Motif-Guided Identification of a Glycoside Hydrolase Family 1 α-L-Arabinofuranosidase in Bifidobacterium adolescentis
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概要
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Members of glycoside hydrolase family 1 (GH1) cleave glycosidic linkages with a variety of physiological roles. Here we report a unique GH1 member encoded in the genome of Bifidobacterium adolescentis ATCC 15703. This enzyme, BAD0156, was identified from over 2,000 GH1 sequences accumulated in a database by a genome mining approach based on a motif sequence. A recombinant BAD0156 protein was characterized to confirm that this enzyme alone specifically hydrolyzes p-nitrophenyl-α-L-arabinofuranoside among the 24 p-nitrophenyl-glycosides examined. Among natural glycosides, α-1,5-linked arabino-oligosaccharides served as substrates, but arabinan, debranched arabinan, arabinoxylan, and arabinogalactan did not. A time course analysis of arabino-oligosaccharide hydrolysis indicated that BAD0156 is an exo-acting enzyme. These results suggest that BAD0156 is an α-L-arabinofuranosidase. This is the first report of a GH1 enzyme that acts specifically on arabinosides, providing information on GH1 substrate specificity.
- 公益社団法人 日本農芸化学会の論文
著者
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Yoshida Ken-ichi
Department Of Agrobioscience Graduate School Of Agricultural Science Kobe University
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SUZUKI Hirokazu
Organization of Advanced Science and Technology, Kobe University
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MURAKAMI Ayano
Department of Agrobioscience, Graduate School of Agricultural Science, Kobe University
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