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.
Keywords: β-casein, reduced glycation, structure, chaperone, allergenicity.
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