Introduction of a disulfide bridge enhances the thermostability of a Streptomyces olivaceoviridis xylanase mutant

文献类型： 外文期刊

第一作者： Yang, H. M.

作者： Yang, H. M.;Yao, B.;Meng, K.;Wang, Y. R.;Bai, Y. G.;Wu, N. F.

作者机构：

关键词： Disulfides chemistry;Dithiothreitol pharmacology;Endo-1;4-beta Xylanases chemistry;Hydrogen-Ion Concentration;Mutation;Streptomyces enzymology;Temperature

期刊名称：JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY （ 影响因子：3.346； 五年影响因子：3.426 ）

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收录情况： SCI

摘要： Substitution of the N-terminus of Streptomyces olivaceoviridis xylanase XYNB to generate mutant TB has been previously shown to increase the thermostability of the enzyme. To further improve the stability of this mutant, we introduced a disulfide bridge (C109-C153) into the TB mutant, generating TS. To assess the effect of the disulfide bridge in the wild-type enzyme, the S109C-N153C mutation was also introduced into XYNB, resulting in XS. The mutants were expressed in Pichia pastoris, the recombinant enzymes were purified, and the effect of temperature and pH on enzymatic activity was characterized. Introduction of the disulfide bridge (C109-C153) into XYNB (XS variant) and TB (TS variant) increased the thermostability up to 2.8-fold and 12.4-fold, respectively, relative to XYNB, after incubation at 70 degrees C, pH 6.0, for 20 min. In addition, a synergistic effect of the disulfide bridge and the N-terminus replacement was observed, which extended the half-life of XYNB from 3 to 150 min. Moreover, XS and TS displayed better resistance to acidic conditions compared with the respective enzymes that did not contain a disulfide bridge.

分类号： Q939.97

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