EC Number   |
Recommended Name |
Application |
|---|
    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 |
| 1.1.1.383 | 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 |
| 1.1.5.9 | 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 |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
biofuel production |
a tailored enzymatic cocktail of alpha-glucuronidase (Agu115) from Schizophyllum commune with alpha-L-arabinofuranosidase (AbfA), xylanase (Xyn10C) and beta-xylosidase (XynB) achieves efficient hydrolysis of softwood xylans, which is instrumental for material- and cost-efficient processes for the generation of biofuels from lignocellulose-based streams. Cooperative enzymatic activities have important significance for enhancing the release of fermentable sugars and therefore generate an attractive sugar platform from lignocellulosic biomass to produce products such as bioethanol by fermentation, and for the production of hemicellulosic polymers and oligosaccharides with tailored molecular structures for material applications |
| 3.2.1.55 | non-reducing end alpha-L-arabinofuranosidase |
biofuel production |
a tailored enzymatic cocktail of alpha-glucuronidase (Agu115) from Schizophyllum commune with alpha-L-arabinofuranosidase (AbfA), xylanase (Xyn10C) and beta-xylosidase (XynB) achieves efficient hydrolysis of softwood xylans, which is instrumental for material- and cost-efficient processes for the generation of biofuels from lignocellulose-based streams. Cooperative enzymatic activities have important significance for enhancing the release of fermentable sugars and therefore generate an attractive sugar platform from lignocellulosic biomass to produce products such as bioethanol by fermentation, and for the production of hemicellulosic polymers and oligosaccharides with tailored molecular structures for material applications |
| 3.2.1.131 | xylan alpha-1,2-glucuronosidase |
biofuel production |
a tailored enzymatic cocktail of alpha-glucuronidase (Agu115) from Schizophyllum commune with alpha-L-arabinofuranosidase (AbfA), xylanase (Xyn10C) and beta-xylosidase (XynB) achieves efficient hydrolysis of softwood xylans. This is instrumental for material- and cost-efficient processes for the generation of biofuels from lignocellulose-based streams. Cooperative enzymatic activities have important significance for enhancing the release of fermentable sugars and therefore generate an attractive sugar platform from lignocellulosic biomass to produce products such as bioethanol by fermentation, and for the production of hemicellulosic polymers and oligosaccharides with tailored molecular structures for material applications |
| 4.2.3.57 | (-)-beta-caryophyllene synthase |
biofuel production |
acute demand for high-density fuels has provided the impetus to pursue biosynthetic methods to produce b-caryophyllene from reproducible sources. Contribution by recombinant production of beta-caryophyllene by assembling a biosynthetic pathway in an engineered Escherichia coli strain |
| 4.2.3.89 | (+)-beta-caryophyllene synthase |
biofuel production |
acute demand for high-density fuels has provided the impetus to pursue biosynthetic methods to produce b-caryophyllene from reproducible sources. Contribution by recombinant production of beta-caryophyllene by assembling a biosynthetic pathway in an engineered Escherichia coli strain |
| 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 |
| 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 |
| 4.2.2.3 | mannuronate-specific alginate lyase |
biofuel production |
Alg17C can be used as the key enzyme to produce alginate monomers in the process of utilizing alginate for biofuels and chemicals production |
| 4.2.2.11 | guluronate-specific alginate lyase |
biofuel production |
Alg17C can be used as the key enzyme to produce alginate monomers in the process of utilizing alginate for biofuels and chemicals production |
| 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 |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
biofuel production |
application of this recombinant beta-xylosidase together with xylanase improves xylan hydrolysis efficiency, thus leading to increased biofuels productivity |
| 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 |
| 1.1.99.18 | 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 |
| 3.2.1.21 | beta-glucosidase |
biofuel production |
biodegradation of lignocellulosic biomass involves a concerted attack by several enzymes, including beta-glucosidases as key component. Current methodologies for biomass conversion to biofuels employ physical and/or chemical pretreatments that disrupt the lignocellulosic biomass in plant cell walls in combination with enzymatic hydrolysis of the cellulose to produce free sugars. Thus, stable cellulolytic enzymes with high enzymatic activity in pretreatment biomass conditions, including high temperatures and acidic conditions, are essential at an industrial scale production. These two features makes beta-glucosidase TpBGL1 to be of significant biotechnological interest |
| 3.2.1.21 | beta-glucosidase |
biofuel production |
biodegradation of lignocellulosic biomass involves a concerted attack by several enzymes, including beta-glucosidases as key component. Current methodologies for biomass conversion to biofuels employ physical and/or chemical pretreatments that disrupt the lignocellulosic biomass in plant cell walls in combination with enzymatic hydrolysis of the cellulose to produce free sugars. Thus, stable cellulolytic enzymes with high enzymatic activity in pretreatment biomass conditions, including high temperatures and acidic conditions, are essential at an industrial scale production. These two features makes beta-glucosidase TpBGL3 to be of significant biotechnological interest |
| 1.14.19.2 | stearoyl-[acyl-carrier-protein] 9-desaturase |
biofuel production |
biodiesel production |
| 3.1.1.3 | triacylglycerol lipase |
biofuel production |
biodiesel production |
| 3.2.1.4 | cellulase |
biofuel production |
bioethanol fermentation using agricultural wastes |
| 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 |
| 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 |
| 3.1.1.3 | triacylglycerol lipase |
biofuel production |
Candida rugosa lipase immobilized on hydrous niobium oxide to be used in the biodiesel synthesis |
| 3.2.1.91 | cellulose 1,4-beta-cellobiosidase (non-reducing end) |
biofuel production |
cellulose hydrolysis is an important step in the production of bioethanol from cellulosic biomass. Two key cellulase enzymes, celB from Caldicellulosiruptor saccharolyticus and beta-glucosidase, are covalently immobilised on polystyrene treated with plasma immersion ion implantation (PIII) which creates radicals that form covalent bonds. The immobilized enzymes are used to produce glucose from carboxymethyl cellulose (CMC), a solubilised form of cellulose. The highest activity of the immobilised celB on PIII treated surfaces was achieved when their immobilisation is carried out at a pH in the range 5-6.5. The immobilized celB on the PIII treated surface had the same activation energy as free celB showing substrate accessibility is not affected by the presence of the surface. The Vmax and Km values of immobilized celB are comparable to those of equal free celB concentrations. The areal density of immobilized celB on the PIII treated surface is estimated to be 0.0003 mg/cm2. The polystyrene surface with immobilized celB at 45°C can be reused over four times (23 hours each) with approximately 30% total activity loss. High ratios of beta-glucosidase to celB enhance the activity of immobilized celB for hydrolysis of carboxymethyl cellulose |
| 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 |
| 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 |
| 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 |
| 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 |
| 1.1.5.2 | 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 |
| 1.10.3.2 | 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 |
| 3.1.1.3 | triacylglycerol lipase |
biofuel production |
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel |
| 3.2.1.99 | arabinan endo-1,5-alpha-L-arabinanase |
biofuel production |
conversion of lignocellulosic biomass to biofuels. Endo-1,5-alpha-L-arabinanase hydrolyzes alpha-1,5-arabinofuranosidic bonds in hemicelluloses such as arabinoxylan and arabinan as well as in other arabinose-containing polysaccharides |
| 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 |
| 3.1.1.117 | (4-O-methyl)-D-glucuronate---lignin esterase |
biofuel production |
decomposition of wood polymers in biorefinery processes |
| 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 |
| 2.3.1.20 | 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 |
| 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 |
| 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 |
| 3.1.3.37 | 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 |
| 4.1.1.39 | ribulose-bisphosphate carboxylase |
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 decarboxylaseC 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 |
| 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 |
| 1.13.11.8 | 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 |
| 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 |
| 3.2.1.4 | 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 |
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 |
| 4.1.1.33 | diphosphomevalonate decarboxylase |
biofuel production |
enzyme establishes a possible route for biological production of petroleum based fuels and plastics by producing isobutene enzymatically |
| 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 |
| 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) |
| 1.2.1.10 | 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) |
| 1.1.1.1 | 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 |
| 1.2.1.10 | 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) |
| 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. |
| 7.6.2.2 | ABC-type xenobiotic transporter |
biofuel production |
gene overexpression in industrial yeast strains improves the alcoholic fermentation performance for sustainable bio-ethanol production |
| 1.1.3.4 | glucose oxidase |
biofuel production |
glucose oxidase is typically used in the anode of biofuel cells to oxidise glucose |
| 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 |
| 3.1.1.117 | (4-O-methyl)-D-glucuronate---lignin esterase |
biofuel production |
inclusion of glucuronoyl-esterases in the enzymatic digestion of lignocellulosic biomass |
| 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 |
| 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 |
| 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 |
| 1.1.99.18 | cellobiose dehydrogenase (acceptor) |
biofuel production |
key enzyme in biofuel cells |
| 1.10.3.2 | laccase |
biofuel production |
lignin degradation of agricultural biomass for biofuel production |
| 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 |
| 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 |
| 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 |
| 3.1.1.3 | triacylglycerol lipase |
biofuel production |
LP326 catalyzes biodiesel production using methanol and various oils |
| 1.11.1.13 | manganese peroxidase |
biofuel production |
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels |
| 1.17.1.9 | 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 |
| 1.14.11.13 | 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 |
| 4.1.2.9 | phosphoketolase |
biofuel production |
overexpression of the PktB isoform leads to a 2fold increase in intracellular acetyl-CoA concentration, and a 2.6fold yield enhancement from methane to microbial biomass and lipids compared to wild-type, increasing the potential for methanotroph lipid-based fuel 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 |
| 3.2.1.8 | endo-1,4-beta-xylanase |
biofuel production |
potential applications on biofuels and paper industries |
| 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 |
| 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 |
| 3.2.1.8 | endo-1,4-beta-xylanase |
biofuel production |
pre-treatment for ethanol formation from lignin-cellulose fibres more efficiently |
| 3.2.1.136 | glucuronoarabinoxylan endo-1,4-beta-xylanase |
biofuel production |
pre-treatment for ethanol formation from lignin-cellulose fibres more efficiently |
| 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 |
| 1.1.1.6 | 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 |
| 1.2.1.10 | 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 |
| 1.2.7.1 | 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 |
| 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 |
| 2.7.1.29 | 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 |
| 4.2.1.11 | phosphopyruvate hydratase |
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 |
| 5.3.1.1 | triose-phosphate isomerase |
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 |
| 5.4.2.11 | phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) |
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 |
| 2.3.1.20 | 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 |
| 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 |
| 1.1.3.10 | 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 |
| 1.1.1.383 | 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 |
| 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 |
| 3.2.1.8 | endo-1,4-beta-xylanase |
biofuel production |
RuCelA can produce xylo-oligosaccharides and cell-oligosaccharides in the continuous saccharification of pretreated rice straw, which can be further degraded into fermentable sugars. Therefor, the bifunctional RuCelA distinguishes itself as an ideal candidate for industrial application |
| 3.2.1.73 | licheninase |
biofuel production |
RuCelA can produce xylo-oligosaccharides and cell-oligosaccharides in the continuous saccharification of pretreated rice straw, which can be further degraded into fermentable sugars. Therefor, the bifunctional RuCelA distinguishes itself as an ideal candidate for industrial application |
| 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 |
| 6.4.1.2 | acetyl-CoA carboxylase |
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 |
