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. 1984 Oct;48(4):900-1.
doi: 10.1128/aem.48.4.900-901.1984.

Properties of Malolactic Activity Purified from Leuconostoc oenos ML34 by Affinity Chromatography

P Spettoli  1 , M P Nuti, A Zamorani
Affiliations

Properties of Malolactic Activity Purified from Leuconostoc oenos ML34 by Affinity Chromatography

P Spettoli et al. Appl Environ Microbiol. 1984 Oct.

Abstract

Malolactic activity from Leuconostoc oenos ML34 is tightly associated with lactic dehydrogenase. A simple and fast procedure, involving affinity chromatography on agarose-hexane-NAD (Agnad), was used to separate malolactic activity from lactic dehydrogenase and other proteins. The yield was ca. 86%, the purification was 5.2-fold, and the K(m) values for l-malate, NAD and Mn were 2.8, 0.13, and 0.028 mM, respectively, at a pH optimum of 5.8.

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