title: Covalent protein adduct formation and protein cross-linking resulting from the maillard reaction between cyclotene and a model food protein.
abstract: 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.
authors.affiliation: New Zealand Institute for Crop and Food Research Limited, Private Bag 4704, Christchurch, New Zealand. j.gerrard@botn.canterbury.ac.nz
authors.forename: J A
authors.initials: JA
authors.lastname: Gerrard
authors.forename: S E
authors.initials: SE
authors.lastname: Fayle
authors.forename: K H
authors.initials: KH
authors.lastname: Sutton
mesh_terms: D002851:Chromatography, High Pressure Liquid; D003517:Cyclopentanes / Q000737:chemistry*; D004044:Dietary Proteins; D005421:Flavoring Agents / Q000737:chemistry*; D015416:Maillard Reaction; D013058:Mass Spectrometry; D008956:Models, Chemical; D011506:Proteins / Q000737:chemistry*; D012259:Ribonuclease, Pancreatic / Q000737:chemistry
chemical_list: D003517:Cyclopentanes; D004044:Dietary Proteins; D005421:Flavoring Agents; D011506:Proteins; C028407:cyclotene; D012259:Ribonuclease, Pancreatic