Horseradish peroxidase-catalyzed cross-linking of feruloylated arabinoxylans with beta-casein |
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Authors: | Boeriu Carmen G Oudgenoeg Gideon Spekking Willem Th J Berendsen Lucienne B J M Vancon Laetitia Boumans Hans Gruppen Harry van Berkel Willem J H Laane Colja Voragen Alphons G J |
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Institution: | Agrotechnology & Food Innovations, Bornsesteeg 59, 6708 PD Wageningen, The Netherlands. Carmen.Boeriu@wur.nl |
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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. |
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