Format:
Online-Ressource
ISSN:
1867-3899
Content:
Abstract: Two types of sulfotransferases, namely recombinant rat liver aryl sulfotransferase AstIV and bacterial aryl sulfotransferase from Desulfitobacterium hafniense, were used for the sulfation of quercetin, its glycosylated derivatives (isoquercitrin and rutin), and dihydroquercetin ((+)‐taxifolin). The rat liver enzyme was able to sulfate only quercetin and taxifolin, whereas the quercetin glycosides remained intact. The D. hafniense enzyme sulfated isoquercitrin and rutin selectively at the C‐4′ position of the catechol moiety with very good yields. Taxifolin was sulfated at the C‐4′ position and a minor amount of the C‐3′ isomer was formed. Sulfation of quercetin proceeded preferentially at the C‐3′ position, but a lower proportion of the C‐4′ isomer was formed as well. A detailed analysis of the kinetics of this reaction is provided and a full structural analysis of all products is presented.
In:
volume:7
In:
number:19
In:
year:2015
In:
pages:3152-3162
In:
extent:11
In:
ChemCatChem, Weinheim : Wiley-VCH, 2009-, 7, Heft 19 (2015), 3152-3162 (gesamt 11), 1867-3899
Language:
English
DOI:
10.1002/cctc.201500298
URN:
urn:nbn:de:101:1-2022121805434092869070
URL:
https://doi.org/10.1002/cctc.201500298
URL:
https://nbn-resolving.org/urn:nbn:de:101:1-2022121805434092869070
URL:
https://d-nb.info/1275881378/34
URL:
https://doi.org/10.1002/cctc.201500298
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