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http://dx.doi.org/10.4014/jmb.1411.11055

Synergistic Action Modes of Arabinan Degradation by Exo- and Endo-Arabinosyl Hydrolases  

Park, Jung-Mi (Department of Food Science and Biotechnology, and Brain Korea 21 Center for Bio-Resource Development, Chungbuk National University)
Jang, Myoung-Uoon (Department of Food Science and Biotechnology, and Brain Korea 21 Center for Bio-Resource Development, Chungbuk National University)
Oh, Gyo Won (Department of Food Science and Biotechnology, and Brain Korea 21 Center for Bio-Resource Development, Chungbuk National University)
Lee, Eun-Hee (Department of Food Science and Biotechnology, and Brain Korea 21 Center for Bio-Resource Development, Chungbuk National University)
Kang, Jung-Hyun (Department of Food Science and Biotechnology, and Brain Korea 21 Center for Bio-Resource Development, Chungbuk National University)
Song, Yeong-Bok (Sejeon Food Research Institute, Sejeon Co.)
Han, Nam Soo (Department of Food Science and Biotechnology, and Brain Korea 21 Center for Bio-Resource Development, Chungbuk National University)
Kim, Tae-Jip (Department of Food Science and Biotechnology, and Brain Korea 21 Center for Bio-Resource Development, Chungbuk National University)
Publication Information
Journal of Microbiology and Biotechnology / v.25, no.2, 2015 , pp. 227-233 More about this Journal
Abstract
Two recombinant arabinosyl hydrolases, α-L-arabinofuranosidase from Geobacillus sp. KCTC 3012 (GAFase) and endo-(1,5)-α-L-arabinanase from Bacillus licheniformis DSM13 (BlABNase), were overexpressed in Escherichia coli, and their synergistic modes of action against sugar beet (branched) arabinan were investigated. Whereas GAFase hydrolyzed 35.9% of L-arabinose residues from sugar beet (branched) arabinan, endo-action of BlABNase released only 0.5% of L-arabinose owing to its extremely low accessibility towards branched arabinan. Interestingly, the simultaneous treatment of GAFase and BlABNase could liberate approximately 91.2% of L-arabinose from arabinan, which was significantly higher than any single exo-enzyme treatment (35.9%) or even stepwise exo- after endo-enzyme treatment (75.5%). Based on their unique modes of action, both exo- and endo-arabinosyl hydrolases can work in concert to catalyze the hydrolysis of arabinan to L-arabinose. At the early stage in arabinan degradation, exo-acting GAFase could remove the terminal arabinose branches to generate debranched arabinan, which could be successively hydrolyzed into arabinooligosaccharides via the endo-action of BlABNase. At the final stage, the simultaneous actions of exo- and endo-hydrolases could synergistically accelerate the L-arabinose production with high conversion yield.
Keywords
Synergistic effect; $\alpha$-L-arabinofuranosidase; endo-(1,5)-$\alpha$-L-arabinanase; arabinan degradation; L-arabinose;
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