Some physico-chemical properties and structural changes of bovine beta-casein upon glycation

The studies on casein structure modification contribute to better understanding of the role of nonamino acid components in forming casein complexes and improving ways of protein functionality. The objective of the experiments was to explain the influence of bovine milk casein glycation on some physico-chemical properties and structural changes. From the the analysis of glycation rate curve the reaction of the first order range can be assumed during the first 24 h, turning to a mixed type afterwards. The isoelectric point and molecular weight of beta-casein increased after glycation and the electrophoretic mobility was slightly modified. The structural changes were also confirmed by different absorption spectra in UV and a better heat stability of the modified beta-casein. The findings showed higher solubility with modified beta-casein. The glycation caused changes in beta-casein, modifying its susceptibility to the trypsin hydrolysis.