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Peroxidase-mediated cross-linking of a tyrosine-containing peptide with ferulic acid

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Author: Oudgenoeg, G. · Hilhorst, R. · Piersma, S.R. · Boeriu, C.G. · Gruppen, H. · Hessing, M. · Voragen, A.G.J. · Laane, C.
Type:article
Date:2001
Institution: Centraal Instituut voor Voedingsonderzoek TNO
Source:Journal of Agricultural and Food Chemistry, 5, 49, 2503-2510
Identifier: 57208
doi: doi:10.1021/jf000906o
Keywords: Nutrition · Coumaric Acids · Cross-Linking Reagents · Gas Chromatography-Mass Spectrometry · Horseradish Peroxidase · Hydrogen Peroxide · Oxidation-Reduction · Tyrosine

Abstract

The tyrosine-containing peptide Gly-Tyr-Gly (GYG) was oxidatively cross-linked by horseradish peroxidase in the presence of hydrogen peroxide. As products, covalently coupled di- to pentamers of the peptide were identified by LC-MS. Oxidative cross-linking of ferulic acid with horseradish peroxidase and hydrogen peroxide resulted in the formation of dehydrodimers. Kinetic studies of conversion rates of either the peptide or ferulic acid revealed conditions that allow formation of heteroadducts of GYG and ferulic acid. To a GYG-containing incubation mixture was added ferulic acid in small aliquots, therewith keeping the molar ratio of the substrates favorable for heterocross-linking. This resulted in a predominant product consisting of two ferulic acid molecules dehydrogenatively linked to a single peptide and, furthermore, two ferulic acids linked to peptide oligomers, ranging from dimers to pentamers. Also, mono- and dimers of the peptide were linked to one molecule of ferulic acid. A mechanism explaining the formation of all these products is proposed. Chemicals/CAS: Coumaric Acids; Cross-Linking Reagents; ferulic acid, 1135-24-6; Horseradish Peroxidase, EC 1.11.1.-; Hydrogen Peroxide, 7722-84-1; Tyrosine, 55520-40-6