Background: ␤-L-Arabinofuranosyl linkages are found in many plant biopolymers, but the degradation enzyme has never been found. Results: A novel ␤-L-arabinofuranosidase was found in Bifidobacterium longum. Conclusion: ␤-L-Arabinofuranosidase plays a key role in Bifidobacterium longum for ␤-L-arabinooligosaccharide usage. Significance: The members of the DUF1680 family might be used for the degradation of plant biopolymers.

This article has been withdrawn by the authors. In the original manuscript, the results of E338A and E366A mutants were reversed. We transformed Escherichia coli BL21 (DE3) cells with the E366A plasmid instead of the E338A plasmid when sample tubes were switched inadvertently. The correct E338A and E366A mutants were expressed, purified, and characterized again. The results showed that Glu-338, and not Glu-366, is critical for catalytic activity. We wish to withdraw the manuscript and submit a corrected manuscript. We apologize for any inconvenience caused by this error.

Background: ␤-L-Arabinofuranosyl linkages are found in many plant biopolymers, but the degradation enzyme has never been found. Results: A novel ␤-L-arabinofuranosidase was found in Bifidobacterium longum. Conclusion: ␤-L-Arabinofuranosidase plays a key role in Bifidobacterium longum for ␤-L-arabinooligosaccharides usage. Significance: The members of DUF1680 family might be used for the degradation of plant biopolymers.