Stability of immobilized α‐chymotrypsin
Stability of immobilized α‐chymotrypsin
复制标题
固定化α-胰凝乳蛋白酶的稳定性
DOI：
10.1002/bit.260230605
复制
发表时间：
1981
影响因子：
3.8
通讯作者：
T. Kamikubo
中科院分区：
文献类型：
--
作者：
Y. Kawamura;K. Nakanishi;R. Matsuno;T. Kamikubo
从实验和理论上研究了游离和固定化α-糜蛋白酶的热性质。采用一级反应和自溶的动力学模型分析了游离α-糜蛋白酶的失活过程。离子强度，Ca 2+浓度和温度的影响进行了讨论，在这里的估计动力学参数包括在这个模型中。研究了几种固定化方法固定化α-糜蛋白酶的失活过程。热变性和自溶对失活的贡献取决于固定化方法。为了定量解释固定化酶的非一级热变性过程，提出了一个考虑固定化酶异质性的模型。
The thermal of free and immobilized α‐chymotrypsin was investigated experimentally and theoretically. The inactivation process of free α‐chymotrypsin was analyzed with a kinetic model which included a first‐ order reaction process and autolysis. The effects of ionic strength, Ca2+ concentration, and temperature are discussed here in terms of the estimated kinetic parameters included in this model. The inactivation process of α‐chymotrypsin immobilized onto various supports by several methods was investigated. The Contribution of thermal denaturation and autolysis to the inactivation depended upon the method of immobilization. To interpret quantitatively the non‐first‐order thermal denaturation process of the immobilized enzyme, a model in which the heterogeneity of the immobilized enzyme was taken into account is proposed.