Systems and methods for producing 2,5-furandicarboxylic acid

Abstract

A method for the production of 2,5-furandicarboxylic acid (FDCA) comprising contacting glucose with a catalyst composition under conditions suitable for the formation of glucarate; acidifying glucarate to form glucaric acid; dehydrating glucaric acid to form FDCA; and recovering FDCA. A method for the production of 2,5-furan dicarboxylic acid dimethyl ester (FDME) comprising contacting glucose with a catalyst composition under conditions suitable for the formation of glycolaldehyde; contacting glycolaldehyde with a transition metal oxidation catalyst under conditions suitable for the formation of glucaric acid; esterifying glucaric acid to form glucaric acid methyl ester; dehydrating the glucaric acid methyl ester to form FDME; and recovering FDME.

Description

SYSTEMS AND METHODS FOR PRODUCING 2,5-FURANDICARBOXYLIC ACIDCROSS-REFERENCE TO RELATED APPLICATIONS

[0001] This application claims benefit and priority of U.S. provisional patent application Serial No 63 / 671 ,395 filed July 15, 2024, and entitled “SYSTEMS AND METHODS FOR PRODUCING 2,5-FURAN DICARBOXYLIC ACID AND 2,5-FURAN DICARBOXYLIC ACID DIMETHYL ESTER,” which is hereby incorporated herein by reference in its entirety for all purposes.STATEMENT REGARDING FEDERALLY SPONSORED RESEARCH OR DEVELOPMENT

[0002] Not applicable.REFERENCE TO SEQUENCE LISTING

[0003] The instant application contains a Sequence Listing which has been submitted electronically in XML file format and is hereby incorporated by reference in its entirety. Said XML file, created on July 10, 2025 is named “3416-07104 CHEMOENZYMATIC SYNTHESIS OF FDCA.xml” and is 5,488 bytes in size.TECHNICAL FIELD

[0004] The present disclosure relates generally to the production of higher value chemicals. More particularly, the present disclosure relates generally to higher value chemicals derived from sugar oxidation products. Still more particularly, the present disclosure relates to novel methods for the production of 2,5-furandicarboxylic acid and derivatives thereof.BACKGROUND

[0005] With sustainability being a desired goal, tremendous progress in bio-based production routes from renewable raw materials to commercial goods continues to occur. Of particular interest is the formation of higher value chemicals from what are termed “platform molecules.” Herein platform molecules refer to bio-based or bioderived chemicals whose constituting elements totally originated from biomass and could be used as building blocks forthe generation of commodity and refined chemicals.

[0006] 2,5-Furandicarboxylic Acid (FDCA) (or its chemical cousin 2,5-furan dicarboxylic acid dimethyl ester (FDME)) has been identified by the US Department of Energy (DOE) as one of the top 12 value-added chemicals that can be considered as a replacementfor several fossil fuel-derived chemicals. FDCA is a biobased organic molecule consisting of two carboxylic acid groups bonded to a central furan ring. FDCA has a higher melting point of 342 °C, which makes it thermally stable and suitable for polymeric applications. Indeed, FDCA can replace petroleum-based terephthalic acid for the production of biobased plastic polyethylene furandicarboxylate (PEF) due to the similarity in its functional group with terephthalic acid.

[0007] An ongoing need exists for novel methods and compositions for the production of FDCA.BRIEF SUMMARY OF THE DISCLOSURE

[0008] Disclosed herein is a method for the production of 2,5-furandicarboxylic acid (FDCA) comprising contacting glucose with a catalyst composition under conditions suitable for the formation of glucarate; acidifying glucarate to form glucaric acid; dehydrating glucaric acid to form FDCA; and recovering FDCA.

[0009] Also disclosed herein is a method for the production of 2,5-furan dicarboxylic acid dimethyl ester (FDME) comprising contacting glucose with a catalyst composition under conditions suitable for the formation of glycolaldehyde; contacting glycolaldehyde with a transition metal oxidation catalyst under conditions suitable for the formation of glucaric acid; esterifying glucaric acid to form glucaric acid methyl ester; dehydrating the glucaric acid methyl ester to form FDME; and recovering FDME.

[0010] Aspects described herein comprise a combination of features and characteristics intended to address various shortcomings associated with certain prior devices, systems, and methods. The foregoing has outlined rather broadly the features and technical characteristics of the disclosed aspects in order that the detailed description that follows may be better understood. The various characteristics and features described above, as well as others, will be readily apparent to those skilled in the art upon reading the following detailed description, and by referring to the accompanying drawings. It should be appreciated that the conception and the specific aspects disclosed may be readily utilized as a basis for modifying or designing other structures for carrying out the same purposes as the disclosed aspects. It should also be realized that such equivalent constructions do not depart from the spirit and scope of the principles disclosed herein.BRIEF DESCRIPTION OF THE DRAWINGS

[0011] For a detailed description of various exemplary aspects, reference will now be made to the accompanying drawings in which:

[0012] Figure 1 depicts the chemical structure of (A) FDCA and (B) FDME.

[0013] Figure 2 depicts schematically the reaction for conversion of biomass to FDCA.

[0014] Figure 3 depicts a process flow diagram providing a general overview for the formation of FDCA from glucose in an aspect of the present disclosure.

[0015] Figure 4 depicts a process flow diagram providing a detailed overview for the formation of FDCA from glucose in an aspect of the present disclosure.

[0016] Figure 5 depicts a process flow diagram providing a general overview for the formation of FDME from glucose in an aspect of the present disclosure.

[0017] Figure 6 depicts a process flow diagram providing a a detailed overview for the formation of FDME from glucose in an aspect of the present disclosure.DETAILED DESCRIPTION

[0018] The following discussion is directed to various exemplary aspects. However, one of ordinary skill in the art will understand that the examples disclosed herein have broad application, and that the discussion of any aspect is meant only to be exemplary of that aspect, and not intended to suggest that the scope of the disclosure, including the claims, is limited to that aspect.

[0019] The figures are not necessarily to scale. Certain features and components herein may be shown exaggerated in scale or in somewhat schematic form and some details of conventional elements may not be shown in interest of clarity and conciseness.

[0020] In the following discussion and in the claims, the terms “including” and “comprising” are used in an open-ended fashion, and thus should be interpreted to mean “including, but not limited to... .” As used herein, the terms “approximately,” “about,” “substantially,” and the like mean within 10% (i.e., plus or minus 10%) of the recited value. Thus, for example, a recited angle of “about 80 degrees” refers to an angle ranging from 72 degrees to 88 degrees.

[0021] Disclosed herein are compositions and methods for the production of FDCA, FDME and derivatives thereof. The chemical structures of FDCA and FDME are depicted in Figure 1 as A and B, respectively. In one or more aspects, a method of the present disclosure comprises the conversion of glucose, obtained from biomass to an oxidized glucose product which is converted to FDCA as depicted in Figure 2. Also disclosed herein are methods and compositions for production of chemicals through agreen and cost-efficient pathway. More particularly, disclosed herein are methods for the production of FDCA, FDME and derivatives thereof. The present disclosure of methods and compositions provide even more green routes and pathways to replace compounds sourced from petrochemicals.

[0022] In one or more aspects, a method of the present disclosure comprises the conversion of glucose to FDCA which is diagrammed in Figure 3. With reference to Figure 3, a method of the present disclosure 100 comprises contacting (a) one or more biocatalysts such as enzymes; (b) a sugar such as glucose; and (c) an oxidizing agent under conditions suitable for the oxidation of glucose. Contacting may be carried out in an Enzyme Oxidation Reactor (EOR) 110 whose product mixture may be conveyed to one or more processes for separation (i.e., separation sequence 120). The separated product mixture may be further processed by reactive distillation 130 whose products are then subjected to purification 140 resulting in the formation of FDCA crystals.

[0023] In an alternative aspect, depicted in Figure 4 is a process flow diagram for the production of FDCA from a sugar such as glucose, 200. In an aspect, enzymes 201 and glucose 202 are contacted in the presence of an oxidizing agent (e.g., air) in an Enzyme Oxidation Reactor 210 under conditions suitable for the oxidation of glucose. Air may be supplied to the EOR 210 via one or more air compressors 204 and 205. A pH adjusting agent such as a hydroxide (e.g., sodium hydroxide) 203 may be introduced to the EOR 210 to adjust the pH of the reaction as needed. The EOR 210 may be a pressure vessel where air is sparged from the bottom, which serves to both provide oxygen for reactions and to mix the tank. This reaction is mildly exothermic and heat may be actively removed to ensure enzyme stability. In order to retain enzyme, the product mixture may be passed through a filtration unit such as a Tangential Flow Filtration (TFF) ultrafilter 215 to separate and recycle the enzyme.

[0024] The product mixture exiting the TFF 215 is an enzyme free permeate comprising glucose oxidation products. In one or more aspects, the product mixture exiting the EOR 210 may comprise glucose oxidation products at yields that can range from about 50% to about 99%, additionally or alternatively, from about 50% to about 90%, additionally or alternatively, from about 50% to about 80%, additionally or alternatively, at least about 55%, at least about 58%, at least about 60%, at least about 62%, at least about 64%, at least about 66%, at least about 68%, at least about 70%, at least about 72%, at least about 74%, at least about 76%, at least about 78%, at least about 80%, at least about 82%, at least about 84%, at least about 86%, at least about 88%, at least about 90%,at least about 92%, at least about 94%, at least about 96%, at least about 98%, at least about or at least about 99%.

[0025] In one or more aspects, the product mixture comprises glucarate; for example, the product mixture may comprise from about 5 weight percent (wt.%) to about 40 wt.% glucarate; additionally or alternatively from about 10 wt.% to about 30 wt.% glucarate; additionally or alternatively from about 15 wt.% to about 25 wt.%; additionally or alternatively about 20 wt.% sodium 5,4-glucarate. Hereinafter, the disclosure will refer to sodium 5,4-glucarate as the oxidation product that is carried forward in the reaction process. In one or more aspects, sodium 5,4-glucarate in water, may be further processed while enzyme rich retentate is recycled back to the EOR 210. In one or more aspects, sodium 5,4-glucarate is then passed to a flash unit 220 for concentration. The flash unit 220 may be a flash drum, falling film heat exchanger, wiped film evaporator, or mechanical vapor recompressor. In one or more aspects, the flash unit 220 operates under rough vacuum (e.g., 2 pounds per square inch absolute (psia) to about 8 psia) with water removed to concentrate sodium 5,4-glucarate up to an amount of about 50 wt.%. Any flash unit disclosed herein may have characteristics similar or identical to those disclosed for flash unit 220.

[0026] It is to be understood that other glucose oxidation products may be formed and processes may be utilized by the ordinarily skilled artisan to separate, purify and / or concentrate any other products. In one or more aspects, the sodium 5,4-glucarate leaving the flash unit 220 has a relatively high concentration, but poor overall purity due to (i) the presence of non-dextrose sugars in the dextrose feed and (ii) side reactions in the enzyme reactors.

[0027] In one or more aspects, a Sequential Simulated Moving Bed (SSMB) chromatography separations unit 230 can be employed to purify the sodium 5,4- glucarate, with water added as eluent. The resulting material may be characterized as having a purity of equal to or greater than about 80%; additionally or alternatively equal to or greater than about 90%; additionally or alternatively equal to or greater than about 95%; additionally or alternatively equal to or greater than about 98%. In some aspects, the sodium 5,4-glucarate in water stream leaves the SSMB 230 as a dilute glucarate solution (e.g., about 10 wt.%). In one or more aspects, unreacted reagents and onstream side products may be recycled back to the EOR 210, with a purge stream removed to prevent the excess accumulation of contaminants.

[0028] In one or more aspects, sodium 5,4-glucarate is converted to 5-dehydro-4-deoxy- D-glucaric acid (5,4-GA). Any suitable means of conversion may be carried out. In an aspect, sodium 5,4-glucarate is subjected to electrodialysis 235. Electrodialysis (also referred to as “ED”) is a separation process that utilizes an electrical potential difference as a driving force to move ions through a semipermeable membrane and removing sodium hydroxide to ensure charge neutrality. In doing so, the pH of the system is dropped down to less than about 2. The product exiting the electrodialysis unit 235 is a dilute 5,4-GA stream.

[0029] In one or more aspects, the dilute 5,4-GA stream is concentrated in a flash unit 240. In some aspects, the process stream further comprises a reverse osmosis unit upstream of the flash unit 240. In the flash unit 240, water may be actively removed and partially replaced with sulfolane, a non-volatile polar aprotic solvent in order to create thermodynamically favorable conditions for dehydration. The 5,4-GA in sulfolane stream may then be conveyed to a reactive distillation system 250, where 5,4-GA is dehydrated to form FDCA, concurrent with water removal via distillation. In one or more aspects, the reactive distillation system 250 could be a combination stirred reactor / flash drum or a distillation column with catalyst impregnated on trays or packing to drive the dehydration reaction.

[0030] In such aspects, the catalyst may comprise a strong-acid catalyst such as AMBERLYST which can be retained physically in the reactive distillation equipment. AMBERLYST refers to a series of macroporous ion exchange resins comprising a solid acid catalyst, commercially available from DUPONT. The reaction distillation system 250 may be operated under rough vacuum (2-8 psia) provided by a vacuum pump 255 to control the temperature to reduce or prevent unwanted side reactions.

[0031] In one or more aspects, FDCA is further processed by being enriched in another flash concentration unit 260. The concentrated FDCA may then be conveyed to one or more crystallizers 270 operated under a vacuum provided by vacuum pump 265. The mother liquor may be conveyed to centrifuge 280 and the centrifuged mother liquor recycled to improve yield. In one or more aspects, a fraction of the mother liquor may be purged to prevent excess impurity accumulation. High-purity FDCA crystals may be recovered.

[0032] FDCA may be formed using the compositions and methods of the present disclosure in a yield of from about 20% to about 90%; additionally or alternatively from about 30% to about 80%;additionally or alternatively from about 40% to about 80%;additionally or alternatively about 20%, about 25%, about 30%, about 35%, about 40%, about 45%, about 50%, about 55%, about 60%, about 65%, about 70%, about 75%, about 80%, about 85%, about 90%, about 95% and a yield of from about 70% to about 99%; additionally or alternatively about 80% to about 99%; additionally or alternatively about from about 90% to about 99%; additionally or alternatively and a purity of about 80%, about 82%, about 84%, about 86%, about 88%, about 90%, about 92%, about 94%, about 96% or about 98%.

[0033] In one or more aspects, the enzymes (i.e., biocatalysts) comprise one or more oxidases. In an aspect, the enzymes comprises a combination a peroxygenase, a glucose oxidase and a glucarate dehydrogenase, along with any cofactors and is collectively termed the “catalytic composition.” In some aspects, the catalytic composition further comprises an optional cofactor, an optional small molecule activator (SMA), an optional single electron oxidizer (SEO) or combinations thereof.

[0034] The oxidases of the catalytic composition may comprise any suitable oxidase enzyme. In some aspects, the oxidase of the catalytic composition comprises a copper radical oxidase (CRO). CROs have been categorized as ‘green’ small-molecule oxidation catalysts as they lack dependence on an organic cofactor and require only molecular oxygen as a cosubstrate. CROs are non-flavoprotein alcohol oxidoreductases that employ molecular oxygen as a terminal electron acceptor to generate hydrogen peroxide. In one or more aspects, a CRO for use in the present disclosure is a wildtype enzyme. In one or more aspects, a CRO for use in the present disclosure is a mutated enzyme.

[0035] In one or more aspects, the catalytic composition disclosed herein further comprises a SMA. Nonlimiting examples of SMAs suitable for use in the present disclosure include L-tryptophan, 2-mercaptobenzothiazole, L-histidine, methylchloroisothiazolinone, o-dianisidine, 2,2'-azino-bis(3-ethylbenzothiazoline-6- sulfonic acid (ABTS), 4-aminoantipyrine, L-tyrosine, (2,2,6,6-tetramethylpiperidin-1- yl)oxyl, chloromethylisothiazolinone, 4-thiazolecarboxylic acid, Sunset yellow FCF, tartrazine, p-benzoquinone, dicoumarol, phthalimide, saccharin, phthalic anhydride, erythrosine B, 2-aminobenzothiazole, thiabendazole, 2-hydroxybenzothiazole, phenothiazine, 6-aminobenzothiazole, indigo carmine, naphthalimide, 2-aminothiazole, thiazole, 2H-1 ,4-benzothiazin-3(4H)-one, 2-oxindole, beta-lapachone, menaquinone, thiamine, 4-methyl-5-thiazoleethanol, Allura Red AC, menadione, p-cresol, Fast greenFCF, Brilliant Blue FCF, methylisothiazolinone, caffeine, veratryl alcohol, fluorescein, and combinations thereof

[0036] In one or more aspects, the catalytic composition disclosed herein further comprises an SEO. In one or more aspects, the SEO is an enzyme such as a laccase, horseradish peroxidase, Dyp-type peroxidase, lactoperoxidase, chloroperoxidase, manganese peroxidase 1 , ascorbate peroxidase, dye-decolorizing peroxidase, unspecific peroxygenase, dehaloperoxidase, catalase-peroxidase, lignin peroxidase, soybean seed coat peroxidase, isoforms thereof or combinations thereof. In some aspects the oxidase catalyst system comprises a cofactor such as thiamine pyrophosphate, NAD+, NADP+, pyridoxal phosphate, methyl cobalamin, cobalamine, biotin, Coenzyme A, tetrahydrofolic acid, menaquinone, ascorbic acid, flavin mononucleotide, flavin adenine dinucleotide, and Coenzyme F420.

[0037] The optional cofactors (e.g., SMA, SEO) disclosed may be present individually in an amount ranging from about 1 ppm to about 500 ppm; additionally or alternatively, from about 5 ppm to about 500 ppm; additionally or alternatively, from about 10 ppm to about 500 ppm; additionally or alternatively, from about 20 ppm to about 500 ppm; additionally or alternatively; additionally or alternatively, from about 40 ppm to about 400 ppm; additionally or alternatively, from about 50 ppm to about 350 ppm; additionally or alternatively, from about 75 ppm to about 200 ppm; additionally or alternatively, about 1 ppm, about 5 ppm, about 10 ppm, about 15 ppm, about 20 ppm, about 25 ppm, about 30 ppm, about 35 ppm, about 40 ppm, about 45 ppm, about 50 ppm, about 55 ppm, about 60 ppm, about 65 ppm, about 70 ppm, about 75 ppm, about 80 ppm, about 85 ppm, about 90 ppm, about 95 ppm, about 100 ppm, about 105 ppm, about 110 ppm, about 115 ppm, about 120 ppm, about 125 ppm, about 130 ppm, about 135 ppm, about 140 ppm, about 145 ppm, about 150 ppm, about 155 ppm, about 160 ppm, about 165 ppm, about 170 ppm, about 175 ppm, about 180 ppm, about 185 ppm, about 190 ppm, about 195 ppm, about 200 ppm, about 205 ppm, about 210 ppm, about 215 ppm, about 220 ppm, about 225 ppm, about 230 ppm, about 235 ppm, about 240 ppm, about 245 ppm, about 250 ppm, about 255 ppm, about 260 ppm, about 265 ppm, about 270 ppm, about 275 ppm, about 280 ppm, about 285 ppm, about 290 ppm, about 295 ppm, about 300 ppm, about 305 ppm, about 310 ppm, about 315 ppm, about 320 ppm, about 325 ppm, about 330 ppm, about 335 ppm, about 340 ppm, about 345 ppm, about 350 ppm, about 355 ppm, about 360 ppm, about 365 ppm, about 370 ppm, about 375 ppm, about 380 ppm, about 385 ppm, about 390 ppm, about 395 ppm, about 400 ppm, about 405ppm, about 410 ppm, about 415 ppm, about 420 ppm, about 425 ppm, about 430 ppm, about 435 ppm, about 440 ppm, about 445 ppm, about 450 ppm, about 455 ppm, about 460 ppm, about 465 ppm, about 470 ppm, about 475 ppm, about 480 ppm, about 485 ppm, about 490 ppm, about 495 ppm, or, additionally or alternatively, about 500 ppm.

[0038] Additional conditions suitable for the oxidation of glucose may include one or more of the following parameters: a catalytic composition may have a combined enzyme concentration in an amount ranging from about 0.01 g / L to about 1 g / L, additionally or alternatively, from about 0.1 g / L to about 1 g / L, additionally or alternatively, from about 0.2 g / L to about 1 g / L, additionally or alternatively, from about 0.4 g / L to about 1 g / L, additionally or alternatively, from about 0.6 g / L to about 1 g / L, additionally or alternatively, from about 0.75 g / L to 1 g / L, additionally or alternatively, about 0.01 g / L, about 0.05 g / L, about 0.1 g / L, about 0.2 g / L, about 0.3 g / L, about 0.4 g / L, about 0.5 g / L, about 0.6 g / L, about 0.7 g / L, about 0.8 g / L, about 0.9 g / L or, additionally or alternatively, an amount of glucose of from about 0.1 weight per volume percent (w / v%) to about 60 w / v%, alternatively from about 5 w / v% to about 50 w / v% or alternatively from about 10 w / v% to about 40 w / v%; a temperature ranging from about 1 °C to about 70 °C, alternatively from about 5 to about 30 °C or alternatively from about 10 °C to about 25 °C; a suitable buffered media providing a pH ranging from about 5 to about 10, alternatively from about 5.5 to about 9 and a substrate amount ranging from about 6.5 to about 8.5, alternatively from about 6.5 to about 8.5 or alternatively from about 7 to about 8; an oxygen pressure of equal to or less than about 500 psi, alternatively from about 50 psi to about 250 psi or alternatively from about 70 psi to about 150 psi and a reaction time ranging from about 1 hour to about 24 hours or from about 2 hours to about 12 hours or from about 3 hours to about 6 hours.

[0039] As will be understood by one of ordinary skill in the art with the benefit of the present disclosure, reactions of the type disclosed herein may result in the production of byproducts (e.g., hydrogen peroxide, etc.) that can detrimentally impact other components of the reaction mixture. For example, hydrogen peroxide may degrade the oxidase resulting in a loss of catalytic activity. In such aspects, mitigation of the detrimental effects of hydrogen peroxide may be carried out such as by the introduction of a catalase (E.C. 1.11.1.61), the use of a hydrogen peroxide-resistant enzyme or combinations thereof.

[0040] In an aspect, any enzyme of the type disclosed herein (e.g., oxidases, peroxidases) is a wild type enzyme, a functional fragment thereof, or a functional variantthereof. “Fragment” as used herein is meant to include any amino acid sequence shorter than the full-length enzyme, but where the fragment maintains a catalytic activity sufficient to meet some user or process goal. Fragments may include a single contiguous sequence identical to a portion of the biocatalyst sequence. Alternatively, the fragment may have or include several different shorter segments where each segment is identical in amino acid sequence to a different portion of the amino acid sequence of the enzyme but linked via amino acids differing in sequence from the enzyme. Herein, a "functional variant" of the enzyme refers to a polypeptide which has at one or more positions of an amino acid insertion, deletion, or substitution, either conservative or non-conservative, and wherein each of these types of changes may occur alone, or in combination with one or more of the others, and / or one or more times in a given sequence but retains catalytic activity.

[0041] In the alternative or in combination with the aforementioned mutations, the enzyme may be mutated to improve the catalytic activity. Mutations may be carried out to enhance the protein or a homolog activity, increase the protein stability in the presence of substrates and products (e.g., hydrogen peroxide) and increase protein yield.

[0042] In an aspect, any enzyme of the type disclosed herein may be cloned into an appropriate expression vector and used to transform cells of an expression system such as E. coli, Saccharomyces sp., Pichi a sp., Aspergillus sp., Trichoderma sp., or Myceliophthora sp. A "vector" is a replicon, such as plasmid, phage, viral construct or cosmid, to which another DNA segment may be attached. Vectors are used to transduce and express a DNA segment in cells. As used herein, the terms "vector" and "construct" may include replicons such as plasmids, phage, viral constructs, cosmids, Bacterial Artificial Chromosomes (BACs), Yeast Artificial Chromosomes (YACs), Human Artificial Chromosomes (HACs), and the like into which one or more gene expression cassettes may be or are ligated. Herein, a cell has been "transformed" by an exogenous or heterologous nucleic acid or vector when such nucleic acid has been introduced inside the cell, for example, as a complex with transfection reagents or packaged in viral particles. The transforming DNA may or may not be integrated (covalently linked) into the genome of the cell.

[0043] In an aspect, the gene of an enzyme disclosed herein is provided as a recombinant sequence in a vector where the sequence is operatively linked to one or more control or regulatory sequences. "Operatively linked" expression controlsequences refer to a linkage in which the expression control sequence is contiguous with the gene of interest to control the gene of interest, as well as expression control sequences that act in trans or at a distance to control the gene of interest.

[0044] The term "expression control sequence" or "regulatory sequences" are used interchangeably and are used herein to refer to polynucleotide sequences which affect the expression of coding sequences to which they are operatively linked. Expression control sequences are sequences that control the transcription, post-transcriptional events, and translation of nucleic acid sequences. Expression control sequences include appropriate transcription initiation, termination, promoter, and enhancer sequences; efficient RNA processing signals such as splicing and polyadenylation signals; sequences that stabilize cytoplasmic mRNA; sequences that enhance translation efficiency (e.g., ribosome binding sites, etc.); sequences that enhance protein stability; and when desired, sequences that enhance protein secretion. The nature of such control sequences differs depending upon the host organism; in prokaryotes, such control sequences generally include promoter, ribosomal binding site, and transcription termination sequence. The term "control sequences" is intended to include, at a minimum, all components whose presence is essential for expression, and can also include additional components whose presence is advantageous, for example, leader sequences and fusion partner sequences.

[0045] The term "recombinant host cell" ("expression host cell", "expression host system", "expression system", or simply "host cell"), as used herein, is intended to refer to a cell into which a recombinant vector has been introduced. It should be understood that such terms are intended to refer not only to the particular subject cell but to the progeny of such a cell. Because certain modifications may occur in succeeding generations due to either mutation or environmental influences, such progeny may not, in fact, be identical to the parent cell, but are still included within the scope of the term "host cell" as used herein. A recombinant host cell may be an isolated cell or cell line grown in culture or may be a cell which resides in a living tissue or organism. In one or more aspects, the catalytic composition comprises a peroxygenase, a glucose oxidase and a glucarate dehydrogenase having SEQ ID No. 1 , SEQ ID No. 2 and SEQ ID No. 3, respectively.

[0046] In one or more aspects, a method of the present disclosure comprises the conversion of glucose to FDME which is diagrammed in Figure 5. With reference to Figure 5, a method of the present disclosure 300 comprises contacting (a) a catalyticcomposition (b) glucose; and (c) an oxidizing agent under conditions suitable for the oxidation of glucose which may be further oxidized in the presence transition metal oxidation catalyst The glucose oxidation product may be formed in an EOR 310 and then conveyed to a metal oxidation reactor 320 to form a product mixture that is subsequently conveyed to a separator 330, esterified 340, dehydrated 350, purified 360 and recovered as FDME crystals.

[0047] In an alternative aspect, depicted in Figure 6 is a process flow diagram 400 for the production of FDME from glucose. In an aspect, enzymes 401 and glucose 402 are contacted in the presence of air in an Enzyme Oxidation Reactor 410 under conditions suitable for the oxidation of glucose to form glucodialdose (GDA). In one or more aspects, air may be supplied to the EOR 410 via air compressors 403 and 404. The EOR 410 may be a pressure vessel where air is sparged from the bottom, which serves to both provide oxygen for reactions and to mix the tank. The reactions occurring in the EOR 410 are mildly exothermic; heat may be actively removed to ensure enzyme stability.

[0048] Conditions suitable for conversion of glucose to GDA may include the use of a combination of oxidizing enzymes. In one or more aspects, disposed within the EOR 410 is a combination of one or more copper radical oxidases and a peroxidase. CROs are a class of non-flavoprotein alcohol oxidoreductases that employ molecular oxygen as a terminal electron acceptor to generate hydrogen peroxide. CROs have been labeled ‘green’ small-molecule oxidation catalysts as they lack dependence on an organic cofactor and utilizes molecular oxygen as a cosubstrate.

[0049] In one or more aspects, the CRO is a galactose 6-oxidase (EC 1.1.3.9, GAO), alternatively a mutated GAO. GAOs function by oxidizing six-carbon (Ce) or similar alcohols of galactose or other sugars to produce aldehydes. A particular example of a CRO is the GAO from Fusarium graminearum. In one or more aspects, the CRO has SEQ ID No. 4.

[0050] In one or more aspects, conditions suitable for the formation of GDA include the presence of a small molecule activator (SMA) and a single electron oxidizer (SEO) such as a peroxidase; both of which facilitate the catalytic activity of the CRO.

[0051] Nonlimiting examples of SMAs suitable for use in the present disclosure include L-tryptophan, 2-mercaptobenzothiazole, L-histidine, methylchloroisothiazolinone, o- dianisidine, 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid (ABTS), 4- aminoantipyrine, L-tyrosine, (2,2,6,6-tetramethylpiperidin-1 -yl)oxyl,chloromethylisothiazolinone, 4-thiazolecarboxylic acid, Sunset yellow FCF, tartrazine, p-benzoquinone, dicoumarol, phthalimide, saccharin, phthalic anhydride, erythrosine B, 2-aminobenzothiazole, thiabendazole, 2-hydroxybenzothiazole, phenothiazine, 6- aminobenzothiazole, indigo carmine, naphthalimide, 2-aminothiazole, thiazole, 21-1-1 ,4- benzothiazin-3(4H)-one, 2-oxindole, beta-lapachone, menaquinone, thiamine, 4- methyl-5-thiazoleethanol, Allura Red AC, menadione, p-cresol, Fast green FCF, Brilliant Blue FCF, methylisothiazolinone, caffeine, veratryl alcohol, fluorescein, and combinations thereof.

[0052] In one or more aspects, the SEO is an enzyme such as a laccase, horseradish peroxidase, Dyp-type peroxidase, lactoperoxidase, chloroperoxidase, manganese peroxidase 1 , ascorbate peroxidase, dye-decolorizing peroxidase, unspecific peroxygenase, dehaloperoxidase, catalase-peroxidase, lignin peroxidase, soybean seed coat peroxidase, isoforms thereof or combinations thereof. In an aspect, the enzyme is horseradish peroxidase.

[0053] In one or more aspects, a catalytic composition for use in EOR 410 comprises a GAO (e.g., SEQ ID No.4), an SEO and a SMA. The catalytic composition may comprise an GAO in an amount ranging from about 0.01 g / L to about 1 g / L, additionally or alternatively, from about 0.1 g / L to about 1 g / L, additionally or alternatively, from about 0.2 g / L to about 1 g / L, additionally or alternatively, from about 0.4 g / L to about 1 g / L, additionally or alternatively, from about 0.6 g / L to about 1 g / L, additionally or alternatively, from about 0.75 g / L to 1 g / L, additionally or alternatively, about 0.01 g / L, about 0.05 g / L, about 0.1 g / L, about 0.2 g / L, about 0.3 g / L, about 0.4 g / L, about 0.5 g / L, about 0.6 g / L, about 0.7 g / L, about 0.8 g / L, about 0.9 g / L or, additionally or alternatively, about 1 g / L. The catalytic composition may comprise an SEO in an amount ranging from about 1 mg / L to about 250 mg / L, additionally or alternatively, from about 5 mg / L to about 250 mg / L, additionally or alternatively, from about 10 mg / L to about 250 mg / L, additionally or alternatively, from about 25 mg / L to about 250 mg / L, additionally or alternatively, from about 50 mg / L to find 250 mg / L, additionally or alternatively, from about 75 mg / L to 250 mg / L, additionally or alternatively, from about 100 mg / L to 250 mg / L, additionally or alternatively, from about 150 mg / L to 250 mg / L, additionally or alternatively, about 1 mg / L, about 5 mg / L, about 10 mg / L, about 15 mg / L, about 20 mg / L, about 25 mg / L, about 30 mg / L, about 35 mg / L, about 40 mg / L, about 45 mg / L, about 50 mg / L, about 55 mg / L, about 60 mg / L, about 65 mg / L, about 70 mg / L, about 75 mg / L, about 80 mg / L, about 85 mg / L, about 90 mg / L, about 95 mg / L, about 100 mg / L, about105 mg / L, about 110 mg / L, about 115 mg / L, about 120 mg / L, about 125 mg / L, about130 mg / L, about 135 mg / L, about 140 mg / L, about 145 mg / L, about 150 mg / L, about155 mg / L, about 160 mg / L, about 165 mg / L, about 170 mg / L, about 175 mg / L, about180 mg / L, about 185 mg / L, about 190 mg / L, about 195 mg / L, about 200 mg / L, about205 mg / L, about 210 mg / L, about 215 mg / L, about 220 mg / L, about 225 mg / L, about230 mg / L, about 235 mg / L, about 240 mg / L, about 245 mg / L or, additionally or alternatively, about 250 mg / L. The catalytic composition may comprise an SMA in an amount ranging from about 1 ppm to about 500 ppm, additionally or alternatively, from about 5 ppm to about 500 ppm, additionally or alternatively, from about 10 ppm to about 500 ppm, additionally or alternatively, from about 20 ppm to about 500 ppm, additionally or alternatively, or from about 40 ppm to about 400 ppm, additionally or alternatively, from about 50 ppm to about 350 ppm additionally or alternatively, from about 75 ppm to about 200 ppm additionally or alternatively, about 1 ppm, about 5 ppm, about 10 ppm, about 15 ppm, about 20 ppm, about 25 ppm, about 30 ppm, about 35 ppm, about 40 ppm, about 45 ppm, about 50 ppm, about 55 ppm, about 60 ppm, about 65 ppm, about 70 ppm, about 75 ppm, about 80 ppm, about 85 ppm, about 90 ppm, about 95 ppm, about 100 ppm, about 105 ppm, about 110 ppm, about 115 ppm, about 120 ppm, about 125 ppm, about 130 ppm, about 135 ppm, about 140 ppm, about 145 ppm, about 150 ppm, about 155 ppm, about 160 ppm, about 165 ppm, about 170 ppm, about 175 ppm, about 180 ppm, about 185 ppm, about 190 ppm, about 195 ppm, about 200 ppm, about 205 ppm, about 210 ppm, about 215 ppm, about 220 ppm, about 225 ppm, about 230 ppm, about 235 ppm, about 240 ppm, about 245 ppm, about 250 ppm, about 255 ppm, about 260 ppm, about 265 ppm, about 270 ppm, about 275 ppm, about 280 ppm, about 285 ppm, about 290 ppm, about 295 ppm, about 300 ppm, about 305 ppm, about 310 ppm, about 315 ppm, about 320 ppm, about 325 ppm, about 330 ppm, about 335 ppm, about 340 ppm, about 345 ppm, about 350 ppm, about 355 ppm, about 360 ppm, about 365 ppm, about 370 ppm, about 375 ppm, about 380 'ppm, about 385 ppm, about 390 ppm, about 395 ppm, about 400 ppm, about 405 ppm, about 410 ppm, about 415 ppm, about 420 ppm, about 425 ppm, about 430 ppm, about 435 ppm, about 440 ppm, about 445 ppm, about 450 ppm, about 455 ppm, about 460 ppm, about 465 ppm, about 470 ppm, about 475 ppm, about 480 ppm, about 485 ppm, about 490 ppm, about 495 ppm, or, additionally or alternatively, about 500 ppm.

[0054] Conditions suitable for the formation of GDA in EOR 410 may include one or more of the following reaction parameters: an amount of sugar (e.g., glucose) of fromabout 0.1 weight per volume percent (w / v%) to about 60 w / v%, alternatively from about 5 w / v% to about 50 w / v% or alternatively from about 10 w / v% to about 40 w / v%; a temperature ranging from about 1 °C to about 70 °C, alternatively from about 5 to about 30 °C or alternatively from about 10 °C to about 25 °C; a suitable buffered media providing a pH ranging from about 5 to about 10, alternatively from about 5.5 to about 9 and a substrate amount ranging from about 6.5 to about 8.5, alternatively from about 6.5 to about 8.5 or alternatively from about 7 to about 8; an oxygen pressure of equal to or less than about 500 psi, alternatively from about 50 psi to about 250 psi or alternatively from about 70 psi to about 150 psi and a reaction time ranging from about 1 hour to about 24 hours or from about 2 hours to about 12 hours or from about 3 hours to about 6 hours.

[0055] As will be understood by one of ordinary skill in the art with the benefit of the present disclosure, reactions of the type disclosed herein may result in the production of byproducts (e.g., hydrogen peroxide, etc.) that can detrimentally impact other components of the reaction mixture. For example, hydrogen peroxide may degrade the oxidase resulting in a loss of catalytic activity. In such aspects, mitigation of the detrimental effects of hydrogen peroxide may be carried out such as by the introduction of a catalase (E.C. 1.11.1.61), the use of a hydrogen peroxide-resistant enzyme or combinations thereof.

[0056] GDA may be formed at yields that can range from about 50% to about 99%, additionally or alternatively, from about 50% to about 90%, additionally or alternatively, from about 50% to about 80%, additionally or alternatively, at least about 55%, at least about 58%, at least about 60%, at least about 62%, at least about 64%, at least about 66%, at least about 68%, at least about 70%, at least about 72%, at least about 74%, at least about 76%, at least about 78%, at least about 80%, at least about 82%, at least about 84%, at least about 86%, at least about 88%, at least about 90%, at least about 92%, at least about 94%, at least about 96%, at least about 98%, at least about or at least about 99%. The GDA intermediate formed may be used without further processing in the methods of the present disclosure.

[0057] In order to retain enzyme, the product mixture may be passed through a separator such as a Tangential Flow Filtration (TFF) ultrafilter 415. The product mixture exiting the TFF 15 is an enzyme free permeate comprising from about 10 wt.% to about 50% GDA; additionally or alternatively from about 15 % to about 40% GDA; additionallyor alternatively from about 20% to about 30% GDA. Enzyme rich retentate may be recycled back to the EOR 415.

[0058] In one or more aspects, the GDA stream is conveyed to a MOR 420 having disposed therein an oxidation catalyst. The GDA may be contacted with the oxidation catalyst and an oxidizing agent in the MOR 420 under conditions suitable for the formation of glucaric acid. In one or more aspects, the oxidation catalyst comprises a transition metal; additionally or alternatively a supported transition-metal oxidation catalyst, additionally or alternatively a nanoparticle supported transition-metal oxidation catalyst. Collectively, these materials are termed herein transition metal oxidation catalyst (TMOC).

[0059] In an aspect, the TMOC comprises a support comprising carbon, ceria, silica, alumina, titania (TiO?), zirconia (ZrO2), a zeolite, or combinations thereof, which contain less than about 1.0 weight percent (wt.%), additionally or alternatively, less than about 0.1 wt.%, or additionally or alternatively less than about 0.01 wt.% SiO2 binders based on the total weight of the support.

[0060] Suitable support materials for use in the TMOC are predominantly mesoporous or macroporous, and substantially free from micropores. For example, the support may comprise less than about 20% micropores. In an aspect, the support is a porous nanoparticle support. As used herein, the term "micropore" refers to a pore with a diameter of less than about 2 nm, as measured by nitrogen adsorption and mercury porosimetry methods and as defined by IUPAC. As used herein, the term "mesopore" refers to pores with diameter from about 2 nm to about 50 nm, as measured by nitrogen adsorption and mercury porosimetry methods and as defined by IUPAC. As used herein, the term "macropore" refers to pores with diameters larger than 50 nm, as measured by nitrogen adsorption and mercury porosimetry methods and as defined by IUPAC.

[0061] In an aspect, the TMOC support comprises a mesoporous carbon extrudate having a mean pore diameter ranging from about 10 nm to about 100 nm and a surface area greater than about 20 m2g_1but less than about 300 m2g-1. Supports suitable for use in the present disclosure may have any suitable shape. For example, the support may be shaped into 0.8-3 mm trilobes, quadralobes, or pellet extrudates. Such shaped supports enable the use of fixed trickle bed reactors to perform the final oxidation step under continuous flow.

[0062] In one or more aspects, the metal comprises a Group 8 metal (e.g., Re, Os, Ir, Pt, Ru, Rh, Pd, Ag), a 3d transition metal, an early transition metal, or combinations thereof. In an aspect, the TMOC comprises gold (Au).

[0063] In an aspect, the TMOC comprises platinum and gold and is heterogeneous, solid-phase TMOCs. In such aspects, suitable catalyst supports include, without limitation, carbon, surface-treated aluminas (such as passivated aluminas or coated aluminas), silicas, titanias, zirconias, zeolites, montmorillonites, and modifications, mixtures or combinations thereof. The catalyst support may be treated so as to promote the preferential deposition of platinum and gold on the outer surface of the support so as to create a shell type TMOC. The platinum and gold-containing compounds that function as a TMOC may be produced by any suitable methodology. For example, the platinum and gold-containing TMOCs may be produced using deposition procedures such as incipient wetness, ion-exchange and deposition-precipitation.

[0064] In other aspects, the TMOC comprises metal phases that are monometallic or multimetallic combinations of Cu, Ag, Au, Ni, Pd, Pt, or Ir. The activity, selectivity, and stability of the active phases can be modulated with dopants of early 3d, 4d, and 5d transition metals, or heavy post transition metals such as Sn, Sb, and Bi. In some aspects, metals (e.g., Group 1 metals) are intercalated into the metal lattice to modulate catalyst properties. In an aspect, a salt precursor of the active phase is deposited onto a support of the type disclosed herein using any suitable methodology. For example, deposition of the active phases may be carried out using techniques such as incipient wetness impregnation, bulk adsorption impregnation, or deposition precipitation. In such aspects, the deposited salt precursor of the active phase is then converted to the active phase via Liquid Phase Reduction (LPR) with a suitable salt (e.g., formate salt) at temperatures of less than about 100 °C or via Gas Phase Reduction (GPR) at temperatures ranging from about 200 °C to about 500 °C or alternatively from about 200 °C to about 450 °C. In an aspect, the metal catalyst comprises gold, platinum, or a combination thereof and calcination in air at temperatures of equal to or greater than about 150 °C is performed.

[0065] In an aspect, the amount of active phase loaded onto a support of the type disclosed herein is less than about 2.0 weight percent (wt.%), additionally or alternatively less than about 1 .5 wt.%, or additionally or alternatively less than about 1 .0 wt.% based on the total weight of the TMOC. In an aspect, the amount of active phase loaded onto a support of the type disclosed herein is equal to or less than about 0.5 wt.% based onthe total weight of the TMOC. In an aspect, the radial distribution of the active phase across the support is anisotropic where the active phase is substantially concentrated in a less than about 500 pm annulus near the surface of the extrudate support in a “coreshell” configuration. The TMOCs of the present disclosure may display a steady state leaching amount of from about 1 ppb to about 100 ppb, additionally or alternatively less than about 100 ppb, additionally or alternatively less than about 90 ppb.

[0066] In an aspect, a TMOC of the type disclosed herein may be operated under one or more of the following reaction parameters: an oxygen pressure of equal to or less than about 500 psi, alternatively from about 50 psi to about 250 psi or alternatively from about 70 psi to about 150 psi; a reaction time ranging from about 1 hour to about 24 hours or from about 2 hours to about 12 hours or from about 3 hours to about 6 hours; and a temperature range of from about 40 °C to about 120 °C, additionally or alternatively form about 40 °C to about 110 °C, or additionally or alternatively from about 50 °C to about 100 °C.

[0067] In an aspect, a product mixture from the MOR 420 comprises GA. In one or more aspects, the MOR 420 is a trickle bed reactor, where high pressure air and permeate from the TFF 415 are reacted over a gold / platinum on carbon catalyst. This reaction is highly exothermic and can be carried out with interstage cooling utilized to control the exotherm.

[0068] In one or more aspects, the GA is conveyed from the MOR 420 to a flash unit 430 where it is concentrated under vacuum supplied by a suitable vacuum pump 425. Flash unit 430 may operate under rough vacuum (approximately 2-8 psia), and result in the removal of water from the GA stream thereby concentrating glucaric acid up to about 50 wt.%. The concentrated GA exiting flash unit 430 may be conveyed to flash unit 440 in order to exchange the water present in the concentrated GA stream with sulfolane. The GA sulfolane mixture provides more thermodynamically favorable conditions for dehydration than the aqueous GA mixture.

[0069] The GA sulfolane mixture may then be conveyed to a reactive distillation esterification (RDE) unit 435 where it is contacted with methanol reactant and homogeneous strong acid catalyst such as a sulfuric acid. Within the RDE unit 435 glucaric acid (within sulfolane) is then converted to glucaric acid methyl ester (GA Ester). Without wishing to be limited by theory, the esterification within the RDE unit 435 may proceed via a Fischer-Speier esterification where water is produced during the esterification (condensation reaction) and active removal of water facilitates highconversion. Active removal of water may be achieved via reactive distillation, where an azeotropic mixture of methanol-water is removed from the top of the RDE unit 435. Though not shown, a secondary distillation column can be used to recover unreacted methanol and return it to the RDE unit 435. The product of the RDE 435, GA Ester in sulfolane, can be removed as water-free bottoms.

[0070] In one or more aspects, the product of RDE unit 435, GA Ester in sulfolane stream, is conveyed to another dehydration and evaporation unit (D&E) 450 where the GA ester undergoes a dehydration reaction to form FDME. In the D&E unit 450 water may be removed to ensure full conversion. The product of the D&E unit 450 is a crude mixture having an amount of FDME ranging from about 10 wt.% to about 50 wt.%, additionally or alternatively from about 15 wt.% to about 40 wt.%; additionally or alternatively from about 20 wt.% to about 30 wt.%.

[0071] In one or more aspects, FDME 460 is then enriched in another flash concentration step in flash unit 460, before being conveyed to a crystallizer 470. High- purity FDME crystals may be recovered from the crystallizer 470 with the mother liquor recycled to improve yield. Both flash unit 460 and crystallizer 470 may be operated under a vacuum facilitated by vacuum pumps 455 and 465, respectively. In some aspects, a fraction of the mother liquor is purged to prevent excess impurity accumulation.

[0072] FDCA may be formed using the compositions and methods of the present disclosure in a yield of from about 20% to about 90%; additionally or alternatively from about 30% to about 80%;additionally or alternatively from about 40% to about 80%; additionally or alternatively about 20%, about 25%, about 30%, about 35%, about 40%, about 45%, about 50%, about 55%, about 60%, about 65%, about 70%, about 75%, about 80%, about 85%, about 90%, about 95% and a yield of from about 70% to about 99%; additionally or alternatively about 80% to about 99%; additionally or alternatively about from about 90% to about 99%; additionally or alternatively and a purity of about 80%, about 82%, about 84%, about 86%, about 88%, about 90%, about 92%, about 94%, about 96% or about 98%.

[0073] In aspects, one or more of the molecules of the present disclosure are biobased molecules characterized by equal to or greater than about 70% of the carbon atoms in the molecule originating from a renewable resource; additionally or alternatively equal to or greater than about 75%; additionally or alternatively equal to or greater than about 80%; additionally or alternatively equal to or greater than about 85%; additionally oralternatively equal to or greater than about 90%. Herein a renewable resource refers to a natural resource, which will replenish to replace the portion depleted by usage and consumption, either through natural reproduction or other recurring processes in a finite amount of time on a human time scale. In one or more aspects, the renewable resource is glucose.

[0074] The following are additional nonlimiting exemplary aspects of the presently disclosed subject matter

[0075] A first aspect which is a method for the production of 2,5-furandicarboxylic acid (FDCA) comprising contacting glucose with a catalyst composition under conditions suitable for the formation of glucarate; acidifying glucarate to form glucaric acid; dehydrating glucaric acid to form FDCA; and recovering FDCA.

[0076] A second aspect which is the method of the first aspect wherein the catalyst composition comprises (i) one or more oxidase enzymes, (ii) an oxidizing agent and (iii) one or more cofactors.

[0077] A third aspect which is the method of the second aspect wherein the one or more oxidase enzymes comprises a copper radical oxidase, a glucarate dehydrogenase, a glucose oxidase, a peroxygenase, mutants thereof, fragments thereof or combinations thereof.

[0078] A fourth aspect which is the method of any of the first through third aspects wherein the catalyst composition comprises a glucarate dehydrogenase, a peroxygenase, a glucose oxidase, mutants thereof or combinations thereof.

[0079] A fifth aspect which is the method of any of the first through fourth aspects wherein the oxidizing agent comprises air.

[0080] A sixth aspect which is the method of any of the second through fifth aspects wherein the cofactor comprises a single electron oxidizer.

[0081] A seventh aspect which is the method of the sixth aspect wherein the single electron oxidizer comprises a laccase, horseradish peroxidase, Dyp-type peroxidase, lactoperoxidase, chloroperoxidase, manganese peroxidase 1 , ascorbate peroxidase, dye-decolorizing peroxidase, unspecific peroxygenase, dehaloperoxidase, catalase- peroxidase, lignin peroxidase, soybean seed coat peroxidase, isoforms thereof or combinations thereof.

[0082] An eighth aspect which is the method of the sixth aspect wherein the cofactor comprises a small molecule activator.

[0083] A ninth aspect which is the method of any of the sixth through eighth aspects wherein the small molecule activator is selected from the group consisting of tryptophan, 2-mercaptobenzothiazole, L-histidine, methylchloroisothiazolinone, o-dianisidine, 2,2'- azino-bis(3-ethylbenzothiazoline-6-sulfonic acid (ABTS), 4-aminoantipyrine, L-tyrosine, (2,2,6,6-tetramethylpiperidin-1-yl)oxyl, chloromethylisothiazolinone, 4- thiazolecarboxylic acid, Sunset yellow FCF, tartrazine, p-benzoquinone, dicoumarol, phthalimide, saccharin, phthalic anhydride, erythrosine B, 2-aminobenzothiazole, thiabendazole, 2-hydroxybenzothiazole, phenothiazine, 6-aminobenzothiazole, indigo carmine, naphthalimide, 2-aminothiazole, thiazole, 2H-1 ,4-benzothiazin-3(4H)-one, 2- oxindole, beta-lapachone, menaquinone, thiamine, 4-methyl-5-thiazoleethanol, Allura Red AC, menadione, p-cresol, Fast green FCF, Brilliant Blue FCF, methylisothiazolinone, caffeine, veratryl alcohol, fluorescein, and combinations thereof.

[0084] A tenth aspect which is the method of any of the sixth through ninth aspects wherein the cofactor is selected from the group consisting of thiamine pyrophosphate, NAD+, NADP+, pyridoxal phosphate, methyl cobalamin, cobalamine, biotin, Coenzyme A, tetrahydrofolic acid, menaquinone, ascorbic acid, flavin mononucleotide, flavin adenine dinucleotide, Coenzyme F420 and combinations thereof.

[0085] An eleventh aspect which is the method of any of the first through tenth aspects wherein the catalyst composition further comprises a catalase.

[0086] A twelfth aspect which is a method for the production of 2,5-furan dicarboxylic acid dimethyl ester (FDME) comprising contacting glucose with a catalyst composition under conditions suitable for the formation of glycolaldehyde; contacting glycolaldehyde with a transition metal oxidation catalyst under conditions suitable for the formation of glucaric acid; esterifying glucaric acid to form glucaricacid methyl ester; dehydrating the glucaric acid methyl ester to form FDME; and recovering FDME.

[0087] A thirteenth aspect which is the method of the twelfth aspect, wherein the one of catalyst composition comprises (i) a copper radical oxidase, (ii) an oxidizing agent and (iii) one or more optional cofactors.

[0088] A fourteenth aspect which is the method of the thirteenth aspect wherein the copper radical oxidase comprises galactose oxidase, a mutated galactose oxidase, fragments thereof or combinations thereof.

[0089] A fifteenth aspect which is the method any of the thirteenth through fourteenth aspects wherein the oxidizing agent comprises air.

[0090] A sixteenth aspect which is the method of any of the thirteenth through fifteenth aspects wherein the cofactor comprises a single electron oxidizer.

[0091] A seventeenth aspect which is the method of the sixteenth aspect wherein the single electron oxidizer comprises a laccase, horseradish peroxidase, Dyp-type peroxidase, lactoperoxidase, chloroperoxidase, manganese peroxidase 1 , ascorbate peroxidase, dye-decolorizing peroxidase, unspecific peroxygenase, dehaloperoxidase, catalase-peroxidase, lignin peroxidase, soybean seed coat peroxidase, isoforms thereof or combinations thereof.

[0092] An eighteenth aspect which is the method of any of the thirteenth through seventeenth aspects wherein the cofactor comprises a small molecule activator.

[0093] A nineteenth aspect which is the method of the eighteenth aspect wherein the small molecule activator is selected from the group consisting of tryptophan, 2- mercaptobenzothiazole, L-histidine, methylchloroisothiazolinone, o-dianisidine, 2,2'- azino-bis(3-ethylbenzothiazoline-6-sulfonic acid (ABTS), 4-aminoantipyrine, L-tyrosine, (2,2,6,6-tetramethylpiperidin-1-yl)oxyl, chloromethylisothiazolinone, 4- thiazolecarboxylic acid, Sunset yellow FCF, tartrazine, p-benzoquinone, dicoumarol, phthalimide, saccharin, phthalic anhydride, erythrosine B, 2-aminobenzothiazole, thiabendazole, 2-hydroxybenzothiazole, phenothiazine, 6-aminobenzothiazole, indigo carmine, naphthalimide, 2-aminothiazole, thiazole, 2H-1 ,4-benzothiazin-3(4H)-one, 2- oxindole, beta-lapachone, menaquinone, thiamine, 4-methyl-5-thiazoleethanol, Allura Red AC, menadione, p-cresol, Fast green FCF, Brilliant Blue FCF, methylisothiazolinone, caffeine, veratryl alcohol, fluorescein, and combinations thereof.

[0094] A twentieth aspect which is the method of any of the thirteenth through nineteenth aspects wherein the cofactor is selected from the group consisting of thiamine pyrophosphate, NAD+, NADP+, pyridoxal phosphate, methyl cobalamin, cobalamine, biotin, Coenzyme A, tetrahydrofolic acid, menaquinone, ascorbic acid, flavin mononucleotide, flavin adenine dinucleotide, and Coenzyme F420.

[0095] A twenty-first aspect which is the method of any of the twelfth through twentieth aspects wherein the transition metal oxidation catalyst comprises (a) a metal and (b) a support.

[0096] A twenty-second aspect which is the method of the twenty-first aspect wherein the support comprises ceramic, metal oxides, glass, titania, silica, alumina, zirconia, ceria, ceramic, carbon or combinations thereof.

[0097] A twenty-third aspect which is the method of any of the twenty-first aspect through twenty-second aspects wherein the support material has a surface area of from about 100 m2 / g to about 1000 m2 / g.

[0098] While aspects of the presently disclosed subject matter have been shown and described, modifications thereof can be made by one skilled in the art without departing from the spirit and teachings of the subject matter. The aspects described herein are exemplary only, and are not intended to be limiting. Many variations and modifications of the subject matter disclosed herein are possible and are within the scope of the disclosed subject matter. Where numerical ranges or limitations are expressly stated, such express ranges or limitations should be understood to include iterative ranges or limitations of like magnitude falling within the expressly stated ranges or limitations (e.g., from about 1 to about 10 includes, 2, 3, 4, etc.; greater than 0.10 includes 0.11 , 0.12, 0.13, etc.). Use of the term "optionally" with respect to any element of a claim is intended to mean that the subject element is required, or alternatively, is not required. Both alternatives are intended to be within the scope of the claim. Use of broader terms such as comprises, includes, having, etc. should be understood to provide support for narrower terms such as consisting of, consisting essentially of, comprised substantially of, etc.

[0099] Accordingly, the scope of protection is not limited by the description set out above but is only limited by the claims which follow, that scope including all equivalents of the subject matter of the claims. Each and every claim is incorporated into the specification as an aspect of the present disclosure. Thus, the claims are a further description and are an addition to the aspects of the present invention. The discussion of a reference herein is not an admission that it is prior art to the presently disclosed subject matter, especially any reference that may have a publication date after the priority date of this application. The disclosures of all patents, patent applications, and publications cited herein are hereby incorporated by reference, to the extent that they provide exemplary, procedural or other details supplementary to those set forth herein.

Claims

CLAIMSWhat is claimed is:

1. A method for the production of 2,5-furandicarboxylic acid (FDCA), the method comprising: contacting glucose with a catalyst composition under conditions suitable for the formation of glucarate; acidifying glucarate to form glucaric acid; dehydrating glucaric acid to form FDCA; and recovering FDCA.

2. The method of claim 1 , wherein the catalyst composition comprises (i) one or more oxidase enzymes, (ii) an oxidizing agent and (iii) one or more cofactors.

3. The method of claim 2, wherein the one or more oxidase enzymes comprises a copper radical oxidase, a glucarate dehydrogenase, a glucose oxidase, a peroxygenase, mutants thereof, fragments thereof or combinations thereof.

4. The method of claim 1 , wherein the catalyst composition comprises a glucarate dehydrogenase, a peroxygenase, a glucose oxidase, mutants thereof or combinations thereof.

5. The method of claim 1 , wherein the oxidizing agent comprises air.

6. The method of claim 2, wherein the cofactor comprises a single electron oxidizer.

7. The method of claim 6, wherein the single electron oxidizer comprises a laccase, horseradish peroxidase, Dyp-type peroxidase, lactoperoxidase, chloroperoxidase, manganese peroxidase 1 , ascorbate peroxidase, dye-decolorizing peroxidase, unspecific peroxygenase, dehaloperoxidase, catalase-peroxidase, lignin peroxidase, soybean seed coat peroxidase, isoforms thereof or combinations thereof.

8. The method of claim 6, wherein the cofactor comprises a small molecule activator.

9. The method of claim 8, wherein the small molecule activator is selected from the group consisting of tryptophan, 2-mercaptobenzothiazole, L-histidine, methylchloroisothiazolinone, o-dianisidine, 2,2'-azino-bis(3-ethylbenzothiazoline-6- sulfonic acid (ABTS), 4-aminoantipyrine, L-tyrosine, (2,2,6,6-tetramethylpiperidin-1- yl)oxyl, chloromethylisothiazolinone, 4-thiazolecarboxylic acid, Sunset yellow FCF, tartrazine, p-benzoquinone, dicoumarol, phthalimide, saccharin, phthalic anhydride, erythrosine B, 2-aminobenzothiazole, thiabendazole, 2-hydroxybenzothiazole, phenothiazine, 6-aminobenzothiazole, indigo carmine, naphthalimide, 2-aminothiazole, thiazole, 2H-1 ,4-benzothiazin-3(4H)-one, 2-oxindole, beta-lapachone, menaquinone, thiamine, 4-methyl-5-thiazoleethanol, Allura Red AC, menadione, p-cresol, Fast green FCF, Brilliant Blue FCF, methylisothiazolinone, caffeine, veratryl alcohol, fluorescein, and combinations thereof.

10. The method of claim 6, wherein the cofactor is selected from the group consisting of thiamine pyrophosphate, NAD+, NADP+, pyridoxal phosphate, methyl cobalamin, cobalamine, biotin, Coenzyme A, tetrahydrofolic acid, menaquinone, ascorbic acid, flavin mononucleotide, flavin adenine dinucleotide, Coenzyme F420 and combinations thereof.

11. The method of claim 1 , wherein the catalyst composition further comprises a catalase.

12. A method for the production of 2,5-furan dicarboxylic acid dimethyl ester (FDME) comprising: contacting glucose with a catalyst composition under conditions suitable for the formation of glycolaldehyde; contacting glycolaldehyde with a transition metal oxidation catalyst under conditions suitable for the formation of glucaric acid; esterify ing glucaric acid to form glucaric acid methyl ester; dehydrating the glucaric acid methyl ester to form FDME; and recovering FDME.

13. The method of claim 12, wherein the one of catalyst composition comprises (i) a copper radical oxidase, (ii) an oxidizing agent, and (iii) one or more optional cofactors.

14. The method of claim 13, wherein the copper radical oxidase comprises galactose oxidase, a mutated galactose oxidase, fragments thereof or combinations thereof.

15. The method of claim 13, wherein the oxidizing agent comprises air.

16. The method of claim 13, wherein the cofactor comprises a single electron oxidizer.

17. The method of claim 16, wherein the single electron oxidizer comprises a laccase, horseradish peroxidase, Dyp-type peroxidase, lactoperoxidase, chloroperoxidase, manganese peroxidase 1 , ascorbate peroxidase, dye-decolorizing peroxidase, unspecific peroxygenase, dehaloperoxidase, catalase-peroxidase, lignin peroxidase, soybean seed coat peroxidase, isoforms thereof or combinations thereof.

18. The method of claim 13, wherein the cofactor comprises a small molecule activator.

19. The method of claim 18, wherein the small molecule activator is selected from the group consisting of tryptophan, 2-mercaptobenzothiazole, L-histidine, methylchloroisothiazolinone, o-dianisidine, 2,2'-azino-bis(3-ethylbenzothiazoline-6- sulfonic acid (ABTS), 4-aminoantipyrine, L-tyrosine, (2,2,6,6-tetramethylpiperidin-1- yl)oxyl, chloromethylisothiazolinone, 4-thiazolecarboxylic acid, Sunset yellow FCF, tartrazine, p-benzoquinone, dicoumarol, phthalimide, saccharin, phthalic anhydride, erythrosine B, 2-aminobenzothiazole, thiabendazole, 2-hydroxybenzothiazole, phenothiazine, 6-aminobenzothiazole, indigo carmine, naphthalimide, 2-aminothiazole, thiazole, 2H-1 ,4-benzothiazin-3(4H)-one, 2-oxindole, beta-lapachone, menaquinone, thiamine, 4-methyl-5-thiazoleethanol, Allura Red AC, menadione, p-cresol, Fast green FCF, Brilliant Blue FCF, methylisothiazolinone, caffeine, veratryl alcohol, fluorescein, and combinations thereof.

20. The method of claim 13, wherein the cofactor is selected from the group consisting of thiamine pyrophosphate, NAD+, NADP+, pyridoxal phosphate, methylcobalamin, cobalamine, biotin, Coenzyme A, tetrahydrofolic acid, menaquinone, ascorbic acid, flavin mononucleotide, flavin adenine dinucleotide, and Coenzyme F420.21 . The method of claim 12, wherein the transition metal oxidation catalyst comprises (a) a metal and (b) a support.

22. The method of claim 21 , wherein the support comprises ceramic, metal oxides, glass, titania, silica, alumina, zirconia, ceria, ceramic, carbon or combinations thereof.

23. The method of claim 21 , wherein the support material has a surface area of from about 100 m2 / g to about 1000 m2 / g.

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