Stabilization of xylanase by random mutagenesis.
作者信息
Arase A, Yomo T, Urabe I, Hata Y, Katsube Y, Okada H
机构信息
Department of Biotechnology, Faculty of Engineering, Osaka University, Japan.
出版信息
FEBS Lett. 1993 Jan 25;316(2):123-7. doi: 10.1016/0014-5793(93)81199-a.
PMID:8420796
Abstract
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.
摘要
Zotero 插件