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KMID : 0364820140500040327
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Korean Journal of Microbiology
2014 Volume.50 No. 4 p.327 ~ p.333
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Comparison of Acidic pH and Temperature Stabilities between Two Bacillus Mannanases Produced from Recombinant Escherichia coli
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Jeon Ho-Jin
Yoon Ki-Hong
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Abstract
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Two genes encoding the mannanase of Bacillus sp. YB-1401 and B. amyloliquefaciens YB-1402, which had been
isolated at acidic pH as mannanase producers, were each cloned into Escherichia coli, and sequenced. Both
mannanase genes consisted of 1,080 nucleotides, encoding polypeptides of 360 amino acid residues. The deduced
amino acid sequences of the two mannanase genes differed by four amino acid residues different, and were highly
homologous to those of mannanases belonging to the glycosyl hydrolase family 26. Comparison of two mannanases
produced from recombinant E. coli indicated that His-tagged mannanase of YB-1402 (HtMAN1402) was more
stable than that of YB-1401 at acidic pH and high temperature. In particular, HtMAN1402 retained more than 50%
of its activity at pH 3.0 after 4 h of pre-incubation, suggesting the enzyme is a valuable candidate for use as a feed
additive. In addition, thermostability of the two mannanases was found to be enhanced by Ca2+ ions.
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KEYWORD
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Bacillus, acidic pH, mannanase gene, stability
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