Abstract
Two strains of Saccharomyces lactis (Y-14 and Y-1057A), medium (Bm) and low (B1) constitutive producers of β-glucosidase, were grown in enriched medium. β-Glucosidase was extracted by autolysis and purified by ammonium sulfate precipitation, gel filtration, and calcium phosphate gel adsorption-elution. The kinetics of release, purification, and stability of β-glucosidase from strains Y-14 and Y-1057A were compared with the enzyme from strain Y-123. The ability of glycerol, sorbitol, and mannitol to stabilize the β-glucosidases is presented. A lower molecular weight, labile form of the Y-14 enzyme is demonstrated. Differences in the initial specific activites of β-glucosidase among the three strains are discussed.
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Selected References
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