Abstract
UDP-glycosyltransferases (UGTs) are a promising class of biocatalysts
that offer a sustainable alternative for chemical glycosylation of
natural products. In this study, we aimed to characterize plant-derived
UGTs from the GT-1 family with an emphasis on their acceptor promiscuity
and their potential application in glycosylation processes. Recombinant
expression in E. coli provided sufficient amounts of enzyme for the in-depth characterization of the salicylic acid UGT from Capsella rubella (UGT-SACr) and the stevia UGT from Stevia rebaudiana (UGT-76G1Sr).
The latter was found to have a remarkably broad specificity with
activities on a wide diversity of structures, from aliphatic and
branched alcohols, over small phenolics to larger flavonoids, terpenoids
and even higher glycoside compounds. As an example for its industrial
potential, the glycosylation of curcumin was thoroughly evaluated. Under
optimized conditions, 96% of curcumin was converted within 24 h into
the corresponding curcumin β-glycosides. In addition, the reaction was
performed in a coupled system with sucrose synthase from Glycine max, to enable the cost-efficient (re)generation of UDP-Glc from sucrose as abundant and renewable resource.
Original language | English |
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Pages (from-to) | 49-55 |
Journal | Journal of Biotechnology |
Volume | 233 |
DOIs | |
Publication status | Published - 1 Jun 2016 |
Fields of Expertise
- Human- & Biotechnology
Treatment code (Nähere Zuordnung)
- Basic - Fundamental (Grundlagenforschung)