β-L-arabinofuranoside non-reducing end β-L-arabinofuranosidase
The enzyme, which was identified in the bacterium Bifidobacterium longum JCM1217, removes the β-L-arabinofuranose residue from the non-reducing end of multiple substrates, including β-L-arabinofuranosyl-hydroxyproline (Ara-Hyp), Ara2-Hyp, Ara3-Hyp, and β-L-arabinofuranosyl-(1→2)-1-O-methyl-β-L-arabinofuranose.
In the presence of 1-alkanols, the enzyme demonstrates transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue. cf. EC 188.8.131.52, non-reducing end α-L-arabinofuranosidase
Fujita, K., Takashi, Y., Obuchi, E., Kitahara, K. and Suganuma, T. Characterization of a novel β-L-arabinofuranosidase in Bifidobacterium longum: functional elucidation of a DUF1680 family member. J. Biol. Chem.286 (2011) 38079–38085. [DOI] [PMID: 21914802]