Transglycosylation activity of Aspergillus oryzae-derived α-glucosidase
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- Nagayoshi Emi
- Department of Bioscience, Faculty of Bio-environmental Science, Kyoto Gakuen University
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- Ozeki Kenji
- Genome Biotechnology Laboratory, Kanazawa Institute of Technology
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- Hata Mai
- Department of Food Science and Nutrition, Mukogawa Women’s University
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- Minetoki Toshitaka
- Ozeki General Research Laboratory
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- Takii Yukio
- Laboratory of Food Science and Health
書誌事項
- タイトル別名
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- Transglycosilation activity of Aspergillus oryzae-derived α-glucosidase
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説明
An Aspergillus oryzae RIB40 (NBRC100959) α-glucosidase （designed as AgdB）gene (agdB) was expressed at high levels in an A. oryzae host by self-cloning. The obtained transformant (MIBA1002) produced intracellular and extracellular α-glucosidase at levels 3- and 10-fold higher, respectively, than the parent host strain. The base sequence of agdB consisted of a 3036-kb structural gene containing three introns and encoding 963 amino acids, and the linear sequence thus obtained from these amino acids was identical to A. oryzae RIB40 unknown protein BAE64257.1. The amino acid sequence had 72% and 51% homology to α-glucosidase B from Aspernillus nidulans and Acremonium implicatum, respectively, which exhibit transglycosylation activity. The sequence has conserved residues specific to glucosyl hydrase family 31 (GH31) α-glucosidases. Tyr296 present in the β→α Loop1 in GH31 is important for transglycosylation. The enzyme produced 2.2% isomaltose, 0.4% maltotriose, and 0.3% kojibiose from 20% maltose substrate. This is the first report of the transglycosylation activity of α-glucosidase B cloned in A. oryzae (unknown protein BAE64257.1).
収録刊行物
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- Journal of Biological Macromolecules
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Journal of Biological Macromolecules 15 (1), 13-27, 2015
日本生物高分子学会