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

Mehran Miroliaei, Mozhgan Shirazi, Reza Yousefi



     Molecular chaperones are characterized by a general behavior, arresting the exposed hydrophobic surfaces of denaturing substrate proteins. In the present study, the capacity of β-caseins (β-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 β-CNs (camel, bovine). Bovine β-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.


β-casein; Aggregation; Yeast Alcohol Dehydrogenase; Apo-Enzyme; Aggregation; 8 Anilino-1-Naphthalenesulfonic Acid (ANS)

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DOI: https://doi.org/10.22037/jps.v2i1.2142


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"Journal of Paramdedical Sciences", is a publication of "School of Paramedical Sciences, Shahid Beheshti University of Medical Sciences" and "Iranian Society of Medical Proteomics".

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EISSN: 2008-4978

PISSN: 2008-496X