STUDIES ON THE DENATURATION OF ENZYMES

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Abstract
The heat-inactivation (63[degree]C) of sweet potato B-amylase, prepared by dialyzing an aqueous solution of Ball''s purified paste proceeds as the first order reaction in respect to time. The rate of the inactivation is increased with the increasing concentration of acetate buffer (0.01-0.1 [image]) of pH 5.4 as well as with the decreasing enzyme concentration (1.2-6 [mu]g N/ml). The enzyme preparation is stable at pH 5.0-5.8 (maximum stability at pH 5.4) against heat-inactivation.

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