| Title |
Detailed Modes of Action and Biochemical Characterization of endo-Arabinanase from Bacillus licheniformis DSM13 |
| Author |
Jung-Mi Park1, Myoung-Uoon Jang1, Jung-Hyun Kang1, Min-Jeong Kim1, So-Won Lee1, Yeong Bok Song2, Chul-Soo Shin3, Nam Soo Han1, and Tae-Jip Kim1* |
| Address |
1Department of Food Science and Technology, Chungbuk National University, Cheongju 361-763, Republic of Korea, 2Sejeon Food Research Institute, Sejeon Co., Seongnam 462-807, Republic of Korea, 3Advanced Protein Technology Co., Suwon 443-813, Republic of Korea |
| Bibliography |
Journal of Microbiology, 50(6),1041-1046, 2012,
|
| DOI |
|
| Key Words |
Bacillus licheniformis DSM13, endo-(1,5)-α-L-arabinanase, gene expression, enzymatic hydrolysis patterns, arabino-oligosaccharides production |
| Abstract |
An endo-arabinanase (BLABNase) gene from Bacillus licheniformis DSM13 was cloned and expressed in Escherichia coli, 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-L-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 arabinooligosaccharides. |
