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Three-dimensional structure of an alkaline xylanase Xyn11A-LC from alkalophilic Bacillus sp. SN5 and improvement of its thermal performance by introducing arginines substitutions.
- Source :
- Biotechnology Letters; Jul2014, Vol. 36 Issue 7, p1495-1501, 7p
- Publication Year :
- 2014
-
Abstract
- 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 Å. Xyn11A-LC has the β-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 °C. The wild type and SB3 had the half-lives of 22 and 68 min at 65 °C at pH 8.0 (Tris/HCl buffer), respectively. CD spectroscopy revealed that the melting temperature ( T) of the wild type and SB3 were 55.3 and 66.9 °C, respectively. These results showed that the introduction of arginines enhance the thermophilicity and thermostability of Xyn11A-LC. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 01415492
- Volume :
- 36
- Issue :
- 7
- Database :
- Complementary Index
- Journal :
- Biotechnology Letters
- Publication Type :
- Academic Journal
- Accession number :
- 96396674
- Full Text :
- https://doi.org/10.1007/s10529-014-1512-7