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Properties of endogenous β-glucosidase of a Pichia anomala strain isolated from Sicilian musts and wines
Authors:Giovanni Spagna  Riccardo N Barbagallo  Rosa Palmeri  Cristina Restuccia  Paolo Giudici  
Institution:

a Department of Horticulture, Floriculture, Arboriculture and Agroindustrial Technology (DOFATA), University of Catania, Via S. Sofia 98, 95123, Catania, Italy

b Interdisciplinary Department of Agriculture, Primary Teacher Training and Healthcare Planning Sciences, University of Modena and Reggio Emilia, Via Kennedy 17, 42100, Reggio Emilia, Italy

Abstract: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.
Keywords:β-Glucosidase  Strain AL 112  Pichia anomala  Arabinosidase
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