Journal of Applied Glycoscience
Online ISSN : 1880-7291
Print ISSN : 1344-7882
Regular Paper
Characterization of a GH36 β-L-Arabinopyranosidase in Bifidobacterium adolescentis
Yuki SasakiNami TogoKanefumi KitaharaKiyotaka Fujita
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Volume 65 (2018) Issue 2 Pages 23-30

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Abstract

β-L-Arabinopyranosidases are classified into the glycoside hydrolase family 27 (GH27) and GH97, but not into GH36. In this study, we first characterized the GH36 β-L-arabinopyranosidase BAD_1528 from Bifidobacterium adolescentis JCM1275. The recombinant BAD_1528 expressed in Escherichia coli had a hydrolytic activity toward p-nitrophenyl (pNP)-β-L-arabinopyranoside (Arap) and a weak activity toward pNP-α-D-galactopyranoside (Gal). The enzyme liberated L-arabinose efficiently not from any oligosaccharides or polysaccharides containing Arap-β1,3-linkages, but from the disaccharide Arap-β1,3-L-arabinose. However, we were unable to confirm the in vitro fermentability of Arap-β1,3-Ara in B. adolescentis strains. The enzyme also had a transglycosylation activity toward 1-alkanols and saccharides as acceptors.

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© 2018 by The Japanese Society of Applied Glycoscience
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