title: Increase of ovalbumin glycation by the maillard reaction after disruption of the disulfide bridge evaluated by liquid chromatography and high resolution mass spectrometry.
abstract: The number of glycation sites of ovalbumin was monitored by Fourier transform ion cyclotron mass spectrometry (FTICR-MS) before and after reducing the pair of the intrachain disulfide bond. Reducing the disulfide bond of the protein greatly improved the reactivity of glycation both in dry-state and solution. The glycation sites identified by MS/MS showed that the major glycation sites of the ovalbumin were lysines. Our results suggest that glycation is strongly dependent on the protein tertiary structure, with significantly stronger reaction when the protein tertiary structure is disrupted after reducing the disulfide bond. The number of glycated sites of the protein was increased from seven to twelve in dry-state and one to two in aqueous solution. The glycation sites were found to be regulated by protein tertiary structure, hydrogen bonding, and neighboring amino acid compositions.
authors: State Key Laboratory of Food Science and Technology, Nanchang University , Nanchang, Jiangxi, 330047, People's Republic of China.
authors: Xiaoqin
authors: X
authors: Huang
authors: Zongcai
authors: Z
authors: Tu
authors: Hui
authors: H
authors: Wang
authors: Qiuting
authors: Q
authors: Zhang
authors: Yan
authors: Y
authors: Shi
authors: Hui
authors: H
authors: Xiao
mesh_terms: D000595:Amino Acid Sequence; D002853:Chromatography, Liquid; D004220:Disulfides / Q000737:chemistry*; D006031:Glycosylation; D008239:Lysine / Q000737:chemistry; D015416:Maillard Reaction; D013058:Mass Spectrometry / Q000379:methods; D008969:Molecular Sequence Data; D010047:Ovalbumin / Q000737:chemistry*; D017434:Protein Structure, Tertiary
chemical_list: D004220:Disulfides; D010047:Ovalbumin; D008239:Lysine