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- W2348804527 abstract "1,3-propanediol oxidoreductase from Klebsiella pneumoniae was purified by DEAE sepharose fast flow ion-exchange chromatography and Blue Sepharose CL-6B affinity chromatography under aerobic conditions.A 35.86-fold purification was obtained with the recovery of 5.17% activity.The optimum temperature and pH of the enzyme activity were 57 ℃ and 9.5 of pH value.At 30 ℃ and at range of pH 8.0～10.0,1,3-propanediol oxidoreductase was stable.At 45 ℃ and pH 9.5 the Km for 1,3-propanediol and NAD+ were 15.8 mmol·L-1 and 0.2 mmol·L-1,respectively.The enzyme oxidized other alcohols such as pentanol,propanol,ethylene glycol and 1,4-butanediol,besides physiological substrate 3-hydroxypropionaldehyde.The enzyme was significantly activated by Mn2+.Reducing agents were able to enhence the activity of 1,3-propanediol oxidoreductase." @default.
- W2348804527 created "2016-06-24" @default.
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- W2348804527 date "2009-01-01" @default.
- W2348804527 modified "2023-09-28" @default.
- W2348804527 title "Purification and Characterization of 1,3-Propanediol Oxidoreductase from Klebsiella pneumoniae" @default.
- W2348804527 hasPublicationYear "2009" @default.
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