1.1.1.1 alcohol dehydrogenase biofuel production ethanol production by the hyperthermophilic archaeon Pyrococcus furiosus by expression of bacterial bifunctional alcohol dehydrogenase (Tx-AdhE). Ethanol and acetate are the only major carbon end-products from glucose under these conditions. The amount of ethanol produced per estimated glucose consumed is increased from the background level 0.7 respectively. Although ethanol production from acetyl-CoA is demonstrated in Pyrococcus furiosus, the highest ethanol yield (from strain Te-AdhEA) is still lower than that of the AAA pathway in Pyrococcus furiosus, which functions via the native enzymes acetyl-CoA synthetase (ACS) and aldehyde oxidoreductase (AOR) along with heterologously expressed alcohol dehydrogenase (AdhA) 1.1.1.1 alcohol dehydrogenase biofuel production expression in Pyrococcus furiosus from which the native aldehyde oxidoreductase (AOR) gene is deleted supports ethanol production. The highest amount of ethanol (estimated 61% theoretical yield) is produced when adhE and adhA from Thermoanaerobacter are co-expressed. A strain containing the Thermoanaerobacter ethanolicus AdhE in a synthetic operon with AdhA is constructed. The AdhA gene is amplified from Thermoanaerobacter sp. X514. The amino acid sequence of AdhA from Thermoanaerobacter sp. X514 is identical to that of AdhA from Thermoanaerobacter ethanolicus. Of the bacterial strains expressing the various heterologous AdhE genes, only those containing AdhE and AdhA from Thermoanaerobacter sp. produced ethanol above background. The Thermoanaerobacter ethanolicus AdhEA strain containing both AdhE and AdhA produces the most ethanol (4.2 mM), followed by Thermoanaerobacter ethanolicus AdhE strain (2.6 mM), Thermoanaerobacter ethanolicus AdhA strain (1.8 mM) and Thermoanaerobacter sp. X514 AdhE strain (1.5 mM). Ethanol and acetate are the only major carbon end-products from glucose under these conditions. For these four strains, the amount of ethanol produced per estimated glucose consumed is increased from the background level to 1.2, 1.0, 0.8 and 0.7 respectively 1.1.1.1 alcohol dehydrogenase biofuel production proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol 1.1.1.1 alcohol dehydrogenase biofuel production alcohol dehydrogenase from cyanobacterium Synechocystis sp. PCC 6803 is a key enzyme for biofuel production. It is a necessary enzyme in the synthesis of ethanol and butanol with critical importance in the production of biofuels. Alcohol dehydrogenase from cyanobacterium Synechocystis sp. PCC 6803 has higher efficiency for the production of alcohols such as 1-butanol and isobutanol 1.1.1.6 glycerol dehydrogenase biofuel production proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol 1.1.1.35 3-hydroxyacyl-CoA dehydrogenase biofuel production 3-hydroxybutyryl-CoA dehydrogenase is an enzyme involved in the synthesis of the biofuel n-butanol by converting acetoacetyl-CoA to 3-hydroxybutyryl-CoA, molecular mechanism of n-butanol biosynthesis, overview 1.1.1.35 3-hydroxyacyl-CoA dehydrogenase biofuel production the highly efficient mutant enzyme K50A/K54A/L232Y can be useful for increasing the production rate of n-butanol in biofuel production 1.1.1.B64 xylitol dehydrogenase (NADP+) biofuel production the enzyme might be useful for production biofuels from D-xylose. Chlorella sorokiniana can uptake D-xylose only by an inducible D-xylose transportation system in a light-dependent manner after induction with D-glucose. Xylose reductase (XDH) then converts 50 to 60% of the consumed D-xylose to xylitol, which is subsequently converted to D-xylulose 1.1.1.86 ketol-acid reductoisomerase (NADP+) biofuel production engineering of Klebsiella pneumoniae to produce 2-butanol from crude glycerol as a sole carbon source by expressing acetolactate synthase (ilvIH), keto-acid reducto-isomerase (ilvC) and dihydroxyacid dehydratase (ilvD) from Klebsiella pneumoniae, and aalpha-ketoisovalerate decarboxylase (kivd) and alcohol dehydrogenase (adhA) from Lactococcus lactis. The engineered strain produces 2-butanol (160 mg/l) from crude glycerol. Elimination of the 2,3-butanediol pathway from the recombinant strain by inactivating alpha-acetolactate decarboxylase (adc) improves the yield of 2-butanol 320 mg/l 1.1.1.195 cinnamyl-alcohol dehydrogenase biofuel production downregulation of (hydroxy)cinnamyl alcohol dehydrogenase (CAD) genes is another promising strategy to increase cell wall digestibility for biofuel production 1.1.1.383 ketol-acid reductoisomerase [NAD(P)+] biofuel production a cytosolically located, cofactor-balanced isobutanol pathway, consisting of a mosaic of bacterial enzymes is expressed in Sacchaormyces cerevisiae. In aerobic cultures, the pathway intermediate isobutyraldehyde is oxidized to isobutyrate rather than reduced to isobutanol. Significant concentrations of the pathway intermediates 2,3-dihydroxyisovalerate and alpha-ketoisovalerate, as well as diacetyl and acetoin, accumulate extracellularly. While the engineered strain cannot grow anaerobically, micro-aerobic cultivation results in isobutanol formation at a yield of 0.018 mol/mol glucose. Simultaneously, 2,3-butanediol is produced at a yield of 0.64 mol/molglucose 1.1.1.383 ketol-acid reductoisomerase [NAD(P)+] biofuel production combination of high activity alcohol dehydrogenase YqhD mutants with IlvC mutants, both accepting NADH as a redox cofactor, in an engineered Escherichia coli strain, enabling comprehensive utilization of the biomass for biofuel applications. The refined strain, shows an increased fusel alcohol yield of about 60% compared to wild type under anaerobic fermentation on amino acid mixtures.When applied to real algal protein hydrolysates, the strain produces 100% and 38% more total mixed alcohols than the wild type strain on two different algal hydrolysates, respectively 1.1.1.383 ketol-acid reductoisomerase [NAD(P)+] biofuel production Recent work has demonstrated glucose to isobutanol conversion through a modified amino acid pathway in a recombinant organism. We demonstrate that an NADH-dependent pathway enables anaerobic isobutanol production at 100% theoretical yield and at higher titer and productivity than both the NADPH-dependent pathway and transhydrogenase over-expressing strain 1.1.3.4 glucose oxidase biofuel production glucose oxidase is typically used in the anode of biofuel cells to oxidise glucose 1.1.3.4 glucose oxidase biofuel production used in miniature membrane-less glucose/O2 biofuel cells 1.1.3.4 glucose oxidase biofuel production the enzyme used for biofuel cells 1.1.3.10 pyranose oxidase biofuel production pyranose oxidase immobilized on carbon nanotubes via covalent attachment, enzyme coating, and enzyme precipitate coating is used to fabricate enzymatic electrodes for enzyme-based biosensors and biofuel cells 1.1.3.47 5-(hydroxymethyl)furfural oxidase biofuel production current large-scale pretreatment processes for lignocellulosic biomass are generally accompanied by the formation of toxic degradation products, such as 5-hydroxymethylfurfural (HMF), which inhibit cellulolytic enzymes and fermentation by ethanol-producing yeast. Overcoming these toxic effects is a key technical barrier in the biochemical conversion of plant biomass to biofuels. Pleurotus ostreatus, a white-rot fungus, can efficiently degrade lignocellulose, and it can tolerate and metabolize HMF involving HMF oxidase (HMFO) encoded by HmfH 1.1.5.2 glucose 1-dehydrogenase (PQQ, quinone) biofuel production construction of a long-life biofuel cell using a hyperthermophilic enzyme. For the cathode, the multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum is used, which catalyzes a four-electron reduction, and, for the anode, the PQQ-dependent glucose dehydrogenase from Pyrobaculum aerophilum is used. When the enzymes are used as electrodes, oriented with carbon nanotubes in a highly organized manner, the maximum output is 0.011 mW at 0.2 V. This output can be maintained 70% after 14 days 1.1.5.2 glucose 1-dehydrogenase (PQQ, quinone) biofuel production its high stability at high temperature makes this enzyme potentially useful for applications in biosensors or biofuel cells 1.1.5.5 alcohol dehydrogenase (quinone) biofuel production comparison of a direct electron transfer bioanode containing both PQQ-ADH (pyrroloquinoline quinone-dependent alcohol dehydrogenase) and PQQ-AldDH (PQQ-dependent aldehyde dehydrogenase) immobilized onto different modified electrode surfaces employing either a tetrabutylammonium-modified Nafion membrane polymer or polyamidoamine (PAMAM) dendrimers. The prepared bioelectrodes are able to undergo direct electron transfer onto glassy carbon surface in the presence as well as the absence of multi-walled carbon nanotubes, also, in the latter case a relevant shift in the oxidation peak of about 180 mV vs. saturated calomel electrode is observed 1.1.5.9 glucose 1-dehydrogenase (FAD, quinone) biofuel production use as anode enzyme in biofuel cells 1.1.5.9 glucose 1-dehydrogenase (FAD, quinone) biofuel production a glucose biofuel cell anode, in which the aminoferrocene and FAD-GDH-immobilized MgO-templated porous carbon is coated on a carbon cloth, is constructed. The anode is combined with bilirubin oxidase and a 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)-immobilized biocathode 1.1.5.9 glucose 1-dehydrogenase (FAD, quinone) biofuel production synthesis of a naphthoquinone-functionalized redox polymer that is used to immobilize and electronically communicate with flavin adenine dinucleotide-dependent glucose dehydrogenase, yielding an enzymatic bioanode that is able to deliver large catalytic current densities for glucose oxidation at a relatively low associated potential 1.1.5.14 fructose 5-dehydrogenase biofuel production an enzymatic gold bioanode fabricated with fructose dehydrogenase and a polyaniline film can be used as a single-compartment fructose biofuel cell 1.1.99.18 cellobiose dehydrogenase (acceptor) biofuel production application in enzymatic fuel cells is limited by their relatively low activity with this substrate 1.1.99.18 cellobiose dehydrogenase (acceptor) biofuel production attractive oxidoreductase for bioelectrochemical applications. Its two-domain structure allows the flavoheme enzyme to establish direct electron transfer to biosensor and biofuel cell electrodes. The application of CDH in these devices is impeded by its limited stability under turnover conditions. Screening results in one CDH variant that exhibits improved turnover stability on a biosensor electrode, which is suitable for the application in implantable continuous glucose monitoring biosensors or biofuel cells 1.1.99.18 cellobiose dehydrogenase (acceptor) biofuel production key enzyme in biofuel cells 1.1.99.18 cellobiose dehydrogenase (acceptor) biofuel production the enzyme can be used for constructing biofuel cells 1.1.99.18 cellobiose dehydrogenase (acceptor) biofuel production the enzyme has applications in renewable biofuel production 1.1.99.18 cellobiose dehydrogenase (acceptor) biofuel production the enzyme is used in biofuel production 1.1.99.29 pyranose dehydrogenase (acceptor) biofuel production pyranose dehydrogenase is a promising candidate for the anodic reaction in enzymatic biofuel cells powered by carbohydrate mixtures 1.1.99.35 soluble quinoprotein glucose dehydrogenase biofuel production the pyrroloquinoline quinone/glucose dehydrogenase (PQQ-GDH) electrode can be used as bioanode within a biofuel cell. PQQ-GDH is efficiently wired by the polymer polythiophene to the multiwalled carbon nanotubes (MWCNT) electrode 1.1.99.35 soluble quinoprotein glucose dehydrogenase biofuel production usage in biofuel cells 1.2.1.10 acetaldehyde dehydrogenase (acetylating) biofuel production ethanol production by the hyperthermophilic archaeon Pyrococcus furiosus by expression of bacterial bifunctional alcohol dehydrogenase from Thermoanaerobacter sp. X514. Ethanol and acetate are the only major carbon end-products from glucose under these conditions. The amount of ethanol produced per estimated glucose consumed is increased from the background level 0.7 respectively. Although ethanol production from acetyl-CoA is demonstrated in Pyrococcus furiosus, the highest ethanol yield (from strain Te-AdhEA) is still lower than that of the AAA pathway in Pyrococcus furiosus, which functions via the native enzymes acetyl-CoA synthetase (ACS) and aldehyde oxidoreductase (AOR) along with heterologously expressed alcohol dehydrogenase (AdhA) 1.2.1.10 acetaldehyde dehydrogenase (acetylating) biofuel production expression in Pyrococcus furiosus from which the native aldehyde oxidoreductase (AOR) gene is deleted supports ethanol production. The highest amount of ethanol (estimated 61% theoretical yield) is produced when adhE and adhA from Thermoanaerobacter are co-expressed. A strain containing the Thermoanaerobacter ethanolicus AdhE in a synthetic operon with AdhA is constructed. The AdhA gene is amplified from Thermoanaerobacter sp. X514. The amino acid sequence of AdhA from Thermoanaerobacter sp. X514 is identical to that of AdhA from Thermoanaerobacter ethanolicus. Of the bacterial strains expressing the various heterologous AdhE genes, only those containing AdhE and AdhA from Thermoanaerobacter sp. produced ethanol above background. The Thermoanaerobacter ethanolicus AdhEA strain containing both AdhE and AdhA produces the most ethanol (4.2 mM), followed by Thermoanaerobacter ethanolicus AdhE strain (2.6 mM), Thermoanaerobacter ethanolicus AdhA strain (1.8 mM) and Thermoanaerobacter sp. X514 AdhE strain (1.5 mM). Ethanol and acetate are the only major carbon end-products from glucose under these conditions. For these four strains, the amount of ethanol produced per estimated glucose consumed is increased from the background level to 1.2, 1.0, 0.8 and 0.7 respectively. Although ethanol production from acetyl-CoA is demonstrated in Pyrococcus furiosus, the highest ethanol yield (from strain Thermoanaerobacter ethanolicus AdhEA) is still lower than that of the previously reported AAA pathway in Pyrococcus furiosus, which functions via native enzymes acetyl-CoA synthetase (ACS) and aldehyde oxidoreductase (AOR) along with heterologously expressed alcohol dehydrogenase (AdhA) 1.2.1.10 acetaldehyde dehydrogenase (acetylating) biofuel production proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) biofuel production proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol 1.2.1.B25 long-chain-fatty-acyl-CoA reductase biofuel production long-chain acyl-CoA reductases (ACRs) catalyze a key step in the biosynthesis of hydrocarbon waxes. As such they are attractive as components in engineered metabolic pathways for drop in biofuels. The slow turnover number measured for Synechococcus elongatus ACR poses a challenge for its use in biofuel applications where highly efficient enzymes are needed 1.2.7.1 pyruvate synthase biofuel production proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol 1.3.3.5 bilirubin oxidase biofuel production the enzyme is used in a biofuel cell comprising enzymeless anode consisting of 0.2 mM braided gold wire modified with colloidal platinum and bilirubin oxidase-modified gold-coated Buckypaper biocathode 1.10.3.2 laccase biofuel production construction of a long-life biofuel cell using a hyperthermophilic enzyme. For the cathode, the multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum is used, which catalyzes a four-electron reduction, and, for the anode, the PQQ-dependent glucose dehydrogenase from Pyrobaculum aerophilum is used. When the enzymes are used as electrodes, oriented with carbon nanotubes in a highly organized manner, the maximum output is 0.011 mW at 0.2 V. This output can be maintained 70% after 14 days 1.10.3.2 laccase biofuel production potential for bioconversion of lignin rich agricultural byproducts into animal feed and cellulosic ethanol. The enzyme effectively improves in vitro digestibility of maize straw 1.10.3.2 laccase biofuel production lignin degradation of agricultural biomass for biofuel production 1.11.1.13 manganese peroxidase biofuel production applications of recombinant enzyme in the pulp and paper industry and in the processing of lignocellulosic materials for ethanol and biofuels production 1.11.1.13 manganese peroxidase biofuel production bioethanol production, the enzymes laccase and manganese peroxidase from Klebsiella pneumoniae are employed for ethanol production from rice and wheat bran biomass which shows 39.29% improved production compared to control, evaluation 1.11.1.13 manganese peroxidase biofuel production microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels 1.11.1.14 lignin peroxidase biofuel production the use of LiP may provide a cost-effective, efficient and greener route for the transformation of biomass into second-generation (2 G) biofuels. Lignin depolymerization is an important step in producing 2 G biofuels and other green chemicals as lignin protects cellulose and hemicellulose against the enzymes required to hydrolyse it to fermentable sugars 1.13.11.8 protocatechuate 4,5-dioxygenase biofuel production enhanced utilization of substrates by enzyme mutants F103T and F103V makes them potentially useful for efforts to develop engineered organisms that catabolize lignin into biofuels or fine chemicals 1.14.11.13 gibberellin 2beta-dioxygenase biofuel production overexpression of GA2ox genes in switchgrass is a feasible strategy to improve plant architecture and reduce biomass recalcitrance for biofuel 1.14.14.91 trans-cinnamate 4-monooxygenase biofuel production lignocellulosic materials provide an attractive replacement for food-based crops used to produce ethanol. Understanding the interactions within the cell wall is vital to overcome the highly recalcitrant nature of biomass. One factor imparting plant cell wall recalcitrance is lignin, which can be manipulated by making changes in the lignin biosynthetic pathway. Eucalyptus trees with down-regulated cinnamate 4-hydroxylase (C4H) or p-coumaroyl quinate/shikimate 3'-hydroxylase (C3'H) expression display lowered overall lignin content. Lowering lignin content rather than altering sinapyl alcohol/coniferyl alcohol/4-coumaryl alcohol ratios is found to have the largest impact on reducing recalcitrance of the transgenic eucalyptus variants. The development of lower recalcitrance trees opens up the possibility of using alternative pretreatment strategies in biomass conversion processes that can reduce processing costs 1.14.14.96 5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase biofuel production lignocellulosic materials provide an attractive replacement for food-based crops used to produce ethanol. Understanding the interactions within the cell wall is vital to overcome the highly recalcitrant nature of biomass. One factor imparting plant cell wall recalcitrance is lignin, which can be manipulated by making changes in the lignin biosynthetic pathway. Eucalyptus trees with down-regulated cinnamate 4-hydroxylase (C4H) or p-coumaroyl quinate/shikimate 3'-hydroxylase (C3'H) expression display lowered overall lignin content. Lowering lignin content rather than altering sinapyl alcohol/coniferyl alcohol/4-coumaryl alcohol ratios is found to have the largest impact on reducing recalcitrance of the transgenic eucalyptus variants. The development of lower recalcitrance trees opens up the possibility of using alternative pretreatment strategies in biomass conversion processes that can reduce processing costs 1.14.19.2 stearoyl-[acyl-carrier-protein] 9-desaturase biofuel production biodiesel production 1.17.1.9 formate dehydrogenase biofuel production NAD+-dependent formate dehydrogenase is capable of the electrochemical reduction of carbon dioxide into formate, which can be ultimately converted to methanol. Enzyme secretion of formate dehydrogenase by yeast is a promising method for creating multi-enzyme devices for biofuel production 1.17.1.9 formate dehydrogenase biofuel production potential applications in NAD(H)-dependent industrial biocatalysis as well as in the production of renewable fuels and chemicals from carbon dioxide. Formate dehydrogenase from Myceliophthora thermophile possess a huge potential for CO2 reduction or NADH generation and under extreme alkaline conditions 2.1.1.246 [methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M methyltransferase biofuel production demonstration of an in vitro ability of MtaABC to produce methanol may ultimately enable the anaerobic oxidation of methane to produce methanol and from methanol alternative fuel or fuel-precursor molecules 2.3.1.8 phosphate acetyltransferase biofuel production proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol 2.3.1.9 acetyl-CoA C-acetyltransferase biofuel production the enzyme catalyses the condensation of two acetyl-coenzyme A molecules to form acetoacetyl-CoA in a dedicated pathway towards the biosynthesis of n-butanol, an important solvent and biofuel 2.3.1.20 diacylglycerol O-acyltransferase biofuel production combining the overexpression of TAG biosynthetic genes, DGAT1 and GPD1, appears to be a positive strategy to achieve a synergistic effect on the flux through the TAG synthesis pathway, and thereby further increase the oil yield of Camelina sativa, application of genetic engineering approaches to boost the metabolic flux of carbon into seed oils 2.3.1.20 diacylglycerol O-acyltransferase biofuel production DGAT1 is a target for genetic manipulation to increase seed oil production in oleaginous plants. Triacylglycerol produced by the enzyme can be a petrochemical alternative 2.3.1.20 diacylglycerol O-acyltransferase biofuel production PtWS/DGAT is a bifunctional enzyme and may serve as a promising target for the engineering of microalga-based oils and waxes for industrial use 2.3.1.20 diacylglycerol O-acyltransferase biofuel production Vernonia diacylglycerol acyltransferase can increase renewable oil production 2.3.1.86 fatty-acyl-CoA synthase system biofuel production Saccharomyces cerevisiae is engineered to produce fatty acid-derived biofuels and chemicals from simple sugars. All three primary genes involved in fatty acid biosynthesis, namely ACC1, FAS1 and FAS2 are overexpressed. Combining this metabolic engineering strategy with terminal converting enzymes (diacylglycerol-acyltransferase,fatty acyl-CoA thioesterase,fatty acyl-CoA reductase, and wax ester synthase for TAG,fatty acid, fatty alcohol and FAEE production, respectively) improves the production levels of all biofuel molecules and chemicals, Saccharomyces cerevisiae provides a compelling platform for a scalable, controllable and economic route to biofuel molecules and chemicals 2.3.1.180 beta-ketoacyl-[acyl-carrier-protein] synthase III biofuel production the enzyme is interesting in order to develop engineered high oil-yielding microalgal strains for biofuel production 2.3.1.217 curcumin synthase biofuel production incorporation of curcumin and phenylpentanoids into lignin has a positive effect on saccharification yield after alkaline pretreatment. To design a lignin that is easier to degrade under alkaline conditions, curcumin (diferuloylmethane) is produced in the model plant Arabidopsis thaliana via simultaneous expression of the turmeric genes diketide-CoA synthase (DCS) and curcumin synthase 2 (CURS2). The transgenic plants produce a plethora of curcumin- and phenylpentanoid-derived compounds with no negative impact on growth. Catalytic hydrogenolysis gives evidence that both curcumin and phenylpentanoids are incorporated into the lignifying cell wall, thereby significantly increasing saccharification efficiency after alkaline pretreatment of the transgenic lines by 14-24% as compared with the wild type 2.3.1.218 phenylpropanoylacetyl-CoA synthase biofuel production incorporation of curcumin and phenylpentanoids into lignin has a positive effect on saccharification yield after alkaline pretreatment. To design a lignin that is easier to degrade under alkaline conditions, curcumin (diferuloylmethane) is produced in the model plant Arabidopsis thaliana via simultaneous expression of the turmeric genes diketide-CoA synthase (DCS) and curcumin synthase 2 (CURS2). The transgenic plants produce a plethora of curcumin- and phenylpentanoid-derived compounds with no negative impact on growth. Catalytic hydrogenolysis gives evidence that both curcumin and phenylpentanoids are incorporated into the lignifying cell wall, thereby significantly increasing saccharification efficiency after alkaline pretreatment of the transgenic lines by 14-24% as compared with the wild type 2.3.3.21 (R)-citramalate synthase biofuel production advantage of the growth phenotype associated with 2-keto acid deficiency to construct a hyperproducer of 1-propanol and 1-butanol by evolving citramalate synthase (CimA) from Methanococcus jannaschii 2.4.1.14 sucrose-phosphate synthase biofuel production enzyme overexpression is used in molecular breeding of energy crops for optimizing yields of biomass and its utilization in second generation biofuel production 2.4.1.21 starch synthase (glycosyl-transferring) biofuel production transgenic Arabidopsis plants overexpressing the starch binding domains of starch synthase III have an advantage for the production of bioethanol in terms of saccharification of essential substrates 2.7.1.29 glycerone kinase biofuel production proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol 2.7.1.40 pyruvate kinase biofuel production proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol 2.7.2.3 phosphoglycerate kinase biofuel production proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol 2.8.4.1 coenzyme-B sulfoethylthiotransferase biofuel production CH4 is an important biofuel as well as a potential feedstock for the chemical industry if it can be converted by Mcr to a liquid biofuel with a high energy density 3.1.1.3 triacylglycerol lipase biofuel production conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel 3.1.1.3 triacylglycerol lipase biofuel production Candida rugosa lipase immobilized on hydrous niobium oxide to be used in the biodiesel synthesis 3.1.1.3 triacylglycerol lipase biofuel production lipase catalyzes biodiesel production using soybean oil and ethanol as substrates and pressurized n-propane as solvent 3.1.1.3 triacylglycerol lipase biofuel production LP326 catalyzes biodiesel production using methanol and various oils 3.1.1.3 triacylglycerol lipase biofuel production biodiesel production 3.1.1.72 acetylxylan esterase biofuel production significant increases in the depolymerisation of corn stover cellulose by cellobiohydrolase I (Cel7A) from Trichoderma reesei are observed using small quantities of purified endocylanase (XynA), ferulic acid esterase (FaeA), and acetyl xylan esterase (Axe1) 3.1.1.73 feruloyl esterase biofuel production Ferulic acid esterases effectively degrade corn fiber and release substantial amounts of ferulic acid and sugars (e.g., glucose and xylose) in the incubation medium. 3.1.1.73 feruloyl esterase biofuel production The biorefining of crop components, such as starch, grain fiber, and crop residues to fermentable substrates for the production of high-value products, such as ethanol and butanol, provides a source of renewable energy 3.1.1.117 (4-O-methyl)-D-glucuronate---lignin esterase biofuel production broad range of industrial applications for the biocatalytic processes of lignocellulose degradation and modification of lignocellulosic materials 3.1.1.117 (4-O-methyl)-D-glucuronate---lignin esterase biofuel production decomposition of wood polymers in biorefinery processes 3.1.1.117 (4-O-methyl)-D-glucuronate---lignin esterase biofuel production efficient and complete enzymatic degradation is an essential prerequisite in the utilization of lignocellulosic material for production of energy and value-added biorefinery products. Glucuronoyl esterase CE15 is a candidate for polishing lignin for residual carbohydrates to achieve pure, native lignin fractions after minimal pretreatment 3.1.1.117 (4-O-methyl)-D-glucuronate---lignin esterase biofuel production inclusion of glucuronoyl-esterases in the enzymatic digestion of lignocellulosic biomass 3.1.1.117 (4-O-methyl)-D-glucuronate---lignin esterase biofuel production the enzyme is a promising candidate as auxiliary enzymes to improve saccharification of plant biomass 3.1.1.117 (4-O-methyl)-D-glucuronate---lignin esterase biofuel production glucuronoyl esterase (GE) has potential for production of biofuels and biomaterials in lignocellulose biorefineries. GE cleaves alkali-labile bonds from the lignincarbohydrate complexes at acidic pH. Removal of glucuronic acid branches from the hemicellulose significantly improved release of fermentable sugars for biofuels production 3.1.3.11 fructose-bisphosphatase biofuel production enhancement of photosynthetic capacity in Euglena gracilis by expression of cyanobacterial fructose-1,6-/sedoheptulose-1,7-bisphosphatase leads to increases in biomass and wax ester production. This is the first step toward the utilization of Euglena gracilis as a sustainable source for biofuel production under photoautotrophic cultivation 3.1.3.37 sedoheptulose-bisphosphatase biofuel production engineered cyanobacteria with enhanced growth show increased ethanol production and higher biofuel to biomass ratio. Speeding up the Calvin-Benson-Bassham cycle theoretically has positive effects on the subsequent growth and/or the end metabolite(s) production. Four Calvin-Benson-Bassham cycle enzymes, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), fructose-1,6/sedoheptulose-1,7-bisphosphatase (FBP/SBPase), transketolase (TK) and aldolase (FBA) are selected to be cooverexpressed with the ethanol synthesis enzymes pyruvate decarboxylase (PDC) and alcohol dehydrogenase (ADH) in the cyanobacterium Synechocystis PCC 6803. An inducible promoter, PnrsB, is used to drive pyruvate decarboxylase and alcohol dehydrogenase expression. When PnrsB is induced and cells are cultivated at 0.065 mM photons/m*s, the RuBisCO-, FBP/SBPase-, TK-, and FBA-expressing strains produce 55%, 67%, 37% and 69% more ethanol and 7.7%, 15.1%, 8.8% and 10.1% more total biomass (the sum of dry cell weight and ethanol), respectively, compared to the strain only expressing the ethanol biosynthesis pathway. The ethanol to total biomass ratio is also increased in Calvin-Benson-Bassham cycle enzymes overexpressing strains. Using the cells with enhanced carbon fixation, when the product synthesis pathway is not the main bottleneck, can significantly increase the generation of a product (exemplified with ethanol), which acts as a carbon sink 3.2.1.1 alpha-amylase biofuel production the recombinant enzyme can be utilized for bioethanol production from jackfruit seed starch 3.2.1.3 glucan 1,4-alpha-glucosidase biofuel production the sake yeast strains constructed in this study are expected to produce bioethanol from starchy materials such as corn. Furthermore, to improve the efficiency of hydrolysis, a combination of sake yeast and various enzymes that cleave alpha-glucoside bonds shall be used 3.2.1.3 glucan 1,4-alpha-glucosidase biofuel production the secreted glucoamylase from Paenibacillus amylolyticus strain NEO03 possesses properties suitable for saccharification processes such as biofuel production 3.2.1.4 cellulase biofuel production the enzyme is a candidate for the utilization of agro-industrial waste for fuel production 3.2.1.4 cellulase biofuel production the enzyme is a tool for biomass conversion. The recombinant enzyme acts in high concentrations of ionic liquids and can therefore degrade alpha-cellulose or even complex cell wall preparations under those pretreatment conditions. The enzymatic conversion of lignocellulosic plant biomass into fermentable sugars is a crucial step in the production of biofuels 3.2.1.4 cellulase biofuel production bioethanol fermentation using agricultural wastes 3.2.1.4 cellulase biofuel production enzyme degrades carbohydrates of dried seaweed Ulva lactula. About 21 mg glucose/g of dry seaweed are obtained which can be further converted to bio-fuel 3.2.1.4 cellulase biofuel production recycling of enzymes during cellulosic bioethanol production in a pilotscale stripper. When increasing the temperature (up to 65°C) or ethanol content (up to 7.5% w/v), the denaturation rate of the enzymes increases. Enzyme denaturation occurs slower when the experiments are performed in fiber beer compared to buffer only. At extreme conditions with high temperature (65°C) and ethanol content (7.5% w/v), polythylenglycol added to fiber beer has no enzyme stabilizing effect 3.2.1.4 cellulase biofuel production potential of using the ionic liquids-tolerant extremophilic cellulases for hydrolysis of ionic liquids-pretreated lignocellulosic biomass, for biofuel production 3.2.1.4 cellulase biofuel production enzymatic cell wall degradation of microalgae for biofuel production: of the Chlorella strains tested, only Chlorella emersonii CCAP211/11N shows sensitivity to cellulase. As these effects of cellulase are minor, cellulose does not appear to play a major role in cell wall integrity or permeability in most of the algal species and strains tested 3.2.1.4 cellulase biofuel production its thermostability, resistance to heavy metal ions and specific activity make this enzyme an interesting candidate for industrial applications