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Carbon-monoxide-driven bioethanol production operates through a tungsten-dependent catalyst. [PDF]
Nat Chem BiolLemaire ON +3 more
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Yeast Alcohol NAD-Oxidoreductaseに対する有機塩基及びNucleotidesの影響
Yeast Alcohol NAD-Oxidoreductaseに対する有機塩基及びNucleotidesの影響openaire
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The emerging role of aldehyde:ferredoxin oxidoreductases in microbially-catalyzed alcohol production
Journal of Biotechnology, 2019The development of a bio-refinery industry based on liquid fuels is presumably key to successful replacement of fossil fuels and a reduction of carbon dioxide (CO2) emissions. Ethanol and longer-chain alcohols are supposed to play a key role since they are relatively easy to produce, using microorganisms as whole-cell biocatalysts.
Laura Sofie Nissen, Mirko Basen
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Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
Aryl-alcohol oxidase (AAO), an FAD-dependent enzyme involved in lignin degradation, has been cloned from Pleurotus eryngii. The AAO protein is composed of 593 amino acids, 27 of which form a signal peptide. It shows 33% sequence identity with glucose oxidase from Aspergillus niger and lower homology with other oxidoreductases.
E, Varela +2 more
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Aryl-alcohol oxidase (AAO), an FAD-dependent enzyme involved in lignin degradation, has been cloned from Pleurotus eryngii. The AAO protein is composed of 593 amino acids, 27 of which form a signal peptide. It shows 33% sequence identity with glucose oxidase from Aspergillus niger and lower homology with other oxidoreductases.
E, Varela +2 more
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Analytica Chimica Acta, 1978
Flowthrough enzyme electrodes are reported for determinations of alcohol, lactate and glutamate. Oxidoreductases mixed with immobilized NAD+ cofactor are held between a suitable platinum electrode and a semipermeable membrane. The coenzyme is readily regenerated either directly by electrochemical oxidation or by using phenazine methosulphate (PMS+) as ...
A. Malinauskas, J. Kulys
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Flowthrough enzyme electrodes are reported for determinations of alcohol, lactate and glutamate. Oxidoreductases mixed with immobilized NAD+ cofactor are held between a suitable platinum electrode and a semipermeable membrane. The coenzyme is readily regenerated either directly by electrochemical oxidation or by using phenazine methosulphate (PMS+) as ...
A. Malinauskas, J. Kulys
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European Journal of Organic Chemistry, 2001
The oxidoreductases Lactobacillus brevis alcohol dehydrogenase (LBADH) and Candida parapsilosis carbonyl reductase (CPCR) are suitable catalysts for the reduction of ketones to afford enantiopure sec. alcohols. A broad variety of alkynones (1, 3, and 5) are accepted as substrates and the corresponding propargylic alcohols (2, 4, and 6) are obtained in ...
Schubert, Thomas +3 more
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The oxidoreductases Lactobacillus brevis alcohol dehydrogenase (LBADH) and Candida parapsilosis carbonyl reductase (CPCR) are suitable catalysts for the reduction of ketones to afford enantiopure sec. alcohols. A broad variety of alkynones (1, 3, and 5) are accepted as substrates and the corresponding propargylic alcohols (2, 4, and 6) are obtained in ...
Schubert, Thomas +3 more
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Nicotinoprotein Alcohol/Aldehyde Oxidoreductases
Advances in experimental medicine and biology, 1996Enzymes with tightly bound NAD(P), acting as cofactor, have been described in the past. Well known examples include UDP-galactose 4-epimerase from E. coli (Wilson and Hogness, 1964) and lactate-oxaloacetate transhydrogenase from V. alcalescens (Allen, 1966).
Sander R. Piersma +2 more
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Coupled oxidoreductase activity of horse liver alcohol dehydrogenase
Archives of Biochemistry and Biophysics, 1972Abstract Two assay procedures were used to study ethanol oxidation by crystalline horse liver alcohol dehydrogenase: (A) Acetaldehyde formed by ethanol oxidation (with and without lactaldehyde) was distilled into a semicarbazide solution and the absorbance of the acetaldehyde semicarbazone formed was measured at 224 nm.
C L, Woodley, N K, Gupta
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Sugar oxidoreductases and veratryl alcohol oxidase as related to lignin degradation
Journal of Biotechnology, 1997Properties of cellobiose:quinone oxidoreductase (CBQ), cellobiose dehydrogenase (CDH), glyoxal oxidase (GLOX), glucose oxidases and veratryl alcohol oxidase (VAO) are reviewed. There is strong evidence that CDH reduces quinones, phenoxy and cation radicals.
P. Ander, MARZULLO, Liberato
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