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.