Horseradish peroxidase-catalyzed cross-linking of feruloylated arabinoxylans with ß-casein

C.G. Boeriu, G. Oudgenoeg, W.T.J. Spekking, L.B.J.M. Berendsen, L. Vancon, H. Boumans, H. Gruppen, W.J.H. van Berkel, N.C.M. Laane, A.G.J. Voragen

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Heterologous conjugates of wheat arabinoxylan and beta-casein were prepared via enzymatic cross-linking, using sequential addition of the arabinoxylan to a mixture of beta-casein, peroxidase, and hydrogen peroxide. The maximal formation of adducts between the beta-casein and the feruloylated arabinoxylan was reached at a protein-to-arabinoxylan ratio of 10:1, in combination with a molar ratio hydrogen peroxide to substrate of 2:1 and a molar protein-to-enzyme ratio between 10(2) and 10(4). The protein-arabinoxylan adducts were separated from the arabinoxylan homopolymers by size exclusion and anion exchange chromatography. The molar ratio protein:arabinoxylan in the purified conjugates varied between 0.1 and 5.6. This is the first report on the large-scale enzymatic preparation of heterologous protein-arabinoxylan conjugates.
Original languageEnglish
Pages (from-to)6633-6639
JournalJournal of Agricultural and Food Chemistry
Issue number21
Publication statusPublished - 2004


  • ferulic acid
  • fungal laccase
  • proteins
  • polysaccharides
  • conjugation
  • pentosans
  • bran

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