PURIFICATION, CHARACTERIZATION AND SOME PROPERTIES OF DIACETYL(ACETOIN) REDUCTASE FROM ENTEROBACTER-AEROGENES

被引：21

作者：

CARBALLO, J ^{[1
]}

MARTIN, R ^{[1
]}

BERNARDO, A ^{[1
]}

GONZALEZ, J ^{[1
]}

机构：

[1] UNIV LEON, FAC VET, FOOD TECHNOL & BIOCHEM LAB, LEON, SPAIN

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1991年 / 198卷 / 02期

关键词：

D O I：

10.1111/j.1432-1033.1991.tb16019.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A new method, faster, milder and more efficient than the one previously described [Bryn, K., Hetland, O. & Stormer, F. C. (1971) Eur. J. Biochem. 18, 116-119], for purification of diacetyl(acetoin) reductase from Enterobacter aerogenes is proposed. The experiments carried out with the electrophoretically pure preparations obtained by this procedure show that the enzyme (a) produces L-glycols from the corresponding L-alpha-hydroxycarbonyls by reversible reduction of their oxo groups and also reduces the oxo group of uncharged alpha-dicarbonyls converting them into L-alpha-hydroxycarbonyls, and (b) is specific for NAD. This is a new enzyme for which we suggest the systematic name of L-glycol:NAD+ oxidoreductase and the recommended name of L-glycol dehydrogenase(NAD). The molecular mass, pI, affinity for substrates and pH profiles of this enzyme are also described.

引用

页码：327 / 332

页数：6

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