NDLI: A novel, alkali-tolerant thermostable xylanase from Saccharomonospora viridis: direct gene cloning, expression and enzyme characterization.

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A novel, alkali-tolerant thermostable xylanase from Saccharomonospora viridis: direct gene cloning, expression and enzyme characterization.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wang, Ziyuan Jin, Yi Wu, Huijun Tian, Zhaofeng Wu, Yuying Xie, Xiangming
Description	Author Affiliation: Wang Z ( College of Biological Sciences and Biotechnology, Beijing Forestry University, 35 QingHua East Road, Beijing, 100083, People's Republic of China.)
Abstract	A xylanase gene, designated Svixyn10A, was cloned from actinomycetes Saccharomonospora viridis and the gene product was characterized. Gene Svixyn10A contains 1,374 bp and encodes a polypeptide of 457 amino acids composed of a glycoside hydrolase family 10 catalytic domain with a putative signal peptide, a short Gly-rich linker and a family 2 carbohydrate-binding module (CBM). The deduced amino acid sequence of SviXyn10A shared the highest identity (57 %) with a hypothetical xylanase from Streptomyces lividans TK24 (ZP_05528201). A recombinant His-tagged xylanase, SviXyn10A was expressed in Escherichia coli BL21 and purified. The optimum pH and temperature for SviXyn10A is 8.0 and 60 °C. Compared with thermophilic and mesophilic counterparts, SviXyn10A was more active at high temperatures, retaining >63 % of its maximum activity at 65-70 °C and ~40 % even at 80 °C. It had broad pH adaptability (>35 % activity at pH 5.0-11.0) and alkali-tolerance (>70 % activity after incubation at pH 8.0-11.0 for 1 h at 37 °C), and was highly thermostable (>75 % activity after incubation at 70 °C for 3 h at pH 8.0). It may be the first alkali-tolerant thermostable xylanase reported from Saccharomonospora. These favorable properties make SviXyn10A a good candidate for application in pulp and paper industries.
File Format	HTM / HTML
ISSN	09593993
Issue Number	8
Volume Number	28
e-ISSN	15730972
Journal	World Journal of Microbiology and Biotechnology
Language	English
Publisher	Springer
Publisher Date	2012-08-01
Publisher Place	Germany
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Amino Acid Sequence Genes, Bacterial Research Support, Non-u.s. Gov't Discipline Microbiology Gene Expression Enzyme Stability Molecular Sequence Data Hot Temperature Phylogeny Recombinant Proteins Metabolism Journal Article Discipline Biotechnology Bacterial Proteins Actinomycetales Dna, Bacterial Base Sequence Classification Cloning, Molecular Genetics Hydrogen-ion Concentration Kinetics Enzymology Endo-1,4-beta Xylanases
Content Type	Text
Resource Type	Article
Subject	Physiology Medicine Applied Microbiology and Biotechnology Biotechnology

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