Stabilization of xylanase by random mutagenesis

FEBS Letters

Hata, Yasuo³  Yomo, Tetsuya¹  Okada, Hirosuke¹  Urabe, Itaru¹  Katsube, Yukiteru²  Arase, Akemi¹ 

[1] Department of Biotechnology, Faculty of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565, Japan;Institute for Protein Research, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565, Japan;Institute for Chemical Research, Kyoto University, Gokasho, Uji, Kyoto 611, Japan

关键词: Xylanase;    Bacillus pumilus;    Random mutagenesis;    Enzyme stabilization;    Heat-resistant mutant;   

DOI  :  10.1016/0014-5793(93)81199-A

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Four heat-resistant mutants of xylanase (N56, N102, N104 and F1) were obtained by random mutagenesis. The mutant genes had the following amino acid changes: N56, Ser-26 to Trp, Gly-38 to Asp and Thr-126 to Ser; N102, Gly-38 to Asp; N104, Gly-38 to Ser and Arg-48 to Lys; F1, Ser-12 to Cys. Kinetic studies showed that N104 is stabilized by an increase in the activation enthalpy, while the other mutants are stabilized by a decrease in the activation entropy.

【 授权许可】

Unknown