Structure-based protein engineering of bacterial β-xylosidase to increase the production yield of xylobiose from xylose

Biochemical and Biophysical Research Communications
Seokho HongNam-Chul Ha

Abstract

Xylobiose consists of two molecules of xylose and has been highly recognized as a food supplement because it possesses high prebiotic functions. β-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, β-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.

Citations

Mar 8, 2019·Interface Focus·Mounir BenkouloucheIsabelle André
Nov 9, 2019·International Journal of Molecular Sciences·Ali RohmanNi Nyoman Tri Puspaningsih
Mar 12, 2020·Biotechnology and Bioengineering·Misha AliQayyum Husain

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