Beta-L-arabinofuranosidase that removes the beta-L-arabinofuranose residue from the non-reducing end of various substrates, including beta-L-arabinofuranosyl-hydroxyproline (Ara-Hyp), Ara-beta-1,2-Ara-beta-Hyp (Ara(2)-Hyp), Ara-beta-1,2-Ara-beta-1,2-Ara-beta-Hyp (Ara(3)-Hyp), and beta-L-arabinofuranosyl-(1->2)-1-O-methyl-beta-L-arabinofuranose. In the presence of 1-alkanols, shows transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue. beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranose + H2O = 2 beta-L-arabinofuranose Zn(2+) ion is involved in the catalytic reaction through maintaining the proper configuration of active site. Strongly inhibited in the presence of thiol modifiers, suggesting a crucial role for cysteine residues in catalysis. Slightly inhibited by EDTA. kcat is 2.0 sec(-1) with beta-Ara2. kcat is 0.013 sec(-1) with Ara-Hyp. kcat is 6.3 sec(-1) with Ara(2)-Hyp. Homodimer in solution. Belongs to the glycosyl hydrolase 127 family. The original article describing the function has been retracted because the results of E338A and E366A mutants were reversed. The authors later submitted a corrected manuscript.