American Journal of Biochemistry and Biotechnology

The Effect of Molecular Chaperone, Alpha-Crystallin, on the Heat-Induced Aggregation of Beta-lactoglobulin

Arezou Ghahghaei

DOI : 10.3844/ajbbsp.2008.317.324

American Journal of Biochemistry and Biotechnology

Volume 4, Issue 4

Pages 317-324


Aggregation of beta-lactoglobulin occurs mainly via intermolecular disulphide bond exchange. Upon heating, beta-lactoglobulin aggregated which increased with increasing pH. The presence of DTT led to more rapid aggregation and precipitation of beta-lactoglobulin. Alpha-Crystallin prevented the aggregation of heat-stressed beta-lactoglobulin and was a more efficient chaperone at higher pH values. In the presence of DTT, however, alpha-crystallin was a less efficient chaperone due to faster aggregation of heated and reduced beta-lactoglobulin.


© 2008 Arezou Ghahghaei. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.