Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 54, Issue 32, Pages 9289-9292Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201503605
Keywords
biocatalysis; glycosylation; protein engineering; resveratrol; sucrose phosphorylase
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Funding
- EC (FP7-project Novosides) [KBBE-4-265854]
- Fund for Scientific Research-Flanders (FWO-Vlaanderen)
- Ghent University (Ghent Bio-Economy)
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Polyphenols display a number of interesting properties but their low solubility limits practical applications. In that respect, glycosylation offers a solution for which sucrose phosphorylase has been proposed as a cost-effective biocatalyst. However, its activity on alternative acceptor substrates is too low for synthetic purposes and typically requires the addition of organic (co-)solvents. Here, we describe the engineering of the enzyme from Thermoanaerobacterium thermosaccharolyticum to enable glycosylation of resveratrol as test case. Based on docking and modeling studies, an active-site loop was predicted to hinder binding. Indeed, the unbolted loop variant R134A showed useful affinity for resveratrol (K-m=185mM) and could be used for the quantitative production of resveratrol 3--glucoside in an aqueous system. Improved activity was also shown for other acceptors, introducing variant R134A as promising new biocatalyst for glycosylation reactions on bulky phenolic acceptors.
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