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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.

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이 논문을 인용한 문헌 (4)

  1. 2007. "" Journal of microbiology and biotechnology, 17(10): 1688~1694 
  2. Yoon, Ki-Hong 2010. "Cloning and Characterization of Mannanase Gene from Bacillus subtilis WL-8" Korean journal of microbiology = 미생물학회지, 46(2): 207~212 
  3. Yoon, Ki-Hong 2010. "Characterization of the Bacillus licheniformis WL-12 Mannanase from a Recombinant Escherichia coli" Journal of applied biological chemistry, 53(2): 71~76 
  4. Jeon, Ho Jin ; Yoon, Ki-Hong 2014. "Comparison of Acidic pH and Temperature Stabilities between Two Bacillus Mannanases Produced from Recombinant Escherichia coli" Korean journal of microbiology = 미생물학회지, 50(4): 327~333 

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