Results 21 to 30 of about 1,029 (146)

Gene Mining and Flavour Metabolism Analyses of Wickerhamomyces anomalus Y-1 Isolated From a Chinese Liquor Fermentation Starter

open access: yesFrontiers in Microbiology, 2022
Luzhou-flavoured liquor is one of Chinese most popular distilled liquors. Hundreds of flavoured components have been detected from this liquor, with esters as its primary flavouring substance.
Xin Shi   +7 more
doaj   +1 more source

Purification of yeast alcohol dehydrogenase by using immobilized metal affinity cryogels [PDF]

open access: yes, 2013
In this study, poly(2-hydroxyethyl methacrylate-glycidylmethacrylate) [poly(HEMA-GMA)] cryogels were prepared by radical cryocopolymerization of HEMA with GMA as a functional comonomer and N,N'-methylene-bisacrylamide (MBAAm) as a crosslinker ...
Uygun, Deniz Aktas   +5 more
core   +1 more source

Substrate specificities of peroxisomal members of short-chain alcohol dehydrogenase superfamily: expression and characterization of dehydrogenase part of Candida tropicalismultifunctional enzyme

open access: yesJournal of Lipid Research, 2000
In addition to several other enzymes, the short-chain alcohol dehydrogenase superfamily includes a group of peroxisomal multifunctional enzymes involved in fatty acid and cholesterol side-chain β-oxidation.
Yong-Mei Qin   +2 more
doaj   +1 more source

Preparation of a highly active alcohol apo-dehydrogenase from yeast [PDF]

open access: yes, 1937
It is generally recognized that an active dehydrogenase system consists of three principal components: (1) an apo-dehydrogenase, the non-dializable and thermo-labile colloidal carrier, protein in nature; (2) a co-enzyme, crystalloidal and comparatively ...
Sreenivasaya, M.
core   +1 more source

Isomerization of an enzyme-coenzyme complex in yeast alcohol dehydrogenase-catalyzed reactions [PDF]

open access: yesJournal of the Serbian Chemical Society, 2003
In this work, all the rate constants in the kinetic mechanism of the yeast alcohol dehydrogenase-catalyzed oxidation of ethanol by NAD+, at pH 7.0, 25°C, have been estimated.
DRAGINJA PERICIN   +2 more
doaj  

In vitro yeast alcohol dehydrogenase enzyme inhibition assays for ten compounds that differentially inhibit growth of sdh2Δ mutant vs. WT yeast. [PDF]

open access: yes, 2013
In vitro yeast alcohol dehydrogenase enzyme inhibition assays for ten compounds that differentially inhibit growth of sdh2Δ mutant vs. WT yeast.
Mary Bundrick (381274)   +12 more
core   +1 more source

Genome and transcriptome analysis of the food-yeast Candida utilis. [PDF]

open access: yesPLoS ONE, 2012
The industrially important food-yeast Candida utilis is a Crabtree effect-negative yeast used to produce valuable chemicals and recombinant proteins. In the present study, we conducted whole genome sequencing and phylogenetic analysis of C. utilis, which
Yasuyuki Tomita   +4 more
doaj   +1 more source

The Primary Structure of Yeast Alcohol Dehydrogenase [PDF]

open access: yesEuropean Journal of Biochemistry, 1977
Eight different types of peptide mixtures from [14C]carboxymethylated yeast alcohol dehydrogenase were obtained using trypsin with or without prior maleylation of the substrate, chymotrypsin, pepsin, microbial proteases or CNBr. Each mixture was fractionated by exclusion chromatography and peptides were further purified on paper.
openaire   +2 more sources

Inhibition of Yeast Alcohol Dehydrogenase by Alkylating Agents [PDF]

open access: yesEuropean Journal of Biochemistry, 1968
1 The kinetic parameters for the irreversible inhibition of yeast alcohol dehydrogenase by iodoacetate, bromopyruvate and N-ethylmaleimide have been measured. 2 For iodoacetate and bromopyruvate, the rate of inhibition decreases with increasing pH. It is concluded that the reaction is promoted by a positive centre on the enzyme with a pKa value of
N, Rashed, B R, Rabin
openaire   +2 more sources

Resurrecting ancestral alcohol dehydrogenases from yeast [PDF]

open access: yesNature Genetics, 2005
Modern yeast living in fleshy fruits rapidly convert sugars into bulk ethanol through pyruvate. Pyruvate loses carbon dioxide to produce acetaldehyde, which is reduced by alcohol dehydrogenase 1 (Adh1) to ethanol, which accumulates. Yeast later consumes the accumulated ethanol, exploiting Adh2, an Adh1 homolog differing by 24 (of 348) amino acids.
J Michael, Thomson   +6 more
openaire   +2 more sources

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