IMPROVEMENT OF THE THERMOSTABILITY OF PYRUVATE DECARBOXYLASE BY MODIFICATION WITH AN AMYLOSE DERIVATIVE

被引：0

作者：

OHBA, H ^{[1
]}

YASUDA, S ^{[1
]}

HIROSUE, H ^{[1
]}

YAMASAKI, N ^{[1
]}

机构：

[1] KYUSHU UNIV, FAC AGR, BIOCHEM LAB, HIGASHI KU, FUKUOKA 812, JAPAN

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1995年 / 59卷 / 08期

关键词：

D O I：

10.1271/bbb.59.1581

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Pyruvate decarboxylase from brewer's yeast was modified with the N-hydroxysuccinimide ester of an amylose glycylglycine adduct and some properties of the resulting conjugate were studied with regard to thermostability. By this conjugation the optimum temperature of the activity of pyruvate decarboxylase shifted from 35 degrees C to 40 degrees C. The conjugate showed a greater resistance than the enzyme to inactivating by heat treatment. It is suggested that AG-ONSu can be advantageously used for stabilization of the thermolabile enzyme.

引用

页码：1581 / 1583

页数：3

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