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[微囊化α-糜蛋白酶的提取与性质]

[Extraction and properties of microcapsulated alpha-chymotrypsin].

作者信息

Aĭsina R B, Kazanskaia N F, Lukasheva E V, Berezin I V

出版信息

Biokhimiia. 1976 Sep;41(9):1656-61.

PMID:974181
Abstract

A method of microencapsulating of the proteolytic enzyme alpha-chymotrypsin into semi-permeable nylon membranes is worked out. The membrane is a polimer of 1,6-hexamethylenediamine and sebacoyl chloride. alpha-Chymotrypsin is enclosed into the capsule together with polyethyleneimine, capable of joining the walls of microcapsules and making the membrane more stable. The optimal concentrations of polyenthyleneimine and alpha-chymotrypsin are 5% and 1% correspondingly. The highest yield of microencapsulated enzyme was obtained for completely acetylated delta-chymotrypsin. The kinetic properties of microencapsulated alpha-chymotrypsin change very slightly as compared to those of the native one.

摘要

研究出了一种将蛋白水解酶α-胰凝乳蛋白酶微囊化到半透性尼龙膜中的方法。该膜是1,6-己二胺和癸二酰氯的聚合物。α-胰凝乳蛋白酶与聚乙烯亚胺一起被包裹在胶囊中,聚乙烯亚胺能够连接微胶囊壁并使膜更稳定。聚乙烯亚胺和α-胰凝乳蛋白酶的最佳浓度分别为5%和1%。完全乙酰化的δ-胰凝乳蛋白酶微囊化酶的产率最高。与天然α-胰凝乳蛋白酶相比,微囊化α-胰凝乳蛋白酶的动力学性质变化非常小。

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