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Glycation of β-lactoglobulin and antiglycation by genistein in different reactive carbonyl model systems
- Kong, Yanghui, Li, Xiaoming, Zheng, Tiesong, Lv, Lishuang
- Food chemistry 2015 v.183 pp. 36-42
- Maillard reaction, Pueraria montana var. lobata, advanced glycation end products, beta-lactoglobulin, crosslinking, dose response, genistein, glycation, pH, polyacrylamide gel electrophoresis, soybeans, sugars, temperature
- Advanced glycation end products (AGEs), which are formed in β-lactoglobulin (β-lg) glycation systems via the Maillard reaction, have been implicated in diabetes-related long-term complications. In the present study, we found that reaction conditions, including temperature, time, pH, reactant type and molar ratio of beta-lg to a sugar/MGO/GO, can significantly affect the formation of AGEs. Using SDS–PAGE, we further demonstrated that genistein, a natural isoflavone found in a number of plants including soybeans and kudzu, can efficiently inhibit cross-links of the glycated β-lg, and suppress the formation AGEs in a dose-dependent manner by trapping reactive dicarbonyl compounds. The products formed from genistein and methylglyoxal (MGO) in the β-lg–MGO assay were analyzed using LC/MS. Both mono-MGO and di-MGO adducts of genistein were detected with this method.