The cells of Bacillus stearothermophilus contain an NADH-dependent diacetyl (acetoin) reductase. The enzyme was easily purified to homogeinity, partially cahracterized, and found to be composed of two subunits with thw same molecular weight. In the presence of NADH, it catalyses the stereospecific reduction of diacetyl first to 3S-acetoin and then to 2S,3S-butanediol; in the presence of NAD+, it catalyses the oxidation of 2S,3S- and meso-butanediol, respectively, to 3S-acetoin and 3R-acetoin, but is unable to oxidise these compounds to diacetyl.
Properties of a diacetyl (acetoin) reductase from Bacillus stearothermophilus
GIOVANNINI, Pier Paolo;MEDICI, Alessandro;RIPPA, Mario
1996
Abstract
The cells of Bacillus stearothermophilus contain an NADH-dependent diacetyl (acetoin) reductase. The enzyme was easily purified to homogeinity, partially cahracterized, and found to be composed of two subunits with thw same molecular weight. In the presence of NADH, it catalyses the stereospecific reduction of diacetyl first to 3S-acetoin and then to 2S,3S-butanediol; in the presence of NAD+, it catalyses the oxidation of 2S,3S- and meso-butanediol, respectively, to 3S-acetoin and 3R-acetoin, but is unable to oxidise these compounds to diacetyl.File in questo prodotto:
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