[Kinetic studies on long-chain alcohol turnover by yeast alcohol dehydrogenase within the transition from real solution to emulsion or suspension].
作者信息
Schöpp W, Rothe U
出版信息
Acta Biol Med Ger. 1975;34(2):197-201.
PMID:1154946
Abstract
The enzymatic oxidation of hexanol, decanol, and tetradecanol by yeast alcohol dehydrogenase was studied. The enzyme was found to catalyze not only conversion in the real aqueous solution of the substrates, but also at the surface of undissolved substrate particles. The kinetic parameters varied on transition from the real solution to dispersion, in dependence on the chain length of the substrate.
摘要
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[Kinetic studies on long-chain alcohol turnover by yeast alcohol dehydrogenase within the transition from real solution to emulsion or suspension].
Acta Biol Med Ger. 1975;34(2):197-201.
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引用本文的文献
1
Kinetics and reaction mechanism of yeast alcohol dehydrogenase with long-chain primary alcohols.酵母乙醇脱氢酶与长链伯醇的动力学及反应机制
Biochem J. 1976 Jul 1;157(1):15-22. doi: 10.1042/bj1570015.
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