A Comparative study on the chaperone-like activity of camel and bovine beta-caseins

Molecular chaperones are characterized by a general behavior, arresting the exposed hydrophobic surfaces of denaturing substrate proteins. in the present study, the capacity of ?-caseins (?-cn) from camel and bovine milk in suppression of thermal aggregation process of apo-yeast alcohol dehydrogenase (yadh) was assessed. apo-i enzyme was prepared by removal of the structural zinc; while apo-ii-protein was obtained by depleting conformational and catalytic zinc atoms. fluorescence spectroscopy using ans probe revealed greater hydrophobic surface in apo-ii adh. considerable decrease in aggregation of the heat treated protein molecules was observed upon exposing to ?-cns (camel, bovine). bovine ?-cn afforded more adverse effects on thermal aggregation. a direct correlation between casein’s chaperone activity and structural stability of the substrate proteins was displayed. moreover, an association between casein source and chaperone-like activity is suggested.