Evaluation of structure,chaperone-like activity and allergenicity of reduced glycated adduct of bovine β-casein

Milk has a potent reducing environment with an important quantity of sugar levels. in the current study β-casein was glycated in the presence of d-glucose and sodium cyanoborohydride as a reducing agent. then,the reduced glucitol adduct of β-casein was used for the structural and functional analyses using different spectroscopic techniques. the results of fluorescence and far ultraviolet circular dichroism assessments suggest important structural alteration upon non-enzymatic glycation of β-casein. in addition,the chaperone activity,micellization properties and antioxidant activity of this protein were altered upon glucose modification. also,as a result of reduced glycation,the allergenicity profile of this protein remained largely unchanged. additional to its energetic and nutritional values,β-casein has important functional properties. the native structure of this protein is important to perform accurately its biological functions. non-enzymatic glycation under reducing state was capable to alter both structural and functional aspects of β-casein. due to effective reducing environment and significant quantity of reducing sugar of human milk,similar structural and functional alterations are most likely to occur upon reducing glycation of β-casein in vivo. also,these changes might be even intensified during chronic hyperglycemia in diabetic mothers. © 2017 bentham science publishers.