A new aspect to chaperone-like activity of bovine β-casein by protein-protein interactions study.

In the present work, chaperone-like activity of bovine β-casein (β-CN) against thermal denaturation and aggregation processes of bovine carbonic anhydrase (BCA) was investigated. We used different instrument and new developed methods for surveillance the structural alteration of BCA and its functional properties upon interaction with bovine β-CN. The thermodynamic data obtained by DSC showed that interaction of β-CN can enhance the thermal stability of enzyme but due to decrease of activation energy of aggregation, the kinetic of process as driven force accelerated the thermal aggregation. In the presence of β-CN due to enhancement of hydrophobicity and favoring the formation of first intermediate of CA, aggregation conveniently occurred with a higher rate at a low temperature.