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KMID : 0880220120500061041
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Journal of Microbiology
2012 Volume.50 No. 6 p.1041 ~ p.1046
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Detailed modes of action and biochemical characterization of endo-arabinanase from Bacillus licheniformis DSM13
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Park Jung-Mi
Jang Myoung-Uoon
Kang Jung-Hyun
Kim Min-Jeong
Lee So-Won
Han Nam-Soo
Kim Tae-Jip
Song Yeong-Bok
Shin Chul-Soo
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Abstract
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An endo-arabinanase (BLABNase) gene from Bacillus licheniformis DSM13 was cloned and expressed in Escherichiacoli, and the biochemical properties of its encoded enzyme were characterized. The BLABNase gene consists of a single open reading frame of 987 nucleotides that encodes 328 amino acids with a predicted molecular mass of about 36 kDa. BLABNase exhibited the highest activity against debranched α-(1,5)-arabinan in 50 mM sodium acetate buffer (pH 6.0) at 55°C. Enzymatic characterization revealed that BLABNase hydrolyzes debranched or linear arabinans with a much higher activity than branched arabinan from sugar beet. Enzymatic hydrolysis pattern analyses demonstrated BLABNase to be a typical endo-(1,5)-α-s-arabinanase (EC 3.2.1.99) that randomly cleaves the internal α-(1,5)-linked L-arabinofuranosyl residues of a branchless arabinan backbone to release arabinotriose mainly, although a small amount of arabino-oligosaccharide intermediates is also liberated. Our results indicated that BLABNase acts preferentially along with the oligosaccharides longer than arabinopentaose, thus enabling the enzymatic production of various arabino-oligosaccharides.
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KEYWORD
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Bacillus licheniformis DSM13, endo-(1, 5)-α-l-arabinanase, gene expression, enzymatic hydrolysis patterns, arabino-oligosaccharides production
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