Covalent Protein Adduct Formation and Protein Cross-Linking Resulting from the Maillard Reaction between Cyclotene and a Model Food Protein

• Published in: Journal of agricultural and food chemistry Vol. 47; no. 3; pp. 1183 - 1188
• Main Authors: Gerrard, Juliet A, Fayle, Sian E, Sutton, Kevin H
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 01.03.1999
• Subjects: Biological and medical sciences; Chromatography, High Pressure Liquid; Cyclopentanes - chemistry; Dietary Proteins; flavor compounds; Flavoring Agents - chemistry; Food industries; Fundamental and applied biological sciences. Psychology; General aspects; high performance liquid chromatography; Maillard Reaction; Maillard reaction products; Mass Spectrometry; Miscellaneous; Models, Chemical; Proteins - chemistry; reaction mechanisms; Ribonuclease, Pancreatic - chemistry; ribonucleases; size exclusion hplc; spectral analysis; Schiff base; Reaction intermediate; Carbonyl compounds; Chemical reaction; Reaction mechanism; Maillard reaction; Crosslinking; Protein
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/jf980811a

Covalent Maillard products of the reactions of carbonyl compounds with proteins are often described in the literature, but, until recently, evidence for their existence has been indirect. Cyclotene (2-hydroxy-3-methylcyclopent-2-enone), a common flavor compound, was incubated with a model food protein, ribonuclease, and found to cross-link the protein. Size exclusion high-performance liquid chromatrography and electrospray mass spectrometry of the early stages of the reaction provide strong evidence for covalent adducts that we believe to be intermediates in the cross-linking reaction. Keywords: Cyclotene; cross-link; Maillard reaction; ribonuclease