Studies on Taka-Amylase A under High Pressure : IV. Influence of Initial Concentration of Enzyme upon Pressure Inactivation and Reactivation

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The influence of initial concentration of enzyme (1-10^<-4>%) at pH 6.5, 7.5, and 9.O upon pressure-inactivation and reactivation was studied. Inactivation and reactivation appeared to follow first-order kinetics; however, the more concentrated the enzyme solution, the greater the rate of inactivation and reactivation. In the equation, k=αCi^β, for the fist-order rate constants of both processes, k, and initial concentration of TAA, Ci, where α and β are constants at a definite pH, temperature, and pressure, the values of β were O.14, O.08, an d for inactivation and O.06, O.06, and O for reactivation at pH 6.5, 7.5, and 9.O, respectively. The rate constants are independent of concentration at pH 9.O, while an increasing dependence is found at lower pH values. In sedimentation studies, pressure-denatured TAA did not associate at pH 9.O, while association was observed at pH 7.5 and 6.5, with the degree of association increasing with decrease of pH. The influence of concentration on pressure-inactivation and reactivation may be attributed to association of the enzyme.
大阪夕陽丘学園短期大学の論文
1966-07-01