2.3.3.21 (R)-citramalate synthase energy production the citratmalate pathway is enhanced for the production of 1-propanol and 1-butanol 3.13.1.3 2'-hydroxybiphenyl-2-sulfinate desulfinase energy production the enzyme is useful in biodesulfurization, in which microorganisms selectively remove sulfur atoms from organosulfur compounds, a viable technology to complement the traditional hydrodesulfurization of fuels 1.1.1.1 alcohol dehydrogenase energy production preparation of a bioanode for use in ethanol oxidation. The bioanode is obtained via immobilization of dehydrogenase enzymes (alcohol dehydrogenase or aldehyde dehydrogenase) with polyamidoamine dendrimers onto carbon paper platforms, using the layer-by-layer technique. The prepared bioanode proves to be capable of producing good power density values 1.2.1.5 aldehyde dehydrogenase [NAD(P)+] energy production preparation of a bioanode for use in ethanol oxidation. The bioanode is obtained via immobilization of dehydrogenase enzymes (alcohol dehydrogenase or aldehyde dehydrogenase) with polyamidoamine dendrimers onto carbon paper platforms, using the layer-by-layer technique. The prepared bioanode proves to be capable of producing good power density values 3.2.1.1 alpha-amylase energy production design of a bioanode that directly utilizes starch as a fuel in an enzymatic biofuel cell. The enzymatic fuel cell is based on three enzymes (alpha-amylase, glucoamylase and glucose oxidase). The carbon paste electrode containing these three enzymes and tetrathiafulvalene can both saccharize and oxidize starchy biomass. In cyclic voltammetry, catalytic currents are successfully observed with both glucose and starchy white rice used as a substrate. A membraneless white rice/O2 biofuel cell is assembled and the electrochemical performance is evaluated. The three enzyme based electrode is used as a bioanode and an immobilized bilirubin oxidase (derived from Myrothecium verrucaria) electrode is used as a biocathode. The biofuel cell deliveres an open circuit voltage of 0.522 V and power density of up to 0.099 mW/cm 1.2.1.8 betaine-aldehyde dehydrogenase energy production the seed of the plant is the raw material for biodiesels 1.3.3.5 bilirubin oxidase energy production the BOD from Bacillus pumilus is an attractive candidate for application in biofuel cells and biosensors showing high activity at neutral pH and high tolerance towards NaCl 1.3.3.5 bilirubin oxidase energy production design of a bioanode that directly utilizes starch as a fuel in an enzymatic biofuel cell. The enzymatic fuel cell is based on three enzymes (alpha-amylase, glucoamylase and glucose oxidase). The carbon paste electrode containing these three enzymes and tetrathiafulvalene can both saccharize and oxidize starchy biomass. In cyclic voltammetry, catalytic currents are successfully observed with both glucose and starchy white rice used as a substrate. A membraneless white rice/O2 biofuel cell is assembled and the electrochemical performance is evaluated. The three enzyme based electrode is used as a bioanode and an immobilized bilirubin oxidase (derived from Myrothecium verrucaria) electrode is used as a biocathode. The biofuel cell delivers an open circuit voltage of 0.522 V and power density of up to 0.099 mW/cm 1.11.1.6 catalase energy production combination oflaccase and catalase in construction of H2O2-O2 based biocathode for applications in glucose biofuel cells. The deposited enzymes laccase and catalase by means of alternating current electrophoretic deposition (AC-EPD) do not inhibit each other and carry out about 90% of the catalytic reduction process of O2-H2O2 1.5.99.13 D-proline dehydrogenase energy production a bio-anode using L-glutamate as the fuel is constructed. To oxidize L-glutamate at the anode, glutamate dehydrogenase, derived from Pyrobaculum islandicum, and proline dehydrogenase derived from Pyrococcus horikoshii, are immobilized for a two-enzyme conjugate enzymatic and redox reaction. To achieve an efficient enzyme reaction and electron transfer, the immobilization ratio of proline dehydrogenase to glutamate dehydrogenase is controlled by varying the molar ratios of dithiobis succinimidyl undecanoate and nitrilotriacetic acid dihydrochloride 1.12.7.2 ferredoxin hydrogenase energy production novel hybrid system for H2 production using visible-light active GaN:ZnO coupled to active [FeFe]-hydrogenase from Escherichia coli (Hyd+ E. coli) overexpressing is developed, which shows the feasibility of being developed for photobiocatalytic H2 evolution under solar light 1.1.3.9 galactose oxidase energy production the enzyme is useful in fuel cells and the usage of biofuel cell with glucose 3.2.1.3 glucan 1,4-alpha-glucosidase energy production the enzyme is useful in fuel ethanol production, enzyme properties and performance, overview 3.2.1.3 glucan 1,4-alpha-glucosidase energy production design of a bioanode that directly utilizes starch as a fuel in an enzymatic biofuel cell. The enzymatic fuel cell is based on three enzymes (alpha-amylase, glucoamylase and glucose oxidase). The carbon paste electrode containing these three enzymes and tetrathiafulvalene can both saccharize and oxidize starchy biomass. In cyclic voltammetry, catalytic currents are successfully observed with both glucose and starchy white rice used as a substrate. A membraneless white rice/O2 biofuel cell is assembled and the electrochemical performance is evaluated. The three-enzyme-based electrode is used as a bioanode and an immobilized bilirubin oxidase (derived from Myrothecium verrucaria) electrode is used as a biocathode. The biofuel cell deliveres an open circuit voltage of 0.522 V and power density of up to 0.099 mW/cm 3.2.1.74 glucan 1,4-beta-glucosidase energy production ethanol production from concentrated agricultural waste corncob 1.1.1.47 glucose 1-dehydrogenase [NAD(P)+] energy production NAD(P)-dependent glucose dehydrogenases have high potential for use in various systems to generate electricity from biological sources for applications in implantable biomedical devices, wireless sensors, and portable electronic devices. Application in biosensors and biofuel cells. Challenges for successful implementation of biofuel cells include increasing the stability of NAD+ and NADP+, and improving the binding of these cofactors in the glucose dehydrogenase enzyme. State-of-the-art fuel cells containing NAD(P)+-dependent GDH usually need an additional unbound cofactor supply from the solution. If the cofactor could be encapsulated in a small volume close to the enzyme or connected via a small linker into the carrier matrix, its reoxidation could be facilitated. Such an encapsulation together with the enzyme could be more effective for improving the fuel cell efficiency relative to the direct electrode binding schemes. Replacing the original cofactor in the enzyme molecule with a modified nicotinamide cofactor analogue would also help to retain the enzyme activity and make the NAD+- and NADP+-dependent enzymes more attractive for applications in fuel cells and sensing devices 1.1.3.4 glucose oxidase energy production design of a bioanode that directly utilizes starch as a fuel in an enzymatic biofuel cell. The enzymatic fuel cell is based on three enzymes (alpha-amylase, glucoamylase and glucose oxidase). The carbon paste electrode containing these three enzymes and tetrathiafulvalene can both saccharize and oxidize starchy biomass. In cyclic voltammetry, catalytic currents are successfully observed with both glucose and starchy white rice used as a substrate. A membraneless white rice/O2 biofuel cell is assembled and the electrochemical performance is evaluated. The three enzyme based electrode is used as a bioanode and an immobilized bilirubin oxidase (derived from Myrothecium verrucaria) electrode is used as a biocathode. The biofuel cell deliveres an open circuit voltage of 0.522 V and power density of up to 0.099 mW/cm 1.1.3.4 glucose oxidase energy production enzyme precipitates coatings of glucose oxidase onto carbon paper for biofuel cell applications. The direct immobilization of enzyme precipitation coatings on hierarchical-structured electrodes with a large surface area can further improve the power density of enzymatic biofuel cells and can make their applications more feasible 1.1.3.4 glucose oxidase energy production glucose oxidase/cellulose-carbon nanotube composite paper as a biocompatible bioelectrode for biofuel cells. Glucose oxidase, which is a redox enzyme capable of oxidizing glucose as a renewable fuel using oxygen, is immobilized on the CL-CNT composite paper. Cyclic voltammograms reveal that the GOx/CL-CNT paper electrode shows a pair of well-defined peaks, which agreed well with that of FAD/FADH2, the redox center of glucose oxidase. These results clearly show that the direct electron transfer between the glucose oxidase and the composite electrode is achieved. It is found that the glucose oxidase immobilized on the composite electrode retains catalytic activity for the oxidation of glucose 1.1.3.4 glucose oxidase energy production mutant glucose oxidase (B11-GOx) is obtained from directed protein evolution and wild-type enzyme. Higher glucose oxidation currents are obtained from B11-GOx both in solution and polymer electrodes compared to wild type enzyme. Improved electrocatalytic activity towards electrochemical oxidation of glucose from the mutant enzyme. The enzyme electrode with the mutant enzyme B11-GOx shows a faster electron transfer indicating a better electronic interaction with the polymer mediator. Promising application of enzymes developed by directed evolution tailored for the applications of biosensors and biofuel cells 1.1.3.4 glucose oxidase energy production triphenylmethane dyes are an alternative for mediated electronic transfer systems in glucose oxidase biofuel cells 1.4.1.2 glutamate dehydrogenase energy production a bio-anode using L-glutamate as the fuel is constructed. To oxidize L-glutamate at the anode, glutamate dehydrogenase, derived from Pyrobaculum islandicum, and proline dehydrogenase derived from Pyrococcus horikoshii, are immobilized for a two-enzyme conjugate enzymatic and redox reaction. To achieve an efficient enzyme reaction and electron transfer, the immobilization ratio of proline dehydrogenase to glutamate dehydrogenase is controlled by varying the molar ratios of dithiobis succinimidyl undecanoate and nitrilotriacetic acid dihydrochloride 2.3.1.15 glycerol-3-phosphate 1-O-acyltransferase energy production the developed glycerol-3-phosphate acyltransferase model structure together with insights gained in the catalytic mechanism of the protein can serve as a valuable reference for biotechnological studies to optimize microalgal strains for enhanced biofuel production 1.12.1.3 hydrogen dehydrogenase (NADP+) energy production application in biofuel cells, to generate an electric current 1.10.3.2 laccase energy production combination oflaccase and catalase in construction of H2O2-O2 based biocathode for applications in glucose biofuel cells. The deposited enzymes laccase and catalase by means of alternating current electrophoretic deposition (AC-EPD) do not inhibit each other and carry out about 90% of the catalytic reduction process of O2-H2O2 1.10.3.2 laccase energy production molecular design of laccase cathode for direct electron transfer in a biofuel cell. Functionalized graphite electrodes with a substrate-like molecule, that can interact as ligand with the redox site of the protein, are able to orientate the coupling of laccase molecule with the electrode surface through the T1 site. This molecular orientation enhances the direct electron transfer between the T1 site and the graphite electrode surface. The molecular design of enzymatic electrodes seems to be a powerful tool for the optimization of enzyme-based fuel cells 1.10.3.2 laccase energy production a CotA mutant from Bacillus licheniformis, operating in basic media and seawater, is effective in catalyzing the bioelectrocatalytic O2 reduction, suggesting a prospective enzyme application for sustainable production of energy from seawater and oxygen 1.14.18.3 methane monooxygenase (particulate) energy production teh enzyme can be used as biocatalysts for industrial activation of methane at relatively low temperatures required for breaking the highly stable C-H bond(s) 1.14.13.25 methane monooxygenase (soluble) energy production teh enzyme can be used as biocatalysts for industrial activation of methane at relatively low temperatures required for breaking the highly stable C-H bond(s) 1.18.6.1 nitrogenase energy production the reaction produces H2 as a by-product and is interesting for production of clean energy 2.3.1.158 phospholipid:diacylglycerol acyltransferase energy production the strong lipase activity of PDAT with broad substrate specificity might be a potential biocatalyst for industrial lipid hydrolysis and conversion, particularly for biofuel production 1.1.3.10 pyranose oxidase energy production enzyme P2O has the potential to be useful for biofuel cell applications 1.1.99.35 soluble quinoprotein glucose dehydrogenase energy production a (PQQ)-GDH electrode is used as an anode to convert the chemical energy of D-glucose into electrical energy by oxidation of the substrate 1.12.98.4 sulfhydrogenase energy production development of economically feasible production system for hydrogen as an alternative energy source of the future. The not-mediated Pyrococcus furiosus sulfhydrogenase/TiO2 system represents a first optimization step towards the development of an economically feasible in vitro hydrogen production process which should be driven by solar light and should utilize waste compounds as source of electrons 3.13.1.1 UDP-sulfoquinovose synthase energy production the enzyme is useful in biodesulfurization, in which microorganisms selectively remove sulfur atoms from organosulfur compounds, a viable technology to complement the traditional hydrodesulfurization of fuels 5.3.1.5 xylose isomerase energy production bioethanol 5.3.1.5 xylose isomerase energy production engineering of Saccharomyces cerevisiae for alcoholic fermentation of D-xylose 5.3.1.5 xylose isomerase energy production engineering Saccharomyces cerevisiae for alcoholic fermentation of D-xylose 5.3.1.5 xylose isomerase energy production genetic engineering of Saccharomyces cerevisiae in order to increase ethanol production by fermentation of D-xylose 5.3.1.5 xylose isomerase energy production genetic engineering of the yeast Hansenula polymorpha in order to increase ethanol production by D-xylose fermentation 5.3.1.5 xylose isomerase energy production genetic engineering of Zymobacter palmae in order to produce ethanol from xylose fermentation