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Screening of Microorganisms Producing Cold-Active Oxidoreductases to Be Applied in Enantioselective Alcohol Oxidation. An Antarctic Survey [PDF]

open access: goldMarine Drugs, 2011
Several microorganisms were isolated from soil/sediment samples of Antarctic Peninsula. The enrichment technique using (RS)-1-(phenyl)ethanol as a carbon source allowed us to isolate 232 psychrophile/psychrotroph microorganisms.
Leandro H. Andrade   +4 more
doaj   +6 more sources

Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase [PDF]

open access: goldBiomolecules, 2013
Enzymes of the non-conventional yeast Yarrowia lipolytica seem to be tailor-made for the conversion of lipophilic substrates. Herein, we cloned and overexpressed the Zn-dependent alcohol dehydrogenase ADH2 from Yarrowia lipolytica in Escherichia coli ...
Margit Winkler   +5 more
doaj   +7 more sources

Generation of Oxidoreductases with Dual Alcohol Dehydrogenase and Amine Dehydrogenase Activity [PDF]

open access: hybridChemistry – A European Journal, 2020
The l‐lysine‐ϵ‐dehydrogenase (LysEDH) from Geobacillus stearothermophilus naturally catalyzes the oxidative deamination of the ϵ‐amino group of l‐lysine.
Vasilis Tseliou   +4 more
semanticscholar   +7 more sources

Expanding the Application Range of Microbial Oxidoreductases by an Alcohol Dehydrogenase from Comamonas testosteroni with a Broad Substrate Spectrum and pH Profile [PDF]

open access: goldCatalysts, 2020
Alcohol dehydrogenases catalyse the conversion of a large variety of ketone substrates to the corresponding chiral products. Due to their high regio- and stereospecificity, they are key components in a wide range of industrial applications.
Daniel Bakonyi   +5 more
semanticscholar   +7 more sources

Nicotinoprotein [NAD(P)‐containing] alcohol/aldehyde oxidoreductases [PDF]

open access: bronzeEuropean Journal of Biochemistry, 1993
Extracts of Gram-positive bacteria like Rhodococcus rhodochrous, Rhodococcus erythropolis and Amycolatopsis methanolica, but not those of several Gram-negative ones, showed dehydrogenase activity for ethanol as well as for methanol when 4-nitroso-N,N ...
Peter W. Van Ophem   +2 more
semanticscholar   +6 more sources

Substrate diffusion and oxidation in GMC oxidoreductases: an experimental and computational study on fungal aryl-alcohol oxidase

open access: greenBiochemical Journal, 2011
AAO (aryl-alcohol oxidase) provides H₂O₂ in fungal degradation of lignin, a process of high biotechnological interest. The crystal structure of AAO does not show open access to the active site, where different aromatic alcohols are oxidized.
Aitor Hernández‐Ortega   +5 more
semanticscholar   +8 more sources

The GMC superfamily of oxidoreductases revisited: analysis and evolution of fungal GMC oxidoreductases

open access: yesBiotechnology for Biofuels, 2019
Background The glucose–methanol–choline (GMC) superfamily is a large and functionally diverse family of oxidoreductases that share a common structural fold.
Leander Sützl   +4 more
doaj   +2 more sources

Biofuel Cells Based on Oxidoreductases and Electroactive Nanomaterials: Development and Characterization [PDF]

open access: yesBiosensors
Amperometric biosensors (ABSs) and enzymatic biofuel cells (BFCs) share several fundamental principles in their functionality, despite serving different primary purposes.
Olha Demkiv   +5 more
doaj   +2 more sources

Structure of Alcohol Oxidase from Pichia pastoris by Cryo-Electron Microscopy. [PDF]

open access: yesPLoS ONE, 2016
The first step in methanol metabolism in methylotrophic yeasts, the oxidation of methanol and higher alcohols with molecular oxygen to formaldehyde and hydrogen peroxide, is catalysed by alcohol oxidase (AOX), a 600-kDa homo-octamer containing eight FAD ...
Janet Vonck   +2 more
doaj   +2 more sources

Core and auxiliary functions of one-carbon metabolism in Pseudomonas putida exposed by a systems-level analysis of transcriptional and physiological responses

open access: yesmSystems, 2023
The soil bacterium Pseudomonas putida is a robust biomanufacturing host that assimilates a broad range of substrates while efficiently coping with adverse environmental conditions. P. putida is equipped with functions related to one-carbon (C1) compounds
Justine Turlin   +4 more
doaj   +2 more sources

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