NDLI: A Novel β-mannanase with High Specific Activity from Bacillus circulans CGMCC1554: Gene Cloning, Expression and Enzymatic Characterization

Content Provider	Springer Nature Link
Author	Yang, Peilong Li, Yanan Wang, Yaru Meng, Kun Luo, Huiying Yuan, Tiezheng Bai, Yingguo Zhan, Zhichun Yao, Bin
Copyright Year	2008
Abstract	A DNA fragment of 2,042 bp containing a novel β-mannanase gene, man5A, was identified from the genome of the mannan-degrading bacterium Bacillus circulans CGMCC1554. The open reading frame of man5A comprised 978 bp encoding a protein of 326 amino acids with a predicted molecular weight of 32 kDa. The amino acid sequence of the encoded mannanase, MAN5A, showed the highest identity (78.5%) to β-mannanases belonging to glycosyl hydrolases family 5. The gene man5A was efficiently expressed in Escherichia coli and Pichia pastoris with the highest activity of 541 U/ml in a 3-L fermenter. Recombinant MAN5A purified from E. coli had a high specific activity of 4,839 U/mg, which is much higher than that of enzymes that showed high sequence identity. The enzyme showed maximum activity at pH 7.6 and 60 °C and resistance to trypsin. After hydrolysis of LBG, oligomannosides accounted for 76% of the hydrolysis products. All these properties collectively make MAN5A a better candidate than current mannanases for use in the food and feed industry.
Starting Page	85
Ending Page	94
Page Count	10
File Format	PDF
ISSN	02732289
Journal	Applied Biochemistry and Biotechnology
Volume Number	159
Issue Number	1
e-ISSN	15590291
Language	English
Publisher	Humana Press Inc
Publisher Date	2008-09-24
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	β-Mannanase Bacillus circulans Expression Characterization High specific activity Biochemistry Biotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology

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