EC Number   |
Recommended Name |
Application |
|---|
    3.2.1.4 | cellulase |
biofuel production |
the enzyme can be useful for production of bioethanol and biofuel |
| 3.2.1.4 | cellulase |
biofuel production |
the fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus has great potential in generating fermentable sugars from renewable agro-residues for biofuel and fine chemical industry. Application of the fusion enzyme (EG-M-Xyn)in combination with Ctec2 (commercial enzyme) in the saccharification leads to a 10-20% net increase in fermentable sugars liberated from pretreated rice straw in comparison to the Ctec2 alone |
| 3.2.1.8 | endo-1,4-beta-xylanase |
biofuel production |
pre-treatment for ethanol formation from lignin-cellulose fibres more efficiently |
| 3.2.1.8 | 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 |
| 3.2.1.8 | endo-1,4-beta-xylanase |
biofuel production |
the enzyme is a candidate for the utilization of agro-industrial waste for fuel production |
| 3.2.1.8 | endo-1,4-beta-xylanase |
biofuel production |
potential applications on biofuels and paper industries |
| 3.2.1.8 | endo-1,4-beta-xylanase |
biofuel production |
the fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus has great potential in generating fermentable sugars from renewable agro-residues for biofuel and fine chemical industry. Application of the fusion enzyme (EG-M-Xyn)in combination with Ctec2 (commercial enzyme) in the saccharification leads to a 10-20% net increase in fermentable sugars liberated from pretreated rice straw in comparison to the Ctec2 alone |
| 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 |
| 3.2.1.21 | beta-glucosidase |
biofuel production |
the saccharification yield of rice straw using Trichoderma reesei cellulase is improved by the addition of MeBglD2. These results show that MeBglD2 can be used to improve plant biomass saccharification, because both substrates and products can activate its enzymatic activity |
| 3.2.1.23 | beta-galactosidase |
biofuel production |
the saccharification yield of rice straw using Trichoderma reesei cellulase is improved by the addition of MeBglD2. These results show that MeBglD2 can be used to improve plant biomass saccharification, because both substrates and products can activate its enzymatic activity |
| 3.2.1.26 | beta-fructofuranosidase |
biofuel production |
the expression of INVA and INVB from Zymomonas mobilis in Pichia pastoris yields new catalysts with improved catalytic properties, making them suitable candidates for ethanol production from cane molasses |
| 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 |
| 3.2.1.37 | 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 |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
biofuel production |
the beta-xylosidase when combined with xylanase shows positive effect on xylan hydrolysis. The higher amount of glucose and xylose generated from sugarcane bagasse hydrolysis using the commercial cocktail Multifect CL supplemented with beta-xylosidase demonstrates that this enzyme has potential to be used as a supplement for commercial cocktails to improve the yield of xylose and glucose release, and this is of great importance for the production of second generation ethanol |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
biofuel production |
the enzyme has great potential for applications in the bioconversion of lignocellulose to sugars, fuel ethanol and chemicals |
| 3.2.1.37 | xylan 1,4-beta-xylosidase |
biofuel production |
the relatively broad pH profile is favourable for industrial application as it offers potential flexibility in terms of process pH and is in line with the current pH range of lignocellulose enzymatic hydrolysis processes for bioethanol production |
| 3.2.1.38 | beta-D-fucosidase |
biofuel production |
the saccharification yield of rice straw using Trichoderma reesei cellulase is improved by the addition of MeBglD2. These results show that MeBglD2 can be used to improve plant biomass saccharification, because both substrates and products can activate its enzymatic activity |
| 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 |
| 3.2.1.73 | 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 |
| 3.2.1.74 | glucan 1,4-beta-glucosidase |
biofuel production |
the enzyme can be used for hydrolysis of cellulosic and hemicellulosic biomass substrates for biofuel production |
| 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 |
| 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 |
| 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 |
| 3.2.1.136 | glucuronoarabinoxylan endo-1,4-beta-xylanase |
biofuel production |
pre-treatment for ethanol formation from lignin-cellulose fibres more efficiently |
| 3.2.1.176 | cellulose 1,4-beta-cellobiosidase (reducing end) |
biofuel production |
successful expression of a chimeric cellobiohydrolase I with essentially full native activity in Yarrowia lipolytica. Yarrowia lipolytica strains can be genetically engineered, ultimately by heterologous expression of fungal cellulases and other enzymes, to directly convert lignocellulosic substrates to biofuels |
| 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 |
| 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 |
| 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 |
| 4.1.99.5 | aldehyde oxygenase (deformylating) |
biofuel production |
the conversion of long-chain fatty aldehydes to corresponding alkanes, that is catalyzed by cyanobacterial aldehyde-deformylating oxygenase (cADO), is probably useful for production of biofuel |
| 4.1.99.5 | aldehyde oxygenase (deformylating) |
biofuel production |
the cyanobacterial aldehyde deformylating oxygenase (cADO) is a key enzyme that catalyzes the unusual deformylation of aliphatic aldehydes for alkane biosynthesis and can be applied to the production of biofuel in vitro and in vivo |
| 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 |
| 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 |
| 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 |
| 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 |
| 5.4.99.13 | isobutyryl-CoA mutase |
biofuel production |
the production of isobutanol, a branched-chain alcohol that can be used as a gasoline substitute, using a CoA-dependent pathway in recombinant Ralstonia eutropha strain H16. The designed pathway involves isobutyryl-CoA mutase activity. The engineered strain produces about 30 mg/l isobutanol from fructose |
| 6.2.1.20 | long-chain-fatty-acid-[acyl-carrier-protein] ligase |
biofuel production |
the enzyme might be useful for biofuel production using cyanobacteria |
| 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 |
| 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 |
