Three-dimensional structure of an alkaline xylanase Xyn11A-LC from alkalophilic Bacillus sp. SN5 and improvement of its thermal performance by introducing arginines substitutions----中国科学院微生物研究所

科研成果

论文题目:	Three-dimensional structure of an alkaline xylanase Xyn11A-LC from alkalophilic Bacillus sp. SN5 and improvement of its thermal performance by introducing arginines substitutions
作者:	Bai Wenqin, Zhou Cheng, Xue Yanfen, Huang Chun-Hsiang, Guo Rey-Ting, Ma Yanhe*
联系作者:	Ma Yanhe*
刊物名称:	Biotechnol Lett
期:
卷:
页:
年份:	2014
影响因子:	1.964
论文下载:
摘要:	The alkaline xylanase Xyn11A-LC from the alkalophilic Bacillus sp. SN5 was expressed in E. coli, purified and crystallized. The crystal structure was determined at a resolution of 1.49 A. Xyn11A-LC has the beta-jelly roll structure typical of family 11 xylanases. To improve its thermostability and thermophilicity, a mutant SB3 was constructed by introducing three arginines on the different sides of the protein surface. SB3 increased the optimum temperature by 5 degrees C. The wild type and SB3 had the half-lives of 22 and 68 min at 65 degrees C at pH 8.0 (Tris/HCl buffer), respectively. CD spectroscopy revealed that the melting temperature (T m) of the wild type and SB3 were 55.3 and 66.9 degrees C, respectively. These results showed that the introduction of arginines enhance the thermophilicity and thermostability of Xyn11A-LC.