Properties of endogenous β-glucosidase of a Pichia anomala strain isolated from Sicilian musts and wines
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- 作者：Spagna ; Giovanni ; Barbagallo ; Riccardo N. ; Palmeri ; Rosa ; Restuccia ; Cristina ; Giudici ; Paolo
- 关键词：β ; -Glucosidase ; Strain AL 112 ; Pichia anomala ; Arabinosidase
- 刊名：Enzyme and Microbial Technology
- 出版年：2002
- 出版时间：December 2, 2002
- 年：2002
- 卷：31
- 期：7
- 页码：1036-1041
- 全文大小：131 K
文摘
The AL 112 strain, isolated from 361 yeast strains in Sicilian musts and wines, has been identified by biochemical and molecular methods as belonging to Pichia anomala, and your endogenous β-glucosidase (βG, EC 3.2.1.21) subsequently characterised. This strain not only has extremely high specific productivity of βG, but above all shows arabinosidase (Ara, EC 3.2.1.55) activity, essential for aroma enhancement of wine. βG from Al 112 is activated by ethanol at the concentrations typically found in wine; it is not inhibited by fructose, whilst glucose, a non-competitive inhibitor, despite lowering activity, actually protects the enzyme from factors that could damage it. It has an optimum temperature of 20°C, compatible with typical cellar conditions, and stability in model must-wine and wine solutions ≥40 days.