Easy Sulphation of Phenols by a Bacterial Arylsulphotransferase

Authors
Publication date 2021
Host editors
  • J. Whitall
  • P.W. Sutton
Book title Applied Biocatalysis
Book subtitle The Chemist’s Enzyme Toolbox
ISBN
  • 9781119487012
ISBN (electronic)
  • 9781119487043
  • 9781119487029
  • 9781119487036
Chapter 10.4
Pages (from-to) 381-386
Publisher Hoboken, NJ : Wiley
Organisations
  • Faculty of Science (FNWI) - Van 't Hoff Institute for Molecular Sciences (HIMS)
Abstract
The use of an enzymatic method to synthesise sulfated compounds is gaining more and more ground. The popularity is mainly due to the availability of bacterial arylsulfotransferaes (ATSs) and the convenient expression methods of the recombinant enzymes. Unlike the eukaryotic sulfotransferases, which use the very expensive 3' phosphoadenosine-5'phosphosulfate (PAPS) and are in general substrate-specific, these bacterial enzymes use cheap sulfate donors such as p-nitrophenyl sulfate (p-NPS) and N-hydroxysuccinimide sulfate. Many different compounds, including nonphenolics, have been reported to be sulfated under mild conditions. We have developed and used the recombinant AST from Desulfitobacterium hafniense, which is easily expressed in Escherichia coli. Here, we report as an example the enzymatic sulfation of E-resveratrol. Through careful selection of the concentration of the donor and the incubation time, it was possible to obtain the four different sulfated resveratrol derivatives.
Document type Chapter
Note Part of chapter 10: Glycosylation, Sulfation and Phosphorylation.
Language English
Published at https://doi.org/10.1002/9781119487043.ch10
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