000 µg / L, about 3500 µg / L to about 5000 µg / L, about 4000 µg / L to about 5000 µg / L, about 4500 µg / L to about 5000 µg / L, about 500 µg / L to about 4725.4 µg / L, about 536.2 µg / L to about 4725.4 µg / L, about 536.3 µg / L to about 4725.4 µg / L, about 574.5 µg / L to about 4725.4 µg / L, about 600 µg / L to about 4725.4 µg / L, about 700 µg / L to about 4725.4 µg / L, about 800 µg / L to about 4725.4 µg / L, about 900 µg / L to about 4725.4 µg / L, about 1000 µg / L to about 4725.4 µg / L, about 1500 µg / L to about 4725.4 µg / L, about 2000 µg / L to about 4725.4 µg / L, about 2500 µg / L to about 4725.4 µg / L, about 3000 µg / L to about 4725.4 µg / L, about 3500 µg / L to about 4725.4 µg / L, about 4000 µg / L to about 4725.4 µg / L, about 4500 µg / L to about 4725.4 µg / L, about 500 µg / L to about 4500 µg / L, about 536.2 µg / L to about 4500 µg / L, about 536.3 µg / L to about 4500 µg / L, about 574.5 µg / L to about 4500 µg / L, about 600 µg / L to about 4500 µg / L, about 700 µg / L to about 4500 µg / L, about 800 µg / L to about 4500 µg / L, about 900 µg / L to about 4500 µg / L, about 1000 µg / L to about 4500 µg / L, about 1500 µg / L to about 4500 µg / L, about 2000 µg / L to about 4500 µg / L, about 2500 µg / L to about 4500 µg / L, about 3000 µg / L to about 4500 µg / L, about 3500 µg / L to about 4500 µg / L, about 4000 µg / L to about 4500 µg / L, about 500 µg / L to about 4000 µg / L, about 536.2 µg / L to about 4000 µg / L, about 536.3 µg / L to about 4000 µg / L, about 574.5 µg / L to about 4000 µg / L, about 600 µg / L to about 4000 µg / L, about 700 µg / L to about 4000 µg / L, about 800 µg / L to about 4000 µg / L, about 900 µg / L to about 4000 µg / L, about 1000 µg / L to about 4000 µg / L, about 1500 µg / L to about 4000 µg / L, about 2000 µg / L to about 4000 µg / L, about 2500 µg / L to about 4000 µg / L, about 3000 µg / L to about 4000 µg / L, about 3500 µg / L to about 4000 µg / L, about 500 µg / L to about 3500 µg / L, about 536.2 µg / L to about 3500 µg / L, about 536.3 µg / L to about 3500 µg / L, about 574.5 µg / L to about 3500 µg / L, about 600 µg / L to about 3500 µg / L, about 700 µg / L to about 3500 µg / L, about 800 µg / L to about 3500 µg / L, about 900 µg / L to about 3500 µg / L, about 1000 µg / L to about 3500 µg / L, about 1500 µg / L to about 3500 µg / L, about 2000 µg / L to about 3500 µg / L, about 2500 µg / L to about 3500 µg / L, about 3000 µg / L to about 3500 µg / L, about 500 µg / L to about 3000 µg / L, about 536.2 µg / L to about 3000 µg / L, about 536.3 µg / L to about 3000 µg / L, about 574.5 µg / L to about 3000 µg / L, about 600 µg / L to about 3000 µg / L, about 700 µg / L to about 3000 µg / L, about 800 µg / L to about 3000 µg / L, about 900 µg / L to about 3000 µg / L, about 1000 µg / L to about 3000 µg / L, about 1500 µg / L to about 3000 µg / L, about 2000 µg / L to about 3000 µg / L, about 2500 µg / L to about 3000 µg / L, about 500 µg / L to about 2500 µg / L, about 536.2 µg / L to about 2500 µg / L, about 536.3 µg / L to about 2500 µg / L, about 574.5 µg / L to about 2500 µg / L, about 600 µg / L to about 2500 µg / L, about 700 µg / L to about 2500 µg / L, about 800 µg / L to about 2500 µg / L, about 900 µg / L to about 2500 µg / L, about 1000 µg / L to about 2500 µg / L, about 1500 µg / L to about 2500 µg / L, about 2000 µg / L to about 2500 µg / L, about 500 µg / L to about 2000 µg / L, about 536.2 µg / L to about 2000 µg / L, about 536.3 µg / L to about 2000 µg / L, about 574.5 µg / L to about 2000 µg / L, about 600 µg / L to about 2000 µg / L, about 700 µg / L to about 2000 µg / L, about 800 µg / L to about 2000 µg / L, about 900 µg / L to about 2000 µg / L, about 1000 µg / L to about 2000 µg / L, about 1500 µg / L to about 2000 µg / L, about 500 µg / L to about 1500 µg / L, about 536.2 µg / L to about 1500 µg / L, about 536.3 µg / L to about 1500 µg / L, about 574.5 µg / L to about 1500 µg / L, about 600 µg / L to about 1500 µg / L, about 700 µg / L to about 1500 µg / L, about 800 µg / L to about 1500 µg / L, about 900 µg / L to about 1500 µg / L, about 1000 µg / L to about 1500 µg / L, about 500 µg / L to about 1000 µg / L, about 536.2 µg / L to about 1000 µg / L, about 536.3 µg / L to about 1000 µg / L, about 574.5 µg / L to about 1000 µg / L, about 600 µg / L to about 1000 µg / L, about 700 µg / L to about 1000 µg / L, about 800 µg / L to about 1000 µg / L, about 900 µg / L to about 1000 µg / L, about 500 µg / L to about 900 µg / L, about 536.2 µg / L to about 900 µg / L, about 536.3 µg / L to about 900 µg / L, about 574.5 µg / L to about 900 µg / L, about 600 µg / L to about 900 µg / L, about 700 µg / L to about 900 µg / L, about 800 µg / L to about 900 µg / L, about 500 µg / L to about 800 µg / L, about 536.2 µg / L to about 800 µg / L, about 536.3 µg / L to about 800 µg / L, about 574.5 µg / L to about 800 µg / L, about 600 µg / L to about 800 µg / L, about 700 µg / L to about 800 µg / L, about 500 µg / L to about 700 µg / L, about 536.2 µg / L to about 700 µg / L, about 536.3 µg / L to about 700 µg / L, about 574.5 µg / L to about 700 µg / L, about 600 µg / L to about 700 µg / L, about 500 µg / L to about 600 µg / L, about 536.2 µg / L to about 600 µg / L, about 536.3 µg / L to about 600 µg / L, about 574.5 µg / L to about 600 µg / L, or about 500, 536.2, 536.3, 574.5, 600, 700, 800, 900, 1000, 1500, 2000, 2500, 3000, 3500, 4000, 4500, 4725.4, 5000, 5460.2, 5500, 6000, 6219, or 6500 µg / L or any range or value therebetween. In some embodiments, the fermented product comprises acetate esters (total phenethyl acetate, isoamyl acetate and ethyl acetate) in an amount from about 536.2 µg / L to about 4725.4 µg / L. It should be understood that the fermentation methods provided herein can be performed under conditions sufficient to produce the desired amount of isoamyl acetate, phenethyl acetate, isoamyl acetate and phenethyl acetate or total acetate esters (isoamyl acetate, phenethyl acetate and isoamyl acetate). In some embodiments, a liquid fermentation composition is provided that comprises: (a) a population of genetically modified yeast cells that are genetically modified to produce one or more acetate esters and / or ethyl esters, where the genetically modified yeast cells are incapable of or have a reduced capability of converting maltose and / or maltotriose to ethanol, (b) a sugar source comprising wort, wherein total sugar in the wort has be attenuated by no more than 25% by the population of genetically modified yeast cells, (c) one or more wort- derived aldehydic and / or non-aldehyde molecules, and (d) no more than about 1.0% (v / v) alcohol. In some embodiments, the liquid fermentation composition contains no more than about 0.5% (v / v) alcohol. In some embodiments, a liquid fermentation composition is provided that comprises: (a) a population of genetically modified yeast cells that are genetically modified to be incapable of or to have a reduced capability of converting maltose and / or maltotriose to ethanol, (b) a sugar source comprising wort, wherein total sugar in the wort has been attenuated by no more than 25% by the population of genetically modified yeast cells, and (c) no more than 1.0% (v / v) alcohol. In some embodiments, the liquid fermentation composition contains no more than about 0.5% (v / v) alcohol. It should be understood that throughout this disclosure, the alcohol by volume provided can include 0% or a minimum value or maximum value, e.g. a minimum of 0.01% alcohol by volume and a maximum of 1.0% alcohol by volume. It should be understood that, in alternative embodiments of the disclosure, the liquid fermentation composition or fermented beverage and / or product has an alcohol by volume of no more than 5% or no more than 2.5%. It should be understood that the population of genetically modified yeast cells can be the modified cells of any aspect(s) of the present disclosure. In some embodiments, the aldehydic molecule is selected from the group consisting of 2-methylbutanal, 2-methylpropanal, hexanal, benzaldehyde, furfural, acetaldehyde, methional, phenylacetaldehyde, and 5-hydrox-methyl-furfural. In some embodiments, the non-aldehyde molecule is selected from the group consisting of (E)-beta-damascenone and 5- ethyl-3-hydroxy-4-methyl-2(5H)-furanone. It should also be understood that the levels of acetate ester(s) and / or ethyl ester(s) recited herein can be characteristic of liquid fermentation compositions disclosed herein. The methods described herein may involve at least one additional fermentation process. Such additional fermentation methods may be referred to as secondary fermentation processes (also referred to as “aging” or “maturing”). As will be understood by one of ordinary skill in the art, secondary fermentation typically involves transferring a fermented beverage to a second receptacle (e.g., glass carboy, barrel) where the fermented beverage is incubated for a period of time. In some embodiments, the secondary fermentation is performed for a period of time between 10 minutes and 12 months. In some embodiments, the secondary fermentation is performed for 10 minutes, 20 minutes, 40 minutes, 40 minutes, 50 minutes, 60 minutes (1 hour), 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 7 hours, 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 13 hours, 14 hours, 15 hours, 16 hours, 17 hours, 18 hours, 19 hours, 20 hours, 21 hours, 22 hours, 23 hours, 24 hours, 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 14 days, 2 weeks, 3 weeks, 4 weeks, 5 weeks, 6 weeks, 7 weeks, 8 weeks, 9 weeks, 10 weeks, 11 weeks, 12 weeks, 13 weeks, 14 weeks, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 12 months, or longer. In some embodiments, the additional or secondary fermentation process of the one or more fermentable sugars may be performed at a temperature of about 4°C to about 30°C. In some embodiments, the additional or secondary fermentation process of one or more fermentable sugars may be carried out at temperature of about 8°C to about 14°C or about 18°C to about 24°C. In some embodiments, the additional or secondary fermentation process of one or more fermentable sugars may be performed at a temperature of about 4°C, 5°C, 6°C, 7°C, 8°C, 9°C, 10°C, 11°C, 12°C, 13°C, 14°C, 15°C, 16°C, 17°C, 18°C, 19°C, 20°C, 21°C, 22°C, 23°C, 24°C, 25°C, 26°C, 27°C, 28°C, 29°C, or 30°C. As will be evident to one of ordinary skill in the art, selection of a time period and temperature for an additional or secondary fermentation process will depend on factors such as the type of beer, the characteristics of the beer desired, and the yeast strain used in the methods. In some embodiments, one or more additional flavor components may be added to the medium prior to or after the fermentation process. Examples include, hop oil, hop aromatics, hop extracts, hop bitters, and isomerized hops extract. Various refinement, filtration, and aging processes may occur subsequent fermentation, after which the liquid is bottled (e.g., captured and sealed in a container for distribution, storage, or consumption). Any of the methods described herein may further involve distilling, pasteurizing, and / or carbonating the fermented product. In some embodiments, the methods involve carbonating the fermented product. Methods of carbonating fermented beverages are known in the art and include, for example, force carbonating with a gas (e.g., carbon dioxide, nitrogen), naturally carbonating by adding a further sugar source to the fermented beverage to promote further fermentation and production of carbon dioxide (e.g., bottle conditioning). Fermented Products Aspects of the present disclosure relate to fermented products produced by any of the methods disclosed herein. In some embodiments, the fermented product is a fermented beverage. In some embodiments, the beverage is beer. In some embodiments, the beverage is sake. In some embodiments, the fermented product is a fermented food product. Examples of fermented food products include, without limitation, cultured yogurt, tempeh, miso, kimchi, sauerkraut, fermented sausage, bread, and soy sauce. Aspects of the present disclosure relate to reducing the sensory detection of undesired molecules such as wort-associated off-flavors in a fermented product. In some embodiments, production of acetate esters and / or ethyl esters, as described herein, results in a reduction in sensory detection of undesired wort-associated off-flavors in a fermented product by about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95% or more relative to sensory detection of undesired wort-associated off-flavors in a fermented product produced using yeast cells that do not produce the acetate esters and / or ethyl esters. In some embodiments, production of 3-mercaptohexanol (3MH), as described herein, results in a reduction in sensory detection of undesired wort-associated off-flavors in a fermented product by about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95% or more relative to sensory detection of undesired wort-associated off-flavors in a fermented product produced using yeast cells that do not produce 3MH. In some embodiments, production of one or more monoterpenes (e.g., linalool, geraniol, and / or citronellol), as described herein, results in a reduction in sensory detection of undesired wort-associated off-flavors in a fermented product by about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95% or more relative to sensory detection of undesired wort-associated off-flavors in a fermented product produced using yeast cells that do not produce the one or more monoterpenes. Methods of measuring levels of wort-associated off-flavors, or a molecule that contributes to the wort-associated off-flavor, will be evident to one of ordinary skill in the art and may include sensory detection (e.g., taste, smell, appearance), for example by a sensory panel of subjects, including for example human taste-testers. In some embodiments, the levels of wort-associated off-flavors, or a molecule that contributes to the wort-associated off-flavor, are measured using gas-chromatography mass-spectrometry (GC / MS). In some embodiments, the levels of wort-associated off-flavors, or a molecule that contributes to the wort-associated off-flavor, are measured using liquid-chromatography mass-spectrometry (LC / MS). In some embodiments, the fermented beverage contains an alcohol by volume (also referred to as “ABV,” “abv,” or “alc / vol”) of less than or equal to about 0.5%, which is considered “non-alcoholic”. In some embodiments, the fermented beverage contains an alcohol by volume of less than about 0.1%, 0.2%, 0.3%, 0.4%, or 0.5%. In some embodiments, the fermented beverage is 0% alcohol by volume (zero alcohol). It should be understood that the fermented products, e.g. fermented beverages of the present disclosure can have the properties recited for the fermentation products throughout this disclosure, e.g. levels of acetate esters and / or ethyl esters and excluded compounds or compounds present below defined levels. Kits Aspects of the present disclosure also provide kits for use of the genetically modified yeast cells, for example to produce a fermented product, e.g., a fermented beverage. In some embodiments, the kit contains a modified cell containing one or more genetic modifications to reduce sensory detection of one or more wort-associated off-flavors of a fermented beverage, wherein the modified cell is not capable of converting maltose and / or maltorotriose to ethanol. In some embodiments, the kit is for the production of a fermented beverage. In some embodiments, the kit is for the production of beer. In some embodiments, the kit is for the production of sake. The kits may also comprise other components for use in any of the methods described herein, or for use of any of the cells as described herein. For example, in some embodiments, the kits may contain grains, water, wort, must, yeast, hops, juice, or other sugar source(s). In some embodiments, the kit may contain one or more fermentable sugars. In some embodiments, the kit may contain one or more additional agents, ingredients, or components. Instructions for performing the methods described herein may also be included in the kits described herein. The kits may be organized to indicate a single-use compositions containing any of the modified cells described herein. For example, the single use compositions (e.g., amount to be used) can be packaged compositions (e.g., modified cells) such as packeted (i.e., contained in a packet) powders, vials, ampoules, culture tube, tablets, caplets, capsules, or sachets containing liquids. The compositions (e.g., modified cells) may be provided in dried, lyophilized, frozen, or liquid forms. In some embodiments, the modified cells are provided as colonies on an agar medium. In some embodiments, the modified cells are provided in the form of a starter culture that may be pitched directly into a medium. When reagents or components are provided as a dried form, reconstitution generally is by the addition of a solvent, such as a medium. The solvent may be provided in another packaging means and may be selected by one skilled in the art. A number of packages or kits are known to those skilled in the art for dispensing a composition (e.g., modified cells). In certain embodiments, the package is a labeled blister package, dial dispenser package, tube, packet, drum, or bottle. Any of the kits described herein may further comprise one or more vessel for performing the methods described herein, such as a carboy or barrel. General Techniques The practice of the subject matter of the disclosure will employ, unless otherwise indicated, conventional techniques of molecular biology (including recombinant techniques), microbiology, cell biology, biochemistry, and immunology, which are within the skill of the art. Such techniques are explained fully in the literature, such as, but without limiting, Molecular Cloning: A Laboratory Manual, J. Sambrook, et al., eds., Fourth Edition, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 2012; Oligonucleotide Synthesis (M. J. Gait, ed., 1984); Methods in Molecular Biology, Humana Press; Cell Biology: A Laboratory Notebook (J. E. Cellis, ed., 1998) Academic Press; Animal Cell Culture (R. I. Freshney, ed., 1987); Introduction to Cell and Tissue Culture (J. P. Mather and P. E. Roberts, 1998) Plenum Press; Cell and Tissue Culture: Laboratory Procedures (A. Doyle, J. B. Griffiths, and D. G. Newell, eds., 1993-8) J. Wiley and Sons; Methods in Enzymology (Academic Press, Inc.); Handbook of Experimental Immunology (D. M. Weir and C. C. Blackwell, eds.); Gene Transfer Vectors for Mammalian Cells (J. M. Miller and M. P. Calos, eds., 1987); Current Protocols in Molecular Biology (F. M. Ausubel, et al., eds., 1987); PCR: The Polymerase Chain Reaction, (Mullis, et al., eds., 1994); Current Protocols in Immunology (J. E. Coligan et al., eds., 1991); Short Protocols in Molecular Biology (Wiley and Sons, 1999). Equivalents and Scope It is to be understood that this disclosure is not limited to any or all of the particular embodiments described expressly herein, and as such may, of course, vary. It is also to be understood that the terminology used herein is for the purpose of describing particular embodiments only and is not intended to be limiting. Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this disclosure belongs. Although any methods and materials similar or equivalent to those described herein can also be used in the practice or testing of the present disclosure, the preferred methods and materials are now described. All publications and patents cited in this disclosure are cited to disclose and describe the methods and / or materials in connection with which the publications are cited. All such publications and patents are herein incorporated by references as if each individual publication or patent were specifically and individually indicated to be incorporated by reference. Such incorporation by reference is expressly limited to the methods and / or materials described in the cited publications and patents and does not extend to any lexicographical definitions from the cited publications and patents (i.e., any lexicographical definition in the publications and patents cited that is not also expressly repeated in the disclosure should not be treated as such and should not be read as defining any terms appearing in the accompanying claims). If there is a conflict between any of the incorporated references and this disclosure, this disclosure shall control. In addition, any particular embodiment of this disclosure that falls within the prior art may be explicitly excluded from any one or more of the claims. Because such embodiments are deemed to be known to one of ordinary skill in the art, they may be excluded even if the exclusion is not set forth explicitly herein. Any particular embodiment of the disclosure can be excluded from any claim, for any reason, whether or not related to the existence of prior art. The citation of any publication is for its disclosure prior to the filing date and should not be construed as an admission that the present disclosure is not entitled to antedate such publication by virtue of prior disclosure. Further, the dates of publication provided could be different from the actual publication dates that may need to be independently confirmed. As will be apparent to those of skill in the art upon reading this disclosure, each of the individual embodiments described and illustrated herein has discrete components and features which may be readily separated from or combined with the features of any of the other several embodiments without departing from the scope or spirit of the present disclosure. Any recited method can be carried out in the order of events recited or in any other order that is logically possible. In the claims articles such as “a,” “an,” and “the” may mean one or more than one unless indicated to the contrary or otherwise evident from the context. Wherever used herein, a pronoun in a gender (e.g., masculine, feminine, neuter, other, etc.) the pronoun shall be construed as gender neutral (i.e., construed to refer to all genders equally) regardless of the implied gender unless the context clearly indicates or requires otherwise. Wherever used herein, words used in the singular include the plural, and words used in the plural include the singular, unless the context clearly indicates or requires otherwise. Claims or descriptions that include “or” between one or more members of a group are considered satisfied if one, more than one, or all of the group members are present in, employed in, or otherwise relevant to a given product or process unless indicated to the contrary or otherwise evident from the context. The disclosure includes embodiments in which exactly one member of the group is present in, employed in, or otherwise relevant to a given product or process. The disclosure includes embodiments in which more than one, or all of the group members are present in, employed in, or otherwise relevant to a given product or process. Furthermore, the disclosure encompasses all variations, combinations, and permutations in which one or more limitations, elements, clauses, and descriptive terms from one or more of the listed claims is introduced into another claim. For example, any claim that is dependent on another claim can be modified to include one or more limitations found in any other claim that is dependent on the same base claim. Where elements are presented as lists (e.g., in Markush group format), each subgroup of the elements is also disclosed, and any element(s) can be removed from the group. It should be understood that, in general, where the disclosure, or aspects of the disclosure, is / are referred to as comprising particular elements and / or features, certain embodiments of the disclosure or aspects of the disclosure consist, or consist essentially of, such elements and / or features. For purposes of simplicity, those embodiments have not been specifically set forth in haec verba herein. It is also noted that the terms “comprising” and “containing” are intended to be open and permits the inclusion of additional elements or steps. Where ranges are given, endpoints are included in such ranges unless otherwise specified. Furthermore, unless otherwise indicated or otherwise evident from the context and understanding of one of ordinary skill in the art, values that are expressed as ranges can assume any specific value or sub–range within the stated ranges in different embodiments of the disclosure, to the tenth of the unit of the lower limit of the range, unless the context clearly dictates otherwise. Those skilled in the art will recognize or be able to ascertain using no more than routine experimentation many equivalents to the specific embodiments described herein. The scope of the present embodiments described herein is not intended to be limited to the above Description, but rather is as set forth in the appended claims. Those of ordinary skill in the art will appreciate that various changes and modifications to this description may be made without departing from the spirit or scope of the disclosure, as defined in the following claims. EXAMPLES Example 1: Maltose-negative yeast strain engineering As described herein, the limited number of maltose-negative yeast strains for brewing presents a significant challenge in the brewing industry. For non-alcoholic beer produced by arrested fermentation with currently available maltose-negative strains, these methods have been associated with substantial worty flavors and aromas. Worty flavors in arrested fermentation beer is a result of the presence of a combination of aldehyde and non-aldehydic molecules. These aldehyde molecules are present in the unfermented wort, and during a normal alcoholic fermentation, the yeast either converts them into other molecules that do not impart flavor, or it sufficiently alters the chemical composition of the beer through the production of ethanol and other flavor molecules such that these molecules are no longer perceptible. In contrast, in an arrested fermentation with maltose-negative strains, it is thought that one or both of these processes do not occur or occur at reduced levels, hence the aldehydes are present and very perceptible as off-flavors in the finished beer. Brewer’s yeast strains contain several different genes for maltose transporters that are responsible for transporting maltose and maltotriose sugars inside the cell. Duplications and rearranges of maltose transporter genes are common among brewing yeast, and brewing strains frequently have greater than 10, or even up to 15 distinct copies of maltose transporter genes encoded in their genomes. Due to the frequent genetic duplications, deletions, and rearranges that occur at maltose transport loci, yeast strains frequently rely on distinct combinations of maltose transporter genes to enable transport of maltose and maltotriose sugars into the cell. Therefore, while deletion of maltose transporter genes is expected to stop yeast from metabolizing certain sugars, it is not clear or predictable which combination of genes need to be deleted to make the strain maltose-negative (deficient in conversion of maltose and / or maltotriose to ethanol). Previously, some MN non-brewing yeast strains were generated by deleting one or more distinct combinations of maltose transporters, but none of these strains had any history of use for brewing beer. If such strains were to be used for brewing, they would likely create off-flavors commonly associated with yeast strains not adapted to beer fermentation (Yabaci Karaoglan, S., Jung, R., Gauthier, M., Kinčl, T. & Dostálek, P. Maltose-Negative Yeast in Non-Alcoholic and Low-Alcoholic Beer Production. Fermentation 8, 273 (2022); Simões, J. et al. Exploiting Non-Conventional Yeasts for Low- Alcohol Beer Production. Microorganisms 11, (2023)). To generate a novel MN yeast variant of an existing brewing yeast strain, the Saccharomyces cerevisiae Chico strain was used. Chico is one of the most widely used craft brewing strains, known for producing clean ales and being a strong flocculator. Unlike other yeast strains engineered previously, the S. cerevisiae Chico strain is known to metabolize both maltose and maltotriose. To engineer the S. cerevisiae Chico strain deficient in maltose and maltotriose fermentation, the genes predicted to be involved in transport of both these wort sugars were deleted. After analyzing genome sequence of the strain (Gallone, B. et al. Domestication and Divergence of Saccharomyces cerevisiae Beer Yeasts. Cell 166, 1397– 1410.e16 (2016)), the genes most likely to encode functional maltose and maltotriose transports were identified as MAL31 and MAL11 (AGT1). Using targeting strain engineering techniques, both of these genes were deleted in S. cerevisiae Chico strain, thus creating strain BY632 (S. cerevisiae Chico MAL31::Δ AGT::Δ). Small scale 20 L beer fermentation experiments were performed with wild-type S. cerevisiae Chico and strain BY632. The fermentations were started with a total wort sugar content of 12° Plato. As shown in FIG.2, BY632 consumed ~21% of the wort sugars during the first 50 hours, after which no additional consumption of wort sugars occurred. In contrast, the parental wild-type S. cerevisiae Chico consumed ~79% of the wort sugars during the 250 hour fermentation. The low attenuation observed for BY632 is due to consumption of glucose in the wort but not maltose or maltotriose, confirming it is a maltose- negative (MN) strain. Notably, the deletion of MAL31 and MAL11 that was necessary to make S. cerevisiae Chico MN are a different combination of maltose transporter genes than those previously deleted to make other non-brewing yeast strains MN, as described above (Yabaci Karaoglan, S., Jung, R., Gauthier, M., Kinčl, T. & Dostálek, P. Maltose-Negative Yeast in Non-Alcoholic and Low-Alcoholic Beer Production. Fermentation 8, 273 (2022); Simões, J. et al. Exploiting Non-Conventional Yeasts for Low-Alcohol Beer Production. Microorganisms 11, (2023)). Example 2: Engineering strains to mask worty flavors in non-alcoholic beer The worty flavors associated with non-alcoholic beers produced by arrested fermentation have been largely attributed to a set of ~10 volatile aldehyde molecules present in these beers, as well as several non-aldehyde molecules like (E)-β-damascenone and 5- ethyl-3-hydroxy-4-methyl-2(5H)-furanone (Gernat, D. C., Brouwer, E. & Ottens, M. Aldehydes as Wort Off-Flavours in Alcohol-Free Beers—Origin and Control. Food Bioprocess Technol.13, 195–216 (2019); Piornos, J. A. et al. Elucidating the Odor-Active Aroma Compounds in Alcohol-Free Beer and Their Contribution to the Worty Flavor. J. Agric. Food Chem. (2020) doi:10.1021 / acs.jafc.0c03902). In some NA beers, the sensory off- notes imparted by these “worty aldehyde” molecules are more pronounced in the aroma, whereas in other beers they are more apparent upon tasting. Many or all of these same aldehyde molecules are also found in alcoholic beers, but due to differences in their concentration and the overall different chemical compositions of alcoholic and non-alcoholic beers, the aldehydic and non-aldehyde molecules produce fewer sensory defects in alcohol beers. Previously it has been shown that worty aromas and off-flavors in non-alcoholic beers produced by arrested fermentation can be reduced by spiking additional exogenous flavor molecules into the beer to mask the perception of the worty notes. For example, addition of exogenous terpineol to unfermented brewing wort was found to reduce the perception of worty flavors and aromas in the wort (Murakami, A., Kawasaki, Y., Ohta, R. & Furukawa, J. Malt beverage having reduced wort off-flavor and process for production thereof. US Patent (2013)), or addition of exogenous isoamyl acetate to lager beer led to an increase in the flavor detection thresholds (less detection) of two worty-aldehyde molecules that were spiked into the same beer (Saison, D., De Schutter, D. P., Uyttenhove, B., Delvaux, F. & Delvaux, F. R. Contribution of staling compounds to the aged flavour of lager beer by studying their flavour thresholds. Food Chem.114, 1206–1215 (2009)). Engineering strains for production of acetate esters and / or ethyl esters Ethyl acetate, isoamyl acetate, and phenethyl acetate are three acetate esters generally produced by yeast during the course of a typical beer fermentation and are major contributors to the “beer-like” aroma and flavor of alcoholic beer [Cite PMID: 38531860]. The concentrations of these three esters in beer can vary greatly depending on the beer style, %ABV, and yeast strain used for fermentation. In general, the range of concentration found in beer are 0-75 mg / L for ethyl acetate, 0-10 mg / L for isoamyl acetate, and 0-1 mg / L for phenethyl acetate (FIG.3A) [Cite PMID: 38531860]. During arrested fermentation, however, reduced levels of these acetate esters are produced due to the reduced levels of wort attenuation and yeast metabolic activity, as well as the lower concentration of ethanol which is required for ethyl acetate biosynthesis. To increase yeast-biosynthesis of ethyl acetate, isoamyl acetate, and phenethyl acetate, the BY632 strain (S. cerevisiae Chico MAL11::Δ AGT1::Δ) was engineered to express enzymes having alcohol-acyltransferase (AAT) activity. Expression of two distinct AAT enzymes was attempted: the S. cerevisiae alcohol-acyltransferase (AAT) enzyme Atf1 (SEQ ID NO: 5), and the Cucumis melo (melon) AAT enzyme, CmAAT1 (SEQ ID NO: 7). Both of these AATs produce all three of the target acetate ester molecules, with CmAAT1 additionally producing several medium chain ethyl esters molecules that positively contribute to beer aroma and flavor. For each of these two AAT enzymes, multiple strains were constructed each of which encoded a distinct promoter sequence driving AAT expression. Each of these promoters was associated with a distinct expression level during beer fermentation as determined by RNA- seq expression measurements. The complete list of strains constructed along with the promoter-AAT genotypes and relative strength of expression of each promoter is shown in the Table 1 below.

[0002] Table 1. All engineered strains are derived from the wild type “Chico” strain. The strength of expression of each promoter used to drive AAT expression is provided in the “Promoter TPMs” column. The data reported in the “Promoter TPMs” column are gene expression measurements in units of Transcripts per Million (TPM) for the genes corresponding to each promoter in a wild-type Chico yeast during beer fermentation as measured by RNA-seq. The “Isoamyl acetate log2 fold change” and “Phenethyl acetate log2 fold change” columns report the levels of these two esters produced by each strain, expressed as the log2 of the ratio of each engineered strain to the wild-type Chico strain, as described below. Each of these engineered strains, as well as Wild-type S. cerevisiae Chico and strain BY632 were used in small-scale malt extract fermentations in order to determine the aroma and concentrations of esters the strains would produce. Following five days of fermentation, the percent attenuation achieved by each strain was determined, and acetate ester and ethyl ester production was measured via gas chromatography-mass spectrometry (GC-MS). The percent attenuation measured for the wild type Chico strain was 84%, while for the MN strain BY632 it was ~17.5%. As expected, BY632 also produced far less isoamyl acetate and phenethyl acetate during fermentation than Chico (Table1). Fermentation with AAT-engineered strains resulted in attenuation that was similar to BY632, but the levels of the two measured acetate esters isoamyl acetate and phenethyl acetate) were higher in all fermentations with AAT-engineered strains than in BY632. The range of ester concentrations in fermentations with the AAT-engineered strains ranged from modestly increased relative to BY632 (e.g. BY1577, BY1578) to over 32-fold greater than even the wild-type Chico strain (e.g. BY1544, BY1504). The concentrations of these esters correlated nearly perfectly with the strength of promoter driving AAT expression in each strain: For each of the two AATs, promoters with higher TPM values were associated with higher levels of ester production, and promoters with lower TPMs resulted in lower levels of esters production. As shown in FIG.3B, in an aroma sensory analysis of these small scale fermentations, BY632 was determined to have a worty aroma, while AAT-engineered strains were determined to have a variety of aromas ranging from worty, to “beer-ey”, to banana / solvent. In general, strains displaying levels of acetate ester production lower than Chico were characterized as having undesirable worty aroma notes, while strains displaying acetate ester production similar to or modestly higher than Chico were characterized as having “beer-ey” aromas and a lack of worty-off notes. Strains with levels of acetate ester production far higher than Chico were characterized as having strong banana and solvent aromas, which is a sign of very high concentrations of isoamyl acetate and ethyl acetate (Note that while ethyl acetate was not measured in these experiments its concentration in beer is generally correlated with isoamyl acetate). While these banana and honey aromas did largely mask the perception of wortyness, their strong intensity detracted from the overall beer-like aroma of the fermentations. Taken together, these sensory data demonstrate that: 1) it is possible to engineer MN yeasts such that in an arrested fermentation, they produce levels of desired “beer-like” ester flavor molecules that are similar to or higher than their concentrations after alcoholic fermentation, and 2) production of these flavor compounds in specific quantities can mask worty flavors without introducing other undesirable aroma notes. Engineering BY632 for 3-mercaptohexanol (3MH) production 3-mercaptohexanol (3MH) is a volatile thiol molecule that is generally produced by yeast at very low levels ( <5 ng / L) during beer fermentation. It was previously demonstrated that expression of the bacterial enzyme having carbon-sulfur-lyase (CSL) activity led to the formation of 2-10 µg / L of 3MH during beer fermentation (Molitor, R. W. et al. The Sensorial and Chemical Changes in Beer Brewed with Yeast Genetically Modified to Release Polyfunctional Thiols from Malt and Hops. Fermentation 8, 370 (2022)). At these concentrations, 3MH imparts desirable guava / passionfruit flavors in beer. It was hypothesized that production of 3MH would be able to mask the worty off- flavors associated with arrested fermentation with MN yeast strains. However, it was previously observed that very high levels of expression of an enzyme having CSL activity were necessary to impart guava / passionfruit flavors in beer and it was not clear whether MN strains engineered to express an enzyme having CSL activity would be able to do so at a sufficient level during the limited fermentation of an arrested fermentation to produce adequate levels of 3MH to mask the worty off-flavors and aromas. In addition, 3MH contains a thiol moiety which makes this molecule highly reactive, especially with aldehydes. Arrested fermentation non-alcoholic beers may contain higher concentrations of free aldehydes than alcoholic beers, and any 3MH produced may be unstable and readily bind with these aldehydes, which would make it flavor-inactive. The total concentrations of aldehydes in arrested fermentation non-alcoholic beers far exceeds the 2 - 10 ug / L of 3MH that results from CSL expression11, and the binding of 3MH to aldehydes cannot meaningfully reduce the concentrations of worty aldehydes. In an effort to determine whether 3MH production during AF is a viable strategy to mask worty aroma, the maltose-negative BY632 strain was engineered to express CSL, resulting in strain BY1502. In 20 L beer fermentations with BY1502, it was observed that the concentration of 3MH in the finished beer was 4 µg / L, whereas the 3MH concentration in BY632 beer was below the detection limit of 50 ng / L. Attenuation in the fermentation with strain BY1502 was 18.4%. Sensory analysis of the resulting beer noted moderate levels of desirable guava / passionfruit flavors and that worty flavors were reduced in intensity relative to BY632, but not absent. In an experiment where the kegged beer produced by strain BY1502 was stored at 4˚C and sampled at weekly intervals over the course of 6 weeks, it was observed that the guava / passionfruit aroma and flavor in the beer remained constant over time, and that the intensity of worty flavors did not meaningfully increase over time. In conclusion, yeast engineered to produce 3MH have the ability to partially mask worty beer flavors without creating any off-flavors that detract from the quality of beer. Engineering BY632 for biosynthesis of linalool, geraniol, and citronellol To further evaluate production of additional flavor molecule to reduce sensory detection of undesired wort-associated off-flavors the maltose-negative strain BY632 was engineered for the biosynthesis of three terpene molecules: linalool, geraniol, and citronellol. These three molecules are found in certain hop varieties and in beers dry-hopped with these hops. In beer, these terpenes impart flavors and aromas that are primarily floral and also citrus, but at high concentrations, unpleasantly soapy. Brewing yeast used in typical alcoholic fermentations have been engineered for the biosynthesis of these three compounds (Denby, C. M. et al. Industrial brewing yeast engineered for the production of primary flavor determinants in hopped beer. Nat. Commun.9, 965 (2018)). Terpenes can be poorly soluble in water. In alcoholic beer this does not present a major issue, as the amphiphilic properties of ethanol facilitate dissolution of hydrophobic terpenes. In non-alcoholic beer however, the low ethanol content makes it more difficult to fully dissolve terpenes (see, US Publication No.2013 / 0280399A1). Brewers have also independently reported issues with the low solubility of terpenes in non-alcoholic beer and that the extraction of hop terpenes in non-alcoholic beer fermentations is less efficient than it is in alcoholic fermentations. In an effort to engineer the maltose-negative strain BY632 for the biosynthesis of linalool, geraniol and citronellol, the following were expressed: 1) a truncated variant of a yeast HMG1 enzyme that catalyzes the rate limiting step in ergosterol biosynthesis; 2) a mutational variant of the yeast ERG20 enzyme that increases formation of the terpene precursor molecule, GPP; 3) a linalool synthase enzyme, McLIS, derived from Mentha citrata (mint); and 4) a geraniol synthase enzyme, ObGES, derived from Ocimum basilicum (basil). Citronellol production in these strains is catalyzed by the endogenous yeast NADPH oxidoreductase enzyme, OYE2, which reduces a portion of the geraniol produced by ObGES into citronellol (Yuan, T.-T. et al. Identification of enzymes responsible for the reduction of geraniol to citronellol. Nat. Products Bioprospect.1, 108 (2011)), resulting in engineered strain BY1505. Each of strains BY1505, BY632, and wild-type S. cerevisiae Chico were used in 20 L beer fermentations and the levels of linalool, geraniol, and citronellol were assessed by gas chromatography-mass spectrometry. As shown in Table 2, beer produced with the BY1505 strain was found to contain higher levels of linalool, geraniol, and citronellol than beer brewed with either BY632 or Chico (Table 2). Table 2. Characteristics of beers produced with wild-type S. cerevisiae Chico, BY632, and BY1505 strains. Levels of linalool, citronellol, and geraniol are reported as GC-MS peak areas. N.D.; Not Detected.

[0003] In sensory analysis by a panel of taste testers, beer fermented with the BY1505 strain was found to contain moderate levels of floral and citrus aroma and flavor notes, which were generally considered to be desirable (Table 2). The presence of these aromas and flavors also substantially reduced the intensity of worty aromas and flavors in this beer as compared to beer fermented with the BY632 strain. In a blinded comparison of the 0.5% ABV beers brewed with BY632, or BY1505 strains or wild-type S. cerevisiae Chico, (~2.5% ABV), the tasting panel rated the beer produced with the BY1505 strain as significantly superior to beer produced with the BY632 strain (p=.008), and nominally superior to even the 2.5% ABV beer brewed with the maltose positive wild-type S. cerevisiae Chico strain (FIG.4). From these data, it is concluded that maltose-negative strains engineered for the biosynthesis of linalool, geraniol and citronellol can substantially reduce the intensity or worty flavors in arrested fermentation non-alcoholic beer without imparting additional off-flavors. Example 3: Yeast Production of Isoamyl Acetate Versus Wort-associated Sensory Attributes A sensory analysis by a panel of taste testers for beers fermented with eight NA beers produced with different levels of isoamyl acetate was performed. A summary of the strains, resulting beer properties and sensory panel assessments from Examples 3 and 4 is provided in Table 3 below. As shown in FIGS.5A-5C, beers with increased concentrations of isoamyl acetate, phenethyl acetate and ethyl acetate are perceived as having reduced levels of undesirable wort-associated sensory attributes. The same trend is observed for all three acetate esters. As shown in FIGS.6A-6C, beers with increased concentrations of isoamyl acetate, phenethyl acetate and ethyl acetate are perceived as having increased levels of undesirable banana and solvent sensory attributes. The same trend is observed for all three acetate esters. *Promoter TPMs refers to the mean transcript per million associated with the indicated promoter during the first 4 days of beer fermentation, as measured by RNA-seq. BY1574, BY1503 and BY1573 shown in Table 3 were found to have desirable ranges for isoamyl acetate, phenethyl acetate, and ethyl acetate. Example 4: Ranked Preference for NA Beers Produced by Different Yeast Strains Five of the beers that were assessed in Example 3, were also compared in a ranked preference test. A summary of the strains and their isoamyl acetate and phenethyl acetate production (levels in the beer) is provided in Table 4 below and summarized in FIG.7. Table 4. As shown in FIG.7, the mean and median preference ranks of beer made with y1574, y1503, and y1573 were higher than beers made with y632 or y1503. Based on these data, a desirable range for isoamyl acetate in NA beers exists between 9.2 µg / L (its concentration in BY632), and 4310 µg / L (its concentration in BY1504). Similarly, a desirable range for phenethyl acetate in NA beers made with MN strains exists between 2.4 µg / L and 1010 µg / L. These data demonstrate that there is an intermediate concentration range for each of isoamyl acetate and phenethyl acetate that is high enough to mask worty off-flavors but also low enough to not impart banana or solvent off-flavors. Example 5 : Modeling a Preferred Range of Acetate Esters The data from ranked preference studies was used to develop models that identify preferred concentration ranges for acetate esters in NA beer with greater specificity. FIG.8 shows the models and Table 5 below provides the preferred desired ranges. In FIG.8, the preferences of the sensory panel for the beer produced by each of the indicated strains is plotted as a function of the concentration of either isoamyl acetate (A), ethyl acetate (B), or phenethyl acetate (C) in that beer. Table 5. SEQUENCE LISTING

[0004] References 27. Wang, X., Bali, M., Medintz, I. & Michels, C. A. Intracellular Maltose Is Sufficient To Induce MAL Gene Expression in Saccharomyces cerevisiae. Eukaryot. Cell 1, 696 (2002). 28. Brickwedde, A. et al. Structural, Physiological and Regulatory Analysis of Maltose Transporter Genes in Saccharomyces eubayanus CBS 12357T. Front. Microbiol.9, (2018). 29. The Oxford Companion to Beer Definition of Plato gravity scale. Craft Beer & Brewing beerandbrewing.com / dictionary / NpUFIRRVLp / . 35. Jean-Alexandre Bureau, Oliva, M. E., Dong, Y. & Ignea, C. Engineering yeast for the production of plant terpenoids using synthetic biology approaches. Nat. Prod. Rep. (2023) doi:10.1039 / D3NP00005B. 36. Hazelwood, L. A., Daran, J.-M., van Maris, A. J. A., Pronk, J. T. & Richard Dickinson, J. The Ehrlich Pathway for Fusel Alcohol Production: a Century of Research on Saccharomyces cerevisiae Metabolism. Appl. Environ. Microbiol.74, 2259 (2008).

Claims

CLAIMS What is claimed is:

1. A genetically modified yeast cell incapable of or having a reduced capability of converting maltose and / or maltotriose to ethanol, comprising a heterologous nucleic acid encoding an enzyme having alcohol acyltransferase (EC 2.3.1.84) activity.

2. The genetically modified yeast cell of claim 1, wherein the cell produces an increased amount of one or more acetate esters and / or ethyl esters compared to a cell that does not comprise the heterologous nucleic acid.

3. The genetically modified yeast cell of claim 2, wherein the acetate ester is selected from the group consisting of ethyl acetate, isoamyl acetate, and phenethyl acetate.

4. The genetically modified yeast cell of claim 2, wherein the ethyl ester is selected from the group consisting of ethyl hexanoate, ethyl octanoate, and ethyl decanoate.

5. The genetically modified yeast cell of any one of claims 1-4, further comprising a heterologous nucleic acid encoding an enzyme having carbon-sulfur-lyase (EC 4.4) activity.

6. The genetically modified yeast cell of claim 5, wherein the enzyme having carbon- sulfur-lyase activity comprises a sequence having at least 90% sequence identity to any one of SEQ ID NO: 9 and 57-62.

7. The genetically modified yeast cell of claim 5, wherein the enzyme having carbon- sulfur-lyase activity comprises a sequence having at least 90% sequence identity to SEQ ID NO:

9.

8. The genetically modified yeast cell of any one of claims 1-7, further genetically modified to produce one or more monoterpenes.

9. The genetically modified yeast cell of claim 8, wherein the monoterpene is selected from the group consisting of linalool, geraniol, and citronellol.

10. The genetically modified yeast cell of any one of claims 8-9, wherein the genetically modified yeast cell comprises a heterologous nucleic acid encoding an enzyme selected from the group consisting of: (a) a truncated variant of a yeast HMG1 enzyme; (b) a variant of a ERG20 enzyme; (c) a linalool synthase; (d) a geraniol synthase; and (e) combinations thereof.

11. The genetically modified yeast cell of claim 10, wherein the truncated variant of a yeast HMG1 enzyme comprises a sequence having at last 90% sequence identity to SEQ ID NO:

11.

12. The genetically modified yeast cell of claim 10, wherein the variant of a ERG20 enzyme comprises a sequence having at least 90% sequence identity to SEQ ID NO:

13.

13. The genetically modified yeast cell of claim 10, wherein the linalool synthase comprises a sequence having at least 90% sequence identity to any one of SEQ ID NOs: 15 and 63-68.

14. The genetically modified yeast cell of claim 10, wherein the linalool synthase comprises a sequence having at least 90% sequence identity to SEQ ID NO:

15.

15. The genetically modified yeast cell of claim 10, wherein the geraniol synthase comprises a sequence having at least 90% sequence identity to any one of SEQ ID NOs: 17 and 69-71.

16. The genetically modified yeast cell of claim 10, wherein the geraniol synthase comprises a sequence having at least 90% sequence identity to SEQ ID NO:

17.

17. The genetically modified yeast cell of any one of claims 10-16, wherein the genetically modified yeast cell comprises a heterologous nucleic acid encoding: (a) the truncated variant of a yeast HMG1 enzyme; (b) the variant of a ERG20 enzyme;(c) the linalool synthase; and (d) the geraniol synthase.

18. The genetically modified yeast cell of any one of claims 1-17, wherein the genetically modified yeast cell is incapable of or has a reduced capability of converting maltose and / or maltotriose to ethanol due to one or more genetic modifications that functionally disrupt one or more enzymes associated with maltose and / or maltotriose transport and / or maltose and / or maltotriose hydrolysis.

19. The genetically modified yeast cell of claim 18, wherein the genetically modified yeast cell comprises one or more modification that functionally disrupt a maltose and / or maltotriose transporter.

20. The genetically modified yeast cell of claim 18, wherein the modified cell comprises one or more modifications that functionally disrupt MAL31 and / or MAL11 (AGT1).

21. The genetically modified yeast cell of claim 18, wherein the modified cell comprises one or more modifications that functionally disrupt MAL31 and / or MAL11 (AGT1).

22. The genetically modified yeast cell of any one of claims 1-21, wherein the modified cell is capable of converting glucose to ethanol.

23. The genetically modified yeast cell of any one of claims 1-22, wherein the heterologous nucleic acid comprises a gene encoding the enzyme having alcohol acyltransferase activity operably linked to a promoter selected from the group consisting of SEQ ID NOs: 19-35 and 72-73.

24. The genetically modified yeast cell of claim 23, wherein the heterologous nucleic acid comprises a gene encoding the enzyme having alcohol acyltransferase activity operably linked to a promoter selected from the group consisting of pSPG1 (SEQ ID NO: 26), pHSP26 (SEQ ID NO: 20), pANT1 (SEQ ID NO: 34), pPEX11 (SEQ ID NO: 35), and pALD6 (SEQ ID NO: 73).

25. The genetically modified yeast cell of claim 23, wherein the enzyme having alcohol acyltransferase activity comprises a sequence having at least 90% sequence identity to any one of SEQ ID NOs: 5, 7 and 36-56.

26. The genetically modified yeast cell of claim 23, wherein the enzyme having alcohol acyltransferase activity comprises a sequence having at least 90% sequence identity to SEQ ID NO: 5 or SEQ ID NO:

7.

27. The genetically modified yeast cell of claim 23, wherein the enzyme having alcohol acyltransferase activity comprises a sequence having at least 90% sequence identity to SEQ ID NO:

5.

28. The genetically modified yeast cell of claim 23, wherein the enzyme having alcohol acyltransferase activity comprises a sequence having at least 90% sequence identity to SEQ ID NO:

7.

29. A liquid fermentation composition comprising: (a) a population of genetically modified yeast cells that are genetically modified to produce one or more acetate esters and / or ethyl esters, wherein yeast cells are incapable of or having a reduced capability of converting maltose and / or maltotriose to ethanol; (b) a sugar source comprising wort, wherein total sugar in the wort has been attenuated by no more than 25% by the population of genetically modified yeast cells; (c) one or more wort-derived aldehydic and / or non-aldehyde molecules; and (d) no more than 1.0% (v / v) alcohol.

30. The liquid fermentation composition of claim 29, wherein the liquid fermentation composition comprises isoamyl acetate, ethyl acetate and phenethyl acetate in a total amount of from about 500 µg / L to about 5500 µg / L, preferably from about 536.2 µg / L to about 4725.4 µg / L.

31. The liquid fermentation composition of claim 29, comprising isoamyl acetate and phenethyl acetate in an amount from about 10 µg / L to about 1500 µg / L, preferably from about 11.4 µg / L to about 1094.7 µg / L.

32. The liquid fermentation composition of claim 29, comprising isoamyl acetate in an amount from about 9.1 µg / L to about 900 µg / L, preferably from about 9.1 µg / L to about 812.8 µg / L, and / or phenethyl acetate in an amount from about 2.3 µg / L to about 500 µg / L, preferably from about 2.3 µg / L to about 281.8 µg / L.

33. The liquid fermentation composition of any one of claims 29-32, wherein the population of yeast cells comprise the genetically modified yeast cell of any one of claims 1- 28.

34. The liquid fermentation composition of any one of claims 29-33, wherein the aldehydric molecule is selected from the group consisting of 2-methylbutanal, 2- methylpropanal, hexanal, benzaldehyde, furfural, acetaldehyde, methional, phenylacetaldehyde, and 5-hydrox-methyl-furfural.

35. The liquid fermentation composition of any one of claims 29-34, wherein the non- aldehyde molecule is selected from the group consisting of (E)-beta-damascenone and 5- ethyl-3-hydroxy-4-methyl-2(5H)-furanone.

36. A liquid fermentation composition comprising: (a) a population of genetically modified yeast cells that are genetically modified to be incapable of or having a reduced capability of converting maltose and / or maltotriose to ethanol; (b) a sugar source comprising wort, wherein total sugar in the wort has been attenuated by no more than 25% by the population of genetically modified yeast cells; and (c) no more than 1.0% (v / v) alcohol.

37. The liquid fermentation composition of claim 36, wherein the genetically modified yeast cells are incapable of converting maltose and / or maltotriose to ethanol due to one or more genetic modifications that functionally disrupt one or more enzymes associated with maltose and / or maltotriose transport, and / or maltose and / or maltotriose hydrolysis.

38. The liquid fermentation composition of claim 37, wherein the population of yeast cells comprise one or more genetic modifications that functionally disrupt a maltose and / or maltotriose transporter.

39. The liquid fermentation composition of claim 37, wherein the population of yeast cells comprise one or more genetic modifications that functionally disrupt MAL31 and / or MAL11 (AGT1).

40. A method of producing a fermented beverage comprising: (a) providing a genetically modified yeast cell comprising a functional disruption in one or more enzymes associated with maltose and / or maltotriose transport, and / or maltose and / or maltotriose hydrolysis in the yeast cell, wherein the functional disruption(s) result in reduced growth of the yeast cell on maltose as a sole sugar source compared to a yeast cell not comprising the genetic modification; (b) providing a medium comprising a wort-derived sugar source; (c) combining the genetically modified yeast cell and the medium to form a fermentation composition; and (d) allowing the fermentation composition to ferment to produce a fermented beverage.

41. The method of claim 40, wherein the genetically modified yeast cell comprises one or more genetic modification that functionally disrupt a maltose and / or maltotriose transporter.

42. The method of claim 40, wherein the genetically modified yeast cell comprises one or more genetic modifications that functionally disrupt MAL31 and / or MAL11 (AGT1).

43. A method of producing a fermented beverage, comprising contacting a population of the genetically modified yeast cell of any one of claims 1-28 with a medium comprising a wort-derived sugar source during a fermentation process to produce the fermented beverage.

44. The method of any one of claims 40-43, wherein the fermented beverage is a reduced alcohol fermented beverage.

45. The method of any one of claims 40-44, wherein the fermented beverage has an alocohol content of less than or equal to about 0.5% (v / v) alcohol.

46. The method of any one of claims 40-45, wherein the method does not include a step of physically removing alcohol from the beverage or prematurely halting fermentation.

47. The method of any one of claims 40-46, wherein at least one fermentable sugar is provided in the wort-derived sugar source.

48. The method of any one of claims 40-47, wherein the fermentation process results in a reduction in the level of wort-derived sugar by at least 15% but no more than 25%.

49. The method of any one of claims 40-48, wherein the fermented beverage is beer.

50. The method of any one of claims 40-49, wherein the fermented beverage comprises isoamyl acetate, ethyl acetate, and phenethyl acetate in a total amount of from about 500 µg / L to about 6500 µg / L, preferably from about 536.2 µg / L to about 4725.4 µg / L.

51. The method of any one of claims 40-49, wherein the fermented beverage comprises isoamyl acetate and phenethyl acetate in an amount from about 10 µg / L to about 1500 µg / L 52. The method of any one of claims 40-49, wherein the fermented beverage comprises isoamyl acetate in an amount from about 9 µg / L to about 900 µg / L, preferably from about 9.1 µg / L to about 812.8 µg / L, and / or phenethyl acetate in an amount from about 2.3 µg / L to about 500 µg / L, preferably from about 2.3 µg / L to about 281.8 µg / L.

53. The method of any one of claims 40-52, further comprising producing the medium, wherein producing the medium comprises: (a) contacting a plurality of grains with water; and (b) boiling or steeping the water and grains to produce wort.

54. The method of claim 53, further comprising adding at least one hop variety to the wort to produce hopped wort.

55. The method of any one of claims 40-54, further comprising adding at least one hop variety to the medium.

56. The genetically modified yeast cell of any one of claims 1-28, the liquid fermentation composition of any one of claims 29-39, or the method of any one of claims 40-55, wherein the yeast cell is of the genus Saccharomyces.

57. The genetically modified yeast cell of any one of claims 1-28, the liquid fermentation composition of any one of claims 29-39, or the method of any one of claims 40-55, wherein the yeast cell is of the species Saccharomyces cerevisiae (S. cerevisiae).

58. The genetically modified yeast cell of any one of claims 1-28, the liquid fermentation composition of any one of claims 29-39, or the method of any one of claims 40-55, wherein the yeast cell is S. cerevisiae Chico Ale yeast, London Ale yeast, Andechs Lager yeast, Augustiner Lager yeast, or American Ale yeast.

59. A genetically modified yeast cell (modified cell) comprising one or more genetic modifications to reduce sensory detection of one or more wort- associated off-flavors of a fermented beverage; wherein the modified cell is not capable of converting maltose and / or maltotriose to ethanol.

60. The genetically modified cell of claim 59, wherein the wort-associated off-flavors comprise aldehydic and / or non-aldehyde molecules.

61. The genetically modified cell of claim 60, (a) wherein the aldehydic molecule is 2- methylbutanal, 2-methylpropanal, hexanal, benzaldehyde, furfural, acetaldehyde, methional, phenylacetaldehyde, or 5-hydrox-methyl-furfural, and / or (b) wherein the non-aldehyde molecule is (E)-beta-damascenone or 5-ethyl-3-hydroxy-4-methyl-2(5H)-furanone.

62. The genetically modified cell of any one of claims 59-61, wherein the modified cell is capable of converting glucose to ethanol.

63. The genetically modified cell of any one of claims 59-61, wherein the modified cell comprises one or more genetic modifications that functionally disrupt one or more proteins associated with maltose and / or maltotriose transport into the modified cell and / or maltose and / or maltotriose hydrolysis by the modified cell.

64. The genetically modified cell of claim 63, wherein the modified cell comprises one or more genetic modifications that functionally disrupt a maltose and / or maltotriose transporter.

65. The genetically modified cell of claim 64, wherein the modified cell comprises one or more genetic modifications that functionally disrupt MAL31 and MAL11 (AGT1).

66. The genetically modified cell of any one of claims 59-65, wherein the one or more genetic modifications to reduce sensory detection of one or more wort-associated off-flavors results in increased production of one or more acetate esters and / or ethyl esters as compared to a cell that does not comprise the genetic modification(s).

67. The genetically modified cell of claim 66, wherein the acetate ester is ethyl acetate, isoamyl acetate, and / or phenethyl acetate.

68. The genetically modified cell of claim 66, wherein the ethyl ester is ethyl hexanoate, ethyl octanoate, and / or ethyl decanoate.

69. The genetically modified cell of any one of claims 66-68, wherein the one or more genetic modifications that increases production of one or more acetate esters and / or ethyl esters comprises overexpression of an enzyme having alcohol acyltransferase (AAT) activity.

70. The genetically modified cell of claim 69, wherein the enzyme having AAT activity comprises a sequence set forth in SEQ ID NO:

5.

71. The genetically modified cell of any one of claims 66-68, wherein the one or more genetic modifications that increases production of one or more acetate esters and / or ethyl esters comprises expression of a heterologous enzyme having alcohol acyltransferase (AAT) activity.

72. The genetically modified cell of claim 71, wherein the heterologous enzyme having AAT activity comprises a sequence set forth in SEQ ID NO: 7.

73. The genetically modified cell of any one of claims 59-65, wherein the one or more genetic modifications to reduce sensory detection of one or more wort-associated off-flavors results in increased production of 3-mercaptohexanol (3MH).

74. The genetically modified cell of claim 73, wherein the one or more genetic modifications that increases production of 3MH comprises expression of a bacterial enzyme having carbon-sulfur-lyase (CSL) activity.

75. The genetically modified cell of claim 74, wherein the bacterial enzyme having CSL activity comprises a sequence set forth in SEQ ID NO:

9.

76. The genetically modified cell of any one of claims 59-65, wherein the one or more genetic modifications to reduce sensory detection of one or more wort-associated off-flavors results in increased production of one or more monoterpene.

77. The genetically modified cell of claim 76, wherein the monoterpene is linalool, geraniol, and / or citronellol.

78. The genetically modified cell of claim 76 or 77, wherein the one or more genetic modifications that increases production of one or more monoterpenes comprises expression of one or more of: (a) a truncated variant of a yeast HMG1 enzyme; (b) a variant of a ERG20 enzyme; (c) a linalool synthase; and / or (d) a geraniol synthase.

79. The genetically modified cell of claim 78, wherein the truncated variant of a yeast HMG1 enzyme comprises a sequence set forth in SEQ ID NO:

11.

80. The genetically modified cell of claim 78 or 79, wherein the variant of ERG20 enzyme comprises a sequence set forth in SEQ ID NO:

13.

81. The genetically modified cell of any one of claims 78-80, wherein the linalool synthase comprises a sequence set forth in SEQ ID NO: 14.

82. The genetically modified cell of any one of claims 78-81, wherein the geraniol synthase comprises a sequence set forth in SEQ ID NO:

16.

83. The genetically modified cell of any one of claims 59-82, wherein the yeast cell is of the genus Saccharomyces.

84. The genetically modified cell of claim 83, wherein the yeast cell is of the species Saccharomyces cerevisiae (S. cerevisiae).

85. The genetically modified cell of claim 84, wherein the yeast cell is S. cerevisiae Chico Ale yeast, London Ale yeast, Andechs Lager yeast, Augustiner Lager yeast, or American Ale yeast.

86. A method of producing a fermented beverage, contacting the modified cell of any one of claims 59-85 with a medium comprising at least one fermentable sugar, wherein the contacting is performed during at least a first fermentation process, to produce a fermented beverage.

87. The method of claim 86, wherein the fermented beverage is a reduced alcohol fermented beverage.

88. The method of claim 86 or 87, wherein the fermented beverage has an alcohol content of less than 0.5% (v / v) alcohol.

89. The method of any one of claims 86-88, wherein the method does not include a step of physically removing alcohol from the beverage or prematurely halting fermentation.

90. The method of any one of claims 86-89, wherein at least one fermentable sugar is provided in at least one sugar source.

91. The method of claim 90, wherein the fermentable sugar is glucose, fructose, and / or sucrose.

92. The method of any one of claims 86-91, wherein the first fermentation process results in a reduction in the level of the fermentable sugar by at least 15%.

93. The method of any one of claims 86-92, wherein the fermented beverage is beer.

94. The method of any one of claims 86-93, wherein the sugar source comprises wort.

95. The method of claim 94, wherein the sugar source is wort and the method further comprises producing the medium, wherein producing the medium comprises: (a) contacting a plurality of grains with water; and (b) boiling or steeping the water and grains to produce wort.

96. The method of claim 95, further comprising adding at least one hop variety to the wort to produce a hopped wort.

97. The method of any one of claims 86-96, further comprising adding at least one hop variety to the medium.

98. The method of any one of claims 86-97, further comprising at least one additional fermentation process.

99. The method of any one of claims 86-98, further comprising carbonating the fermented product.

100. A genetically modified brewing yeast cell (modified cell) comprising one or more genetic modifications to functionally disrupt maltose / maltotriose transporters MAL31 and MAL11 (AGT1).

101. A fermented beverage produced by the method of any one of claims 40-58.

102. A fermented beverage comprises alcohol in an amount of no more than 1.0% (v / v) and nucleic acids from the genetically modified yeast cell of any one of claims 1-28.

103. The fermented beverage of claim 102, wherein the fermented beverage comprises alcohol in an amount of no more than 0.5% (v / v).

104. The genetically modified yeast cell of any one of claims 1-28 or 56-85; the liquid fermentation composition of any one of claims 29-39; or the method of any one of claims 40- 55 and 86-99, wherein the yeast cell is a brewing yeast cell.

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