Open AccessPurification and properties of a novel polyol dehydrogenase of bacterial origin
Author(s) -
Dhawale Motiram R.,
Kropinski Andrew M.,
Hay George W.,
Szarek Walter A.
Publication year - 1984
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1984.tb01365.x
Subject(s) - ribitol , nad+ kinase , sorbose , cofactor , enzyme , biochemistry , sephadex , dehydrogenase , polyol , xylitol , sorbitol , chemistry , bacteria , sodium azide , oxidoreductase , stereochemistry , biology , fermentation , organic chemistry , polyurethane , fructose , genetics
A bacterium, as yet unidentified, has been isolated from floor dust by direct selection on minimal agar using l ‐glucitol ( d ‐gulitol) as the sole carbon energy source. The bacterium possesses a constitutive enzyme which catalyzes the reaction: l ‐glucitol + NAD + → d ‐sorbose + NADH + H + . A new species of enzyme has been induced by l ‐arabinitol or ribitol, but not l ‐ or d ‐glucitol, and the induction is only partially counteracted by the glucose‐repression effect. The constitutive enzyme was purified by fractionation on Sephadex G‐200 gel and chromatography on DEAE Biogel A. The enzyme required NAD + , but not NADP + , as a cofactor. It oxidizes also ribitol, xylitol and l ‐arabinitol, but not d ‐arabinitol, lactitol or a variety of other commercially available alditols. The enzyme is not inhibited by 10 mM sodium azide but is totally inhibited by 0.1 mM potassium ferricyanide.