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Molecular and biochemical characterization of a bimodular xylanase from marinifilaceae bacterium strain SPP2

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成果类型:
期刊论文
作者:
Han, Zhenggang;Shang-guan, Fang;Yang, Jiangke*
通讯作者:
Yang, Jiangke
作者机构:
[Shang-guan, Fang; Yang, Jiangke; Han, Zhenggang] Wuhan Polytech Univ, Coll Biol & Pharmaceut Engn, Wuhan, Hubei, Peoples R China.
通讯机构:
[Yang, Jiangke] W
Wuhan Polytech Univ, Coll Biol & Pharmaceut Engn, Wuhan, Hubei, Peoples R China.
语种:
英文
关键词:
FN3 domain;glycoside hydrolase;Marinifilaceae bacterium;xylanase;Xylooligosaccharide
期刊:
Frontiers in Microbiology
ISSN:
1664-302X
年:
2019
卷:
10
期:
JUL
页码:
457951
基金类别:
This work was financially supported by the project (No. DY135-B2-06) from the China Ocean Mineral Resources R&D Association.
机构署名:
本校为第一且通讯机构
院系归属:
生命科学与技术学院
摘要:
In this study, the first xylantic enzyme from the family Marinifilaceae, XynSPP2, was identified from Marinifilaceae bacterium strain SPP2. Amino acid sequence analysis revealed that XynSPP2 is a rare Fn3-fused xylanase, consisting of a signal peptide, a fibronectin type-III domain (Fn3), and a C-terminal catalytic domain belonging to glycoside hydrolase family 10 (GH10). The catalytic domain shared 17-46% identities to those of biochemically characterized GH10 xylanases. Structural analysis revealed that the conserved asparagine and glutamine ...

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