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

J Agric Food Chem. 2004 Oct 20;52(21):6633-9. doi: 10.1021/jf049622k.

Abstract

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.

MeSH terms

  • Caseins / metabolism*
  • Coumaric Acids / metabolism*
  • Cross-Linking Reagents
  • Horseradish Peroxidase / metabolism*
  • Spectroscopy, Fourier Transform Infrared
  • Triticum / chemistry
  • Xylans / metabolism*

Substances

  • Caseins
  • Coumaric Acids
  • Cross-Linking Reagents
  • Xylans
  • arabinoxylan
  • ferulic acid
  • Horseradish Peroxidase