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Creating Space for Large Acceptors: Rational Biocatalyst Design for Resveratrol Glycosylation in an Aqueous System
Author(s) -
DirksHofmeister Mareike E.,
Verhaeghe Tom,
De Winter Karel,
Desmet Tom
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201503605
Subject(s) - biocatalysis , glycosylation , chemistry , resveratrol , rational design , aqueous solution , combinatorial chemistry , solubility , organic chemistry , catalysis , biochemistry , nanotechnology , materials science , reaction mechanism
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 =185 m M ) and could be used for the quantitative production of resveratrol 3‐α‐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.