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Biochemical and in silico characterization of glycosyltransferases from red sweet cherry (Prunus avium L.) reveals their broad specificity toward phenolic substrates

Clayton-Cuch, Daniel (författare)
Adelaide Glycomics, University of Adelaide, School of Agriculture, Food and Wine, Waite Campus, Adelaide, South Australia, Australia, Waite Campus; CSIRO, Waite Campus, Glen Osmond, SA 5064, Australia, Waite Campus
Yu, Long (författare)
Adelaide Glycomics, University of Adelaide, School of Agriculture, Food and Wine, Waite Campus, Adelaide, South Australia, Australia, Waite Campus
McDougal, Daniel (författare)
Institute for Photonics and Advanced Sensing, (IPAS), School of Biological Sciences, The University of Adelaide, Adelaide, South Australia 5005, Australia
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Burbidge, Crista A. (författare)
CSIRO, Waite Campus, Glen Osmond, SA 5064, Australia, Waite Campus
Bruning, John B. (författare)
Institute for Photonics and Advanced Sensing, (IPAS), School of Biological Sciences, The University of Adelaide, Adelaide, South Australia 5005, Australia
Bradley, David (författare)
Agilent Technologies Australia Pty Ltd, Mulgrave, Melbourne, Victoria, Australia, Mulgrave
Böttcher, Christine (författare)
CSIRO, Waite Campus, Glen Osmond, SA 5064, Australia, Waite Campus
Bulone, Vincent (författare)
KTH,Glykovetenskap,Adelaide Glycomics, University of Adelaide, School of Agriculture, Food and Wine, Waite Campus, Adelaide, South Australia, Australia, Waite Campus
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 (creator_code:org_t)
Elsevier BV, 2024
2024
Engelska.
Ingår i: Food Chemistry: Molecular Sciences. - : Elsevier BV. - 2666-5662. ; 8
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
Stäng  
  • Polyphenolic compounds are a class of phytonutrients that play important roles in plants and contribute to human health when incorporated into our diet through fruit consumption. A large proportion occur as glycoconjugates but the enzymes responsible for their glycosylation are poorly characterized. Here, we report the biochemical and structural characterization of two glycosyltransferases from sweet cherry named PaUGT1 and PaUGT2. Both are promiscuous glucosyltransferases active on diverse anthocyanidins and flavonols, as well as phenolic acids in the case of PaUGT1. They also exhibit weaker galactosyltransferase activity. The expression of the gene encoding PaUGT1, the most active of the two proteins, follows anthocyanin accumulation during fruit ripening, suggesting that this enzyme is the primary glycosyltransferase involved in flavonoid glycosylation in sweet cherry. It can potentially be used to synthesize diverse glycoconjugates of flavonoids for integration into bioactive formulations, and for generating new fruit cultivars with enhanced health-promoting properties using breeding methods.

Ämnesord

LANTBRUKSVETENSKAPER  -- Lantbruksvetenskap, skogsbruk och fiske -- Livsmedelsvetenskap (hsv//swe)
AGRICULTURAL SCIENCES  -- Agriculture, Forestry and Fisheries -- Food Science (hsv//eng)

Nyckelord

Anthocyanins
Cherry
Flavonols
Glycosyltransferase
Phenolic compounds
Protein structure modelling

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