Results 181 to 190 of about 623,332 (218)
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Microbial Alcohol, Aldehyde and Formate Ester Oxidoreductases
Advances in Experimental Medicine and Biology, 1993Formation of alcohols by natural processes takes place in the fermentative breakdown of sugars and the oxidative dissimilation of alkanes. In view of the wide-spreadness of these processes, it is understandable that many microbial species have the capacity to degrade these compounds.
J A Duine +2 more
exaly +3 more sources
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.
Mirko Basen
exaly +3 more sources
BBA - Proteins and Proteomics, 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.
Angel T Martinez, Maria Jesus Martinez
exaly +3 more sources
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.
Angel T Martinez, Maria Jesus Martinez
exaly +3 more sources
Microbial Alcohol/Aldehyde Oxidoreductases in Enantioselective Conversions
1992Microbes have an enormous diversity of alcohol and aldehyde oxidoreductases. A brief overview is given of the types known and of some novel ones discovered recently. Except from the classical, NAD-dependent, alcohol dehydrogenase (the long chain, zinc-containing type, EC 1.1.1.1), these enzymes are unexplored with respect to enantioselectivity.
Arie Geerlof, J A Duine, J A Jongejan
exaly +2 more sources
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 ...
J Kulys, A Malinauskas
exaly +2 more sources
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 ...
J Kulys, A Malinauskas
exaly +2 more sources
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 ...
Michael Müller
exaly +2 more sources
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 ...
Michael Müller
exaly +2 more sources
Acta Crystallographica Section D: Biological Crystallography, 2009
Lignin biodegradation, a key step in carbon recycling in land ecosystems, is carried out by white-rot fungi through an H(2)O(2)-dependent process defined as enzymatic combustion. Pleurotus eryngii is a selective lignin-degrading fungus that produces H(2)O(2) during redox cycling of p-anisylic compounds involving the secreted flavoenzyme aryl-alcohol ...
Israel Fernández +2 more
exaly +3 more sources
Lignin biodegradation, a key step in carbon recycling in land ecosystems, is carried out by white-rot fungi through an H(2)O(2)-dependent process defined as enzymatic combustion. Pleurotus eryngii is a selective lignin-degrading fungus that produces H(2)O(2) during redox cycling of p-anisylic compounds involving the secreted flavoenzyme aryl-alcohol ...
Israel Fernández +2 more
exaly +3 more sources
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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Quinoprotein oxidoreductases for the oxidation of alcohols, sugars and amines
1994Quinoproteins are enzymes containing a quinone cofactor, that is the non-covalently bound PQQ or the protein-chain-integrated TPQ or TTQ. Quinoprotein dehydrogenases play a role in non-phosphorylative degradation of sugars, alcohols, aldehydes, ketones, and amines by Gram-negative bacteria, providing useful energy to the organism by their capacity to ...
J. A. Duine, J. A. Jongejan, S. de Vries
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