Purification, characterization and some properties of diacetyl(acetoin) reductase from Enterobacter aerogenes

Abstract

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‐α‐hydroxycarbonyls by reversible reduction of their oxo groups and also reduces the oxo group of uncharged α‐dicarbonyls converting them into l‐α‐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. Copyright © 1991, Wiley Blackwell. All rights reserved