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Search term: biofuel production

Results 1 - 43 of 43
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
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
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
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 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
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
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)
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
stearoyl-[acyl-carrier-protein] 9-desaturase
biofuel production
biodiesel production
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
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
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
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 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
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
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
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
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
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
glucuronoarabinoxylan endo-1,4-beta-xylanase
biofuel production
pre-treatment for ethanol formation from lignin-cellulose fibres more efficiently
xenobiotic-transporting ATPase
biofuel production
gene overexpression in industrial yeast strains improves the alcoholic fermentation performance for sustainable bio-ethanol production
diphosphomevalonate decarboxylase
biofuel production
enzyme establishes a possible route for biological production of petroleum based fuels and plastics by producing isobutene enzymatically
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
Results 1 - 43 of 43