Purification of α-acetolactate decarboxylase from Lactobacillus casei DSM 2547

Abstract

α-Acetolactate decarboxylase has been purified to homogeneity, by fast protein liquid chromatography and high performance elution chromatography, from a partially purified α-acetolactate decarboxylase preparation from Lactobacillus casei DSM 2547. The pure enzyme exhibited a specific activity of 375 kU·mg-1 and exerted its optimal activity at pH 4.5 to 5.0 and at a temperature of 40°C. Its isoelectric point was estimated to pH 4.7 and its molecular weight was found to be 48,000. The enzyme was inhibited by o-phenanthroline and could be partially reactivated by zinc ions. An HPLC method for the determination of α-acetolactate is described. © 1985 Carlsberg Laboratory.