, Volume 30, Issue 8, pp 1469-1475
Date: 15 Apr 2008

One-step purification and characterization of an intracellular β-glucosidase from Metschnikowia pulcherrima

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A collection of 60 non-Saccharomyces yeasts isolated from grape musts in Uruguayan vineyards was screened for β-glucosidase activity and Metschnikowia pulcherrima was the best source of this enzyme activity. Its major β-glucosidase was successfully purified to homogeneity by ion-exchange chromatography on amino-agarose gel. The enzyme exhibited an optimum catalytic activity at 50°C and pH 4.5 and was active against (1 → 4)-β and (1 → 2)-β glycosidic linkages. In spite of preserving 100% of its activity and stability in the presence of 12% (v/v) ethanol and 5 g glucose/l, the enzyme was unstable below pH 4. We characterized the β-glucosidase from M. pulcherrima with a view to its potential applications in wine-making.