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KMID : 1094720100150040590
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Biotechnology and Bioprocess Engineering
2010 Volume.15 No. 4 p.590 ~ p.594
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Characterization of a recombinant endo-1,5-α-l-arabinanase from the isolated bacterium Bacillus licheniformis
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Seo Eun-Seon
Lim Yu-Ri
Kim Yeong-Su
Park Chang-Su
Oh Deok-Kun
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Abstract
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The bacterium Bacillus licheniformis, which exhibits high hydrolytic activity toward arabinan, was isolated from soil, and its gene encoding endo-1,5-α-l-arabinanase was cloned and sequenced. The gene has an open reading frame that encodes 328 amino acids, including a signal peptide of 37 amino acids. Endo-1,5-α-l-arabinanase, a member of glycosyl hydrolase family 43, was expressed in Escherichia coli and purified as a 34-kD monomer with a specific activity of 27 U/mg. Optimal activity toward debranched arabinan (linear 1,5-α-l-arabinan) occurred at pH 6.0 and 35°C, with a k cat of 160/sec and a K m of 19 mg/mL.
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KEYWORD
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endo-1,5-α-l-arabinanase, Bacillus licheniformis, arabinan, gene cloning, screening, characterization
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