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首页> 外文期刊>Preparative biochemistry & biotechnology: An international journal for rapid communication >Functional Stabilization of Trypsin by Conjugation with beta-Cyclodextrin-Modified Carboxymethylcellulose
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Functional Stabilization of Trypsin by Conjugation with beta-Cyclodextrin-Modified Carboxymethylcellulose

机译：通过与β-环糊精修饰的羧甲基纤维素结合来稳定胰蛋白酶的功能

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摘要

Bovine Pancreatic trypsin was chemically modified by a beta-cyclodextrin-carboxymethylcellulose polymer using 1-ethyl-3-(3-dimethyl-aminopropyl) carbodiimide as coupling agent. The conjugate retained 110% and 95% of the initial esterolytic and proteolytic activity, respectively, and contained about 2 mol of polymer per mol of trypsin. The optimum temperature for trypsin was increased to 8 deg C after conjugation. The thermostability of the enzyme was increased to about 16 deg C after modification. The conjugate prepared was also more stable against thermal incubation at different temperatures ranging from 45 deg C to 60 deg C. In comparison with native trypsin, the polymer-enzyme complex was more resistant to autolytic degradation at pH 9.0, retaining about 65% of the initial activity after 3h incubation. In addition, modification protected trypsin against denaturation in the presence of sodium dodecylsulfate.
机译：使用1-乙基-3-（3-二甲基-氨基丙基）碳二亚胺作为偶联剂，通过β-环糊精-羧甲基纤维素聚合物对牛胰胰蛋白酶进行化学修饰。该缀合物分别保留了初始酯水解活性和蛋白水解活性的110％和95％，并且每摩尔胰蛋白酶含有约2摩尔聚合物。结合后，胰蛋白酶的最佳温度增加到8摄氏度。修饰后，酶的热稳定性增加到约16℃。制备的结合物在45°C至60°C的不同温度下对热孵育的稳定性也更高。与天然胰蛋白酶相比，聚合物-酶复合物在pH 9.0时更能抵抗自降解，保留了约65％的结合物。孵育3h后的初始活性。另外，修饰在十二烷基硫酸钠存在下保护胰蛋白酶不变性。

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