Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
686019 | Bioresource Technology | 2008 | 5 Pages |
Abstract
A thermostable xylanase gene (stxI) obtained from Streptomyces thermonitrificans NTU-88 on domain analysis revealed an N-terminal catalytic domain featuring homology to a known xylanase within the glycoside hydrolase family 11. Recombinant STXI retained more than 60% of its activity following its incubation for at 60 °C for 24 h. These characteristics were close to thermophile and mesophile Streptomyces strains. The main hydrolysis products of xylan degraded by STXI included large xylooligosaccharide fragments. These results indicated that STXI was a typical endoxylanase. As regards the phylogenetic relationships of GH11, STXI and the other xylanase deriving from Streptomyces were included in a subgroup of the aerobic bacterial group. This result implied that the evolutionary relationships between the various xylanases deriving from Streptomyces strains were convergent.
Keywords
Related Topics
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Chemical Engineering
Process Chemistry and Technology
Authors
Hsueh-Ling Cheng, Pei-Min Wang, Yu-Chi Chen, Shang-Shyng Yang, Yo-Chia Chen,