Structure-based protein engineering of bacterial β-xylosidase to increase the production yield of xylobiose from xylose
- Research Institute for Agriculture and Life Sciences, Center for Food and Bioconvergence, Center for Food Safety and Toxicology, Department of Agicultural Biotechnology, Seoul National University, Seoul, 08826 (Korea, Republic of)
- Center for Food and Bioconvergence, Department of Biosystems & Biomaterials Science and Engineering, College of Agriculture and Life Sciences (CALS), Seoul National University, Seoul, 08826 (Korea, Republic of)
Highlights: • The crystal structures of β-xylosidase from Bacillus pumilus in complex with xylobiose were determined. • β-xylosidase was engineered to increase the yield of xylobiose based on the determined structures. • The protein engineering strategy used in this study could be applied within the same family of enzymes. 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.
- OSTI ID:
- 23137015
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 501, Issue 3; Other Information: Copyright (c) 2018 Elsevier Inc. All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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