Horseradish peroxidase-catalyzed cross-linking of feruloylated arabinoxylans with β-casein
article
Heterologous conjugates of wheat arabinoxylan and β-casein were prepared via enzymatic cross-linking, using sequential addition of the arabinoxylan to a mixture of β-casein, peroxidase, and hydrogen peroxide. The maximal formation of adducts between the β-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 102 and 104. 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.
Topics
Food technologyβ-caseinArabinoxylanCross-linkingHeterocouplingPeroxidasesProteinArabinoxylanBeta caseinHorseradish peroxidaseHydrogen peroxideAnion exchange chromatographyCatalysisEnzyme isolationGel permeation chromatographyProtein cross linkingWheatCaseinsCoumaric AcidsCross-Linking ReagentsHorseradish PeroxidaseSpectroscopy, Fourier Transform InfraredTriticumXylansArmoracia rusticanaTriticum aestivum
TNO Identifier
238057
ISSN
00218561
Source
Journal of Agricultural and Food Chemistry, 52(21), pp. 6633-6639.
Pages
6633-6639
Files
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