THE COMPONENTS OF MALTOZYMASE IN YEAST, AND THEIR BEHAVIOR DURING DEADAPTATION

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Abstract
The metabolism of glucose by maltose adapted cells in N-free buffer led to an increase in vivo of a-glucosidase, crypticity towards its activity, and an eventual loss of the enzyme. The a-glucosidase was found both soluble and attached to particles. During deadaptation the enzyme was solubilized. The crypticity was attributed to the loss of a glucoside-permeation mechanism, which permits normally the internal accumulation of maltose and other a-glucosides. The permease is both inhibited and inactivated by glucose. Such losses eliminated maltose fermentation and induced a-glucosidase synthesis by suppressing the entry of the inducer.