RT Journal Article SR Electronic T1 Isolation and Properties of β-Glucosidase Produced by Debaryomyces hansenii and Its Application in Winemaking JF American Journal of Enology and Viticulture JO Am. J. Enol. Vitic. FD American Society for Enology and Viticulture SP 231 OP 235 VO 50 IS 3 A1 Yanai, Takaaki A1 Sato, Michikatsu YR 1999 UL http://www.ajevonline.org/content/50/3/231.abstract AB An intracellular β-glucosidase (EC 3.2.1.21) from Debaryomyces hansenii Y-44 was purified and characterized. The enzyme was purified to homogeneity from the cell-free extracts by a combination of column chromatography with DEAE-Toyopearl 650M and Butyl-Toyopearl 650S. The size of the enzyme was 95 kDa by native-PAGE, and the pl was 4.9. The enzyme was the most active at pH 7.0 and at around 25°C. The activity was highly tolerant to glucose, and only 20% inhibited in 500 mM glucose. The enzyme was tolerant to ethanol; its activity was only slightly reduced by 6% in the presence of 15% (v/v) ethanol. As the enzyme was inhibited with p-chloromercuribenzoate, it belongs to the class of SH-enzymes. The enzyme efficiently released monoterpenols from the glycosides extracted from Muscat grape must. The fermentation of Muscat juice coupled with the enzyme addition produced a considerable increase in the concentration of monoterpenols. Especially the linalool and nerol contents increased by 90% and 116%, respectively. The practical usefulness of the enzyme in juice processing and winemaking was suggested.