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Study of catalase immobilized on a silicate matrix for non-aqueous biocatalysis

机译:非水生物催化固定在硅酸盐基质上的过氧化氢酶的研究

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Catalytic activity of catalase(CAT)immobilized on a modified silicate matrix to mediate decomposition of meta-chloroperoxibenzoic acid(3-CPBA)in acetonitrile has been investigated by means of quantitative UV-spectrophotometry.Under the selected experimental conditions,the kinetic parameters:the apparent Michaelis constant(K_M),the apparent maximum rate of enzymatic reaction(V~(app)_(max)),the first order specific rate constants(k_(sp)), the energy of activation(E_a)and the pre-exponential factor of the Arrhenius equation(Z_0) were calculated.Conclusions regarding the rate-limiting step of the overall catalytic process were drawn from the calculated values of the Gibbs energy of activation DELTA G*,the enthalpy of activation DELTA H*,and the entropy of activation DELTA S*.
机译:通过定量紫外分光光度法研究了固定在改性硅酸盐基质上的过氧化氢酶(CAT)介导间氯过氧苯甲酸(3-CPBA)在乙腈中分解的催化活性。在选定的实验条件下,动力学参数为:表观米氏常数(K_M),酶促反应的表观最大速率(V〜(app)_(max)),一阶比速率常数(k_(sp)),活化能(E_a)和预计算了Arrhenius方程(Z_0)的指数因子。从活化DELTA G *的吉布斯能量,活化DELTA H *的焓和计算值得出了整个催化过程的限速步骤的结论。激活熵ΔS *。

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