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Effect of the Degree of Myosin Oxidation on the Production of Advanced Glycation End Products in Channel Catfish |
Lü Xinmeng, GAO Jingyao, ZHOU Zhi, SHI Liu, QIAO Yu, WU Wenjin, LUO Hongyu, HUANG Yun, PENG Tiaofeng, XIONG Guangquan, WANG Lan |
1. College of Biological and Food Engineering, Hubei Minzu University, Enshi 445000, China; 2. Key Laboratory of Cold Chain Logistics Technology for Agro-product, Ministry of Agriculture and Rural Affairs, Institute of Agro-products Processing and Nuclear Agricultural Technology, Hubei Academy of Agricultural Sciences, Wuhan 430064, China; 3. Honghu Wannong Aquatic Food Co. Ltd., Jingzhou 433200, China; 4. Hubei Huachun Food Co. Ltd., Jingmen 420800, China |
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Abstract To investigate the effect of protein oxidation degree on the generation of advanced glycation end products (AGEs) in the subsequent thermal processing of prepared aquatic products, catfish myosin was oxidized to different degrees in the Fenton system, and oxidized myosin was glycated with monosaccharides (glucose) and disaccharides (sucrose) and polysaccharides (dextran). The relationship between the degree of myosin oxidation, different saccharides and AGEs generation was analyzed by measuring protein carbonyl and total sulfhydryl group contents, endogenous fluorescence intensity and surface hydrophobicity, as well as the contents of the glycation intermediates glycoxal (GO) and methylglyoxal (MGO), fluorescent AGEs, Nε-carboxymethyllysine (CML) and Nε-carboxyethyllysine (CEL). The results showed that the carbonyl content and surface hydrophobicity increased, the total sulfhydryl content and endogenous fluorescence intensity decreased with increasing H2O2 content in the system, and the content of GO, MGO, fluorescent AGEs, CML and CEL increased significantly with increasing degree of oxidation of myosin (P < 0.05). Correlation analysis showed that in the reaction products of oxidized myosin with glucose, the CML and CEL contents had a highly significant negative correlation with the total sulfhydryl content (P < 0.01) and the endogenous fluorescence intensity had a highly significant negative correlation with the CML content (P < 0.01) and a significant negative correlated with the CEL content (P < 0.05). In addition, the carbonyl content and the surface hydrophobicity had a highly significant positive correlation with the CML and CEL contents (P < 0.01). In the reaction products of oxidized myosin with dextran, the total sulfhydryl content and the endogenous fluorescence intensity were significantly negatively correlated with the CML content (P < 0.05) and highly significantly negatively correlated with the CEL content (P < 0.01), and the carbonyl content and the surface hydrophobicity had a highly significant positive correlation with the CML and CEL contents (P < 0.01). In the reaction products of oxidized myosin with sucrose, the CEL content was significantly positively correlated with the carbonyl content (P < 0.05), and the increase in GO and MGO contents promoted the formation of AGEs. Therefore, protein oxidation significantly promoted the generation of AGEs in the system, and the rate of glycation with monosaccharides was the highest.
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