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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 ( p NP)-β-L-arabinopyranoside (Ara p ) and a weak activity toward p NP-α-D-galactopyranoside (Gal). The enzyme liberated L-arabinose efficiently not from any oligosaccharides or polysaccharides containing Ara p -β1,3-linkages, but from the disaccharide Ara p -β1,3-L-arabinose. However, we were unable to confirm the in vitro fermentability of Ara p -β1,3-Ara in B. adolescentis strains. The enzyme also had a transglycosylation activity toward 1-alkanols and saccharides as acceptors.

Characterization of a GH36 β-L-Arabinopyranosidase in <i>Bifidobacterium adolescentis</i>