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Biotechnol Lett. 2008 Aug;30(8):1469-75. doi: 10.1007/s10529-008-9708-3. Epub 2008 Apr 15.

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

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  • 1Departamento de Biociencias, Facultad de Química, Cátedra de Bioquímica, Gral Flores 2124, CC1157 Montevideo, Uruguay.


A collection of 60 non-Saccharomyces yeasts isolated from grape musts in Uruguayan vineyards was screened for beta-glucosidase activity and Metschnikowia pulcherrima was the best source of this enzyme activity. Its major beta-glucosidase was successfully purified to homogeneity by ion-exchange chromatography on amino-agarose gel. The enzyme exhibited an optimum catalytic activity at 50 degrees C and pH 4.5 and was active against (1 --> 4)-beta and (1 --> 2)-beta 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 beta-glucosidase from M. pulcherrima with a view to its potential applications in wine-making.

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