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KMID : 0364820090450030257
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Korean Journal of Microbiology
2009 Volume.45 No. 3 p.257 ~ p.262
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Properties of a Bacillus licheniformis Cellulase Produced by Recombinant Escherichia coli
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Park Jong-Duk
Kim Yeon-A
Yoon Ki-Hong
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Abstract
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Carboxymethyl celluase (cellulase) was purified from cell-free extract of the recombinant Escherichia coli carrying a Bacillus licheniformis WL-12 cellulase gene by DEAE-Sepharose and phenyl-Sepharose column chromatography with specific activity of 163 U/mg protein. The molecular mass of the purified enzyme was estimated to be approximately 49.5 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme had a pH optimum at 5.5 and a temperature optimum at 55oC. The activity of the enzyme was completely inhibited by SDS (5 mM), and slightly enhanced by Cu2+ (5 mM). The cellulase was active on CMC, konjac, barely glucan and lichenan, while it did not exhibit activity towards xylan, locust bean gum, and p-nitrophenyl-β-glucopyranoside. The predominant products resulting from the cellulase hydrolysis were cellobiose and cellotriose for cellooligosaccharides including cellotriose, cellotetraose and cellopentaose. The enzyme could hydrolyze cellooligosaccharides larger than cellobiose.
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KEYWORD
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B. licheniformis, cellulase, E. coli, properties, purification
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