Localization, purification, and characterization of a novel β‐glucosidase from Hanseniaspora uvarum Yun268

β-Glucosidase is a key enzyme that hydrolyzes nonvolatile glycosylated precursors of aroma compounds and enhances the organoleptic quality of wines. In this study, a novel β-glucosidase from Hanseniaspora uvarum Yun268 was localized, purified, and characterized. Results indicated that β-glucosidase activity was mainly distributed within the cells. After purification via ammonium sulfate precipitation combined with chromatography, β-glucosidase specific activity increased 8.36 times, and the activity recovery was 56.90%. The enzyme had a molecular mass of 74.22 kDa. It has a Michaelis constant (K