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[固定在气相二氧化硅衍生物上的淀粉酶的性质]

[Properties of amylase immobilized on aerosil derivatives].

作者信息

Kolesnik L A, Galich I P, Koval'chuk T A

出版信息

Ukr Biokhim Zh (1978). 1979 Jul-Aug;51(4):369-73.

PMID:38550
Abstract

The properties of three preparations of alpha-amylase immobilized on aminoaerosil by 2,4-toluylenediisocyanate and N,N'-dicyclohexylcarbodiimide as well as on carboxyaerosil by N,N'-dicyclohexylcarbodiimide were compared with the properties of soluble enzyme. Under immobilization the pH-effect and pH-stability zones of amylase are 0.5--1.0 pH units shifted towards the alkaline region. The preparations in which the enzyme is bound with the matrix through the amine groups on carboxyaerosil by N,N'-dicyclohexylcarbodiimide and on aminoaerosil by 2,4 toluylenediisocyanate are the most stable at 50 degrees C and to the EDTA effect. The preparation obtained by means of 2,4-toluylenediisocyanate contains a greater amount of the bound protein, is more active and stable.

摘要

比较了通过2,4-甲苯二异氰酸酯和N,N'-二环己基碳二亚胺固定在氨基气凝胶上以及通过N,N'-二环己基碳二亚胺固定在羧基气凝胶上的三种α-淀粉酶制剂与可溶性酶的性质。在固定化过程中,淀粉酶的pH效应和pH稳定区向碱性区域移动0.5-1.0个pH单位。通过N,N'-二环己基碳二亚胺使酶通过羧基气凝胶上的胺基与基质结合以及通过2,4-甲苯二异氰酸酯使酶通过氨基气凝胶上的胺基与基质结合的制剂在50℃下对EDTA效应最稳定。通过2,4-甲苯二异氰酸酯获得的制剂含有更多的结合蛋白,活性更高且更稳定。

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