Horseradish Peroxidase-Catalyzed Cross-Linking of Feruloylated Arabinoxylans with β-Casein

• DOI: 10.1021/jf049622k
• Publication Date: 2004-10-13T05:07:34Z
• Authors: Carmen G. Boeriu; Gideon Oudgenoeg; Willem Th. J. Spe...; Lucienne B. J. M....; Laetitia Vancon; Hans Boumans; Harry Gruppen; Willem J. H. van ...; Colja Laane; Alphons G. J. Vor...
• Keywords: Coumaric Acids; bran; polysaccharides; Caseins; 04 agricultural and veterinary sciences; proteins; pentosans; Cross-Linking Reagents; fungal laccase; Spectroscopy, Fourier Transform Infrared; Xylans; 0405 other agricultural sciences; Horseradish Peroxidase; Triticum; conjugation; ferulic acid

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.