Enzymatic acylation of flavonoid glycosides by a carbohydrate esterase of family 16 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2014-11

AUTHORS

Peter Biely, Mária Cziszárová, Ken K. Y. Wong, Alan Fernyhough

ABSTRACT

The acetyl esterase of Trichoderma reesei belonging to carbohydrate esterase (CE) family 16 catalyzes transacylations to carbohydrate moieties of flavonoid glycosides, esculin and rutin. The enzyme recognizes as acyl donors vinyl esters of short carboxylic acids. Esculin was acylated at position 3 of the glucosyl residue in aqueous solutions saturated with vinyl acetate and vinyl propionate. The yields of esculin monoacetate and monopropionate of esculin in aqueous medium (esculin 40 mM, enzyme 40 µg/ml, 40 °C, 3 days) were 67 and 55 %, respectively. Replacement of water by 2-propanol was required for a similar acylation of rutin at 4 mM concentration. The yields of rutin monoacetate and propionate were 60 and 30 %, respectively. The results indicate that the enzyme could be used for an easy modification of solubility and hydrophobicity of glycosylated compounds, including drugs and functional food additives. More... »

PAGES

2249-2255

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10529-014-1599-x

DOI

http://dx.doi.org/10.1007/s10529-014-1599-x

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1037085359

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/25048225


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