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

Protein Pept Lett. 2017;24(1):46-55. doi: 10.2174/0929866524666161121144025.


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: allergenicity; chaperone; reduced glycation; structure; β-casein.

MeSH terms

  • Allergens / chemistry*
  • Allergens / immunology
  • Allergens / metabolism
  • Animals
  • Caseins / chemistry*
  • Caseins / immunology
  • Caseins / metabolism*
  • Cattle
  • Child, Preschool
  • Circular Dichroism
  • Glycosylation
  • Humans
  • Immunoglobulin E / metabolism
  • Infant
  • Micelles
  • Milk / chemistry
  • Milk / immunology*
  • Protein Conformation
  • Protein Structure, Secondary


  • Allergens
  • Caseins
  • Micelles
  • Immunoglobulin E