SOME PHYSICOCHEMICAL PROPERTIES AND STRUCTURAL-CHANGES OF BOVINE BETA-CASEIN UPON GLYCATION

The studies on casein structure modification contribute to better unde rstanding of the role of nonamino acid components in forming casein co mplexes and improving ways of protein functionality. The objective of the experiments was to explain the influence of bovine milk casein gly cation on some physico-chemical properties and structural changes. Fro m the the analysis of glycation rate curve the reaction of the first o rder range can be assumed during the first 24 h, turning to a mixed ty pe afterwards. The isoelectric point and molecular weight of beta-case in increased after glycation and the electrophoretic mobility was slig htly 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 sus ceptibility to the trypsin hydrolysis.