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Publication Abstract from PubMed

Xylobiose consists of two molecules of xylose and has been highly recognized as a food supplement because it possesses high prebiotic functions. beta-xylosidase exhibits enzymatic activity to hydrolyze xylobiose, and the enzyme can also catalyze the reverse reaction in the presence of high concentrations of xylose. Previously, beta-xylosidase from Bacillus pumilus IPO (BpXynB), belonging to GH family 43, was employed to produce xylobiose from xylose. To improve the enzymatic efficiency, this study determined the high-resolution structure of BpXynB in a complex with xylobiose and engineered BpXynB based on the structures. The structure of BpXynB deciphered the residues involved in the recognition of the xylobiose. A site-directed mutation at the residue for xylobiose recognition increased the yield of xylobiose by 20% compared to a similar activity of the wild type enzyme. The complex structure of the mutant enzyme and xylobiose provided the structural basis for a higher yield of the engineered protein. This engineered enzyme would enable a higher economic production of xylobiose, and a similar engineering strategy could be applied within the same family of enzymes.

Structure-based protein engineering of bacterial beta-xylosidase to increase the production yield of xylobiose from xylose.,Hong S, Kyung M, Jo I, Kim YR, Ha NC Biochem Biophys Res Commun. 2018 Jun 27;501(3):703-710. doi:, 10.1016/j.bbrc.2018.05.051. PMID:29752942^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.