Evaluation of Structure, Chaperone-Like Activity and Allergenicity of Reduced Glycated Adduct of Bovine β-casein

Publisher: Bentham Science Publishers

E-ISSN: 1875-5305|24|1|46-55

ISSN: 0929-8665

Source: Protein and Peptide Letters, Vol.24, Iss.1, 2016-12, pp. : 46-55

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Abstract

Milk has a potent reducing environment with an important quantity of sugar levels. In thecurrent study #946;-casein was glycated in the presence of D-glucose and sodium cyanoborohydride as areducing agent. Then, the reduced glucitol adduct of #946;-casein was used for the structural and functionalanalyses using different spectroscopic techniques. The results of fluorescence and far ultravioletcircular dichroism assessments suggest important structural alteration upon non-enzymatic glycationof #946;-casein. In addition, the chaperone activity, micellization properties and antioxidant activityof this protein were altered upon glucose modification. Also, as a result of reduced glycation, theallergenicity profile of this protein remained largely unchanged. Additional to its energetic and nutritionalvalues, #946;-casein has important functional properties. The native structure of this protein isimportant to perform accurately its biological functions. Non-enzymatic glycation under reducingstate was capable to alter both structural and functional aspects of #946;-casein. Due to effective reducingenvironment and significant quantity of reducing sugar of human milk, similar structural and functionalalterations are most likely to occur upon reducing glycation of ?-casein in vivo. Also, thesechanges might be even intensified during chronic hyperglycemia in diabetic mothers.