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α-淀粉酶在多孔玻璃和硅铬合金上的固定化

[Immobilization of alpha-amylase on porous glass and silochrome].

作者信息

Dvali M Sh, Varlamov V P, Kvesitadze G I, Rogozhin S V

出版信息

Prikl Biokhim Mikrobiol. 1978 Jan-Feb;14(1):15-7.

PMID:24839
Abstract

Immobilized forms of alpha-amylase from Aspergillus oryzae were prepared on the porous glass and silochrome by the glutaraldehyde method. An addition of calcium ions at a concentration of 0.05 M to the reaction mixture during immobilization stabilized the enzyme activity. pH optimum of the insoluble form of alpha-amylase was 5.8 and that of the soluble form was 4.7. Storage of the insoluble enzyme as water suspension in 0.015 M CaCl2 at 4 degrees C for six months and twenty times repeated specific reaction did not affect significantly the activity of insoluble alpha-amylase.

摘要

采用戊二醛法在多孔玻璃和硅铬上制备了米曲霉α-淀粉酶的固定化形式。在固定化过程中向反应混合物中添加浓度为0.05 M的钙离子可稳定酶活性。不溶性α-淀粉酶的最适pH为5.8,可溶性α-淀粉酶的最适pH为4.7。将不溶性酶作为水悬浮液保存在0.015 M氯化钙中,于4℃保存6个月并进行20次重复的特定反应,对不溶性α-淀粉酶的活性没有显著影响。

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