期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 61, 期 12, 页码 3140-3147出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf305451p
关键词
alpha-aminoadipic semialdehyde; gamma-glutamic semialdehyde; AGEs; protein oxidation; Maillard reaction
资金
- Spanish Ministry of Economics and Competitiveness (SMEC) [RYC-2009-03901, AGL2010-15134]
- Executive Research Agency from the European Community [PERG05-GA-2009-248959]
- FPI grant from the SMEC
Carbonylation is recognized as one of the most remarkable chemical modifications in oxidized proteins and is generally ascribed to the direct attack of free radicals to basic amino acid residues. The purpose of this work was to investigate the formation of specific carbonyls, alpha-aminoadipic and gamma-glutamic semialdehydes (AAS and GGS, respectively), in myofibrillar proteins (MP) through a Mail lard-type pathway in the presence of reducing sugars. The present study confirmed the concurrent formation of protein carbonyls and advanced glycation end-products (AGEs) during incubation (80 degrees C/48 h) of MP (4 mg/mL) in the presence of reducing sugars (0.5 M). Copper irons (10 mu M) were found to promote the formation of protein carbonyls, and a specific inhibitor of the Maillard reaction (0.02 M pyridoxamine) blocked the carbonylation process which emphasize the occurrence of a Maillard-type pathway. The Maillard-mediated carbonylation occurred in a range of reducing sugars (0.02-0.5 M) and reaction temperatures (4-110 degrees C) compatible with food systems. Upcoming studies on this topic may contribute further to shed light on the complex interactions between protein oxidation and the Maillard reaction and the impact of the protein damage on food quality and human health.
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