~ Present address: Novo Industri A/S, Novo All& DK-2880 BagsvaerdKeywords: et-acetolactate, a-acetolactate decarboxylase, acetoin, diacetyl, lactic acid bacteria, beer maturation, HPLC ct-Acetolactate decarboxylase has been purified to homogeneity, by fast protein liquid chromatography and high performance elution chromatography, from a partially purified ct-acetolactate decarboxylase preparation from Lactobacillus casei DSM 2547. The pure enzyme exhibited a specific activity of 375 kU. mg-' and exerted its optimal activity at pH 4.5 to 5.0 and at a temperature of 40 ~ 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 ct-acetolactate is described.