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.
- ferulic acid
- fungal laccase
Boeriu, C. G., Oudgenoeg, G., Spekking, W. T. J., Berendsen, L. B. J. M., Vancon, L., Boumans, H., ... Voragen, A. G. J. (2004). Horseradish peroxidase-catalyzed cross-linking of feruloylated arabinoxylans with ß-casein. Journal of Agricultural and Food Chemistry, 52(21), 6633-6639. https://doi.org/10.1021/jf049622k