Purification and properties of the B-Glucosidase of a yeast capable of fermenting cellobiose to ethanol: Dekkera intermedia Van der Walt.

Abstract

The intracellular enzyme β-glucosidase of Dekkera intermedia was partially purified by ion-exchange chromatography and gel filtration. The molecular weight of this enzyme was 310,000; its optimum pH was 5.0 and optimum temperature was 55°C. This enzyme was active against different β-glucosides and was inhibited by p-chloromercurybenzoate, gluconolactone, and glucose. A “glucosyltransferase” activity appeared in the presence of ethanol. The biosynthesis of this enzyme was constitutive but repressed by glucose.