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Cloning of a Bacillus subtilis WL-7 Mannanase Gene and Characterization of the Gene Product  

KWEUN , MIN-A (School of Food Science and Biotechnology, Woosong University)
LEE, MI-SUNG (School of Food Science and Biotechnology, Woosong University)
CHOI, JOON-HO (R&D Center, KoBioTech Co.)
CHO, KI-HAENG (R&D Center, CTCBIO Inc.)
YOON, KI-HONG (School of Food Science and Biotechnology, Woosong University, Bioresouce and Application Research Center, Woosong University)
Publication Information
Journal of Microbiology and Biotechnology / v.14, no.6, 2004 , pp. 1295-1302 More about this Journal
Abstract
A gene encoding the mannanase of Bacillus subtilis WL-7, which had been isolated from Korean soybean paste, was cloned into Escherichia coli, and the gene product was purified from the culture filtrate of the recombinant E. coli. This mannanase gene, designated manA, consisted of 1,086 nucleotides, encoding a polypeptide of 362 amino acid residues. The deduced amino acid sequence was highly homologous to those of mannanases belonging to the glycosyl hydrolase family 26. The molecular mass of the purified mannanase was 38 kDa as estimated by SDS-PAGE. The enzyme had a pH optimum at 6.0 and a temperature optimum at $55^{\circ}C$. The enzyme was active on locust bean gum, konjak, guar gum, and lichenan, while it did not exhibit activity towards yeast mannan, laminarin, carboxymethylcellulose, $\beta$­glucan, xylan, and para-nitrophenyl-$\beta$-mannopyranoside.
Keywords
Bacillus subtilis WL-7; mannanase; gene; purification; recombinant Escherichia coli;
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