Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase [PDF]
Biomolecules, 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 +6 more sources
Screening of Microorganisms Producing Cold-Active Oxidoreductases to Be Applied in Enantioselective Alcohol Oxidation. An Antarctic Survey [PDF]
Marine 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
Generation of Oxidoreductases with Dual Alcohol Dehydrogenase and Amine Dehydrogenase Activity [PDF]
Chemistry - A European Journal, 2021 The l-lysine-ϵ-dehydrogenase (LysEDH) from Geobacillus stearothermophilus naturally catalyzes the oxidative deamination of the ϵ-amino group of l-lysine.
Vasilis Tseliou +2 more
exaly +7 more sources
Biofuel Cells Based on Oxidoreductases and Electroactive Nanomaterials: Development and Characterization [PDF]
BiosensorsAmperometric biosensors (ABSs) and enzymatic biofuel cells (BFCs) share several fundamental principles in their functionality, despite serving different primary purposes.
Olha Demkiv +5 more
doaj +3 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.
Werner Hummel, Michael Müller
exaly +3 more sources
Iron-Containing Alcohol Dehydrogenase from Hyperthermophiles [PDF]
BioTechIron-containing alcohol dehydrogenases (Fe-ADHs) from hyperthermophiles represent a distinct class of oxidoreductases characterized by exceptional thermostability, catalytic versatility, and unique metal-dependent properties.
Ching Tse, Kesen Ma
doaj +2 more sources
Biotechnology 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
Engineering a newly identified alcohol dehydrogenase from Sphingobium Sp. for efficient utilization of nicotinamide cofactors biomimetics [PDF]
Bioresources and BioprocessingNicotinamide cofactor biomimetics (NCBs) serve as low-cost alternatives to the expensive NAD(P)+/NAD(P)H, holding significant potential for applications in oxidoreductases. In this study, an alcohol dehydrogenase (SpADH2) from Sphingobium sp.
Yichun Zhu +5 more
doaj +2 more sources
Substrate specificity mapping of fungal CAZy AA3_2 oxidoreductases
Biotechnology for Biofuels and BioproductsBackground Oxidative enzymes targeting lignocellulosic substrates are presently classified into various auxiliary activity (AA) families within the carbohydrate-active enzyme (CAZy) database.
Hongbo Zhao +9 more
doaj +2 more sources
Display of Bombyx mori alcohol dehydrogenases on the Bacillus subtilis spore surface to enhance enzymatic activity under adverse conditions. [PDF]
PLoS ONE, 2011 Alcohol dehydrogenases (ADHs) are oxidoreductases catalyzing the reversible oxidation of alcohols to corresponding aldehydes or ketones accompanied by nicotinamide adenine dinucleotide (NAD) or nicotinamide adenine dinucleotide phosphate (NADP) as ...
Nan Wang +6 more
doaj +2 more sources