NDLI: Cloning, expression, and characterization of a new xylanase with broad temperature adaptability from Streptomyces sp. S9

Content Provider	Springer Nature Link
Author	Li, Ning Meng, Kun Wang, Yaru Shi, Pengjun Luo, Huiying Bai, Yingguo Yang, Peilong Yao, Bin
Copyright Year	2008
Abstract	A new xylanase gene, xynAS9, was cloned from Streptomyces sp. S9, which was isolated from Turpan Basin, China. The full-length gene consists of 1,395 bp and encodes 465 amino acids including 38 residues of a putative signal peptide. The overall amino acid sequence shares the highest identity (50.8%) with a putative endo-1,4-β-xylanase from Streptomyces avermitilis of the glycoside hydrolase family 10. The gene fragment encoding the mature xylanase was expressed in Escherichia coli BL21 (DE3). The recombinant protein was purified to electrophoretic homogeneity and subsequently characterized. The optimal pH and temperature for the recombinant enzyme were 6.5 and 60°C, respectively. The enzyme showed broad temperature adaptability, retaining more than 65% of the maximum activity when assayed at 50–80°C. The enzyme also had good thermal and pH stability. The K m values for oat spelt xylan and birchwood xylan substrates were 2.85 and 2.43 mg ml−1, with the V max values of 772.20 and 490.87 μmol min−1 mg−1, respectively. The hydrolysis products of xylan were mainly xylose and xylobiose. These favorable properties should make XynAS9 a good candidate in various industrial applications.
Starting Page	231
Ending Page	240
Page Count	10
File Format	PDF
ISSN	01757598
Journal	Applied Microbiology and Biotechnology
Volume Number	80
Issue Number	2
e-ISSN	14320614
Language	English
Publisher	Springer-Verlag
Publisher Date	2008-06-03
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	Streptomyces sp. S9 Turpan Basin Xylanase Xylose Microbial Genetics and Genomics Microbiology Biotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Applied Microbiology and Biotechnology Biotechnology

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