固定于羧甲基纤维素上的胰酶的制备及性质

[Preparation and properties of pancreatin immobilized on carboxymethylcellulose].

作者信息

Nekliudov A D, Ivankin A N, Baburina M I

机构信息

All-Russia Research Institute of the Meat Industry, Moscow, Russia.

出版信息

Prikl Biokhim Mikrobiol. 1998 Jan-Feb;34(1):61-5.

PMID:9566291

Abstract

A method for immobilizing pancreation on carboxymethylcellulose (CMC) is proposed. The optimum reaction conditions were determined: CMC, 1 x 10(-4) M; 1-ethyl 3-(dimethylaminopropyl)-carbodiimide, 2 x 10(-4) M; incubation time, 18 h at 4 degrees C. They allow obtaining a conjugate of the enzyme with the polymer displaying 85% of the protease and 92% of the esterase activity. Both the native and immobilized enzymes were shown to contain thermolabile and thermostable fractions with different inactivation constants. Immobilization of the enzyme was found to increase its thermal stability by a factor of 1.5 to 3. Thermodynamic constants of blood protein hydrolysis by native and immobilized enzymes were determined.

摘要

提出了一种将胰腺固定在羧甲基纤维素（CMC）上的方法。确定了最佳反应条件：CMC，1×10⁻⁴ M；1-乙基-3-（二甲基氨基丙基）碳二亚胺，2×10⁻⁴ M；孵育时间，4℃下18小时。这些条件使得能够获得酶与聚合物的缀合物，该缀合物显示出85%的蛋白酶活性和92%的酯酶活性。天然酶和固定化酶均显示含有具有不同失活常数的热不稳定和热稳定部分。发现酶的固定化使其热稳定性提高了1.5至3倍。测定了天然酶和固定化酶水解血液蛋白质的热力学常数。