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Search term: biofuel production

Results 1 - 90 of 90
EC Number
Application
Commentary
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)
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
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
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
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
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
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
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
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
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
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
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
glucose oxidase
biofuel production
glucose oxidase is typically used in the anode of biofuel cells to oxidise glucose
glucose oxidase
biofuel production
used in miniature membrane-less glucose/O2 biofuel cells
glucose oxidase
biofuel production
the enzyme used for biofuel cells
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
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
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
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
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
glucose 1-dehydrogenase (FAD, quinone)
biofuel production
use as anode enzyme in biofuel cells
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)
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
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)
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
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
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
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
laccase
biofuel production
lignin degradation of agricultural biomass for biofuel production
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
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
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
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
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
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
stearoyl-[acyl-carrier-protein] 9-desaturase
biofuel production
biodiesel production
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
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
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
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
fatty-acyl-CoA synthase
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
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
(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
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
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
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
triacylglycerol lipase
biofuel production
Candida rugosa lipase immobilized on hydrous niobium oxide to be used in the biodiesel synthesis
triacylglycerol lipase
biofuel production
lipase catalyzes biodiesel production using soybean oil and ethanol as substrates and pressurized n-propane as solvent
triacylglycerol lipase
biofuel production
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
triacylglycerol lipase
biofuel production
biodiesel production
triacylglycerol lipase
biofuel production
LP326 catalyzes biodiesel production using methanol and various oils
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)
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.
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
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
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
cellulase
biofuel production
recycling of enzymes during cellulosic bioethanol production in a pilotscale stripper. When increasing the temperature (up to 65C) 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 (65C) and ethanol content (7.5% w/v), polythylenglycol added to fiber beer has no enzyme stabilizing effect
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
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
cellulase
biofuel production
bioethanol fermentation using agricultural wastes
cellulase
biofuel production
potential of using the ionic liquids-tolerant extremophilic cellulases for hydrolysis of ionic liquids-pretreated lignocellulosic biomass, for biofuel production
cellulase
biofuel production
the enzyme is a candidate for the utilization of agro-industrial waste for fuel production
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
cellulase
biofuel production
its thermostability, resistance to heavy metal ions and specific activity make this enzyme an interesting candidate for industrial applications
endo-1,4-beta-xylanase
biofuel production
pre-treatment for ethanol formation from lignin-cellulose fibres more efficiently
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
endo-1,4-beta-xylanase
biofuel production
the enzyme is a candidate for the utilization of agro-industrial waste for fuel production
endo-1,4-beta-xylanase
biofuel production
potential applications on biofuels and paper industries
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; 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
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
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 45C 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
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
glucuronoarabinoxylan endo-1,4-beta-xylanase
biofuel production
pre-treatment for ethanol formation from lignin-cellulose fibres more efficiently
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
diphosphomevalonate decarboxylase
biofuel production
enzyme establishes a possible route for biological production of petroleum based fuels and plastics by producing isobutene enzymatically
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
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
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
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
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
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
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
(-)-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
(+)-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
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
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; 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
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
long-chain-fatty-acid-[acyl-carrier-protein] ligase
biofuel production
the enzyme might be useful for biofuel production using cyanobacteria
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
ABC-type xenobiotic transporter
biofuel production
gene overexpression in industrial yeast strains improves the alcoholic fermentation performance for sustainable bio-ethanol production
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