Effect of family 22 carbohydrate-binding module on the thermostability of Xyn10B catalytic module from Clostridium stercorarium

被引：21

作者：

Araki, Rie ^{[1
]}

Karita, Shuichi ^{[1
]}

Tanaka, Akiyoshi ^{[1
]}

Kimura, Tetsuya ^{[1
]}

Sakka, Kazuo ^{[1
]}

机构：

[1] Mie Univ, Grad Sch Bioresources, Tsu, Mie 5148507, Japan

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2006年 / 70卷 / 12期

关键词：

carbohydrate-binding module; xylanase; thermostability; differential scanning calorimetry (DSC);

D O I：

10.1271/bbb.60348

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：

A family 22 carbohydrate-binding module (CBM22) from Clostridium stercorarium Xylanase10B raised the optimum temperature of the xylanase, but in the remaining activity of heating test, apparently the catalytic module alone showed higher remaining activity. Differential scanning calorimetry showed that CBM22 conferred resistance to thermal unfolding of the enzyme and prevented the enzyme from refolding after thermal unfolding.

引用

页码：3039 / 3041

页数：3

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