Abstract
The influence of pH value on the temperature-dependent polymerisation of β-casein was investigated by the method of light scattering, ultracentrifuge and optical rotatory dispersion. β-Casein used in the experiment was fractionated on DEAE-cellulose according to the method of Gehrke et al. The ultracentrifuge and light scattering data indicated that the temperature-dependent polymerization of β-casein is dependent extremely on pH value and occur easily as the pH value shift toward its isoelectric point, that is, the ability of, β-casein to polymerize is connected with the electrostatic forces between molecules. On the other hand the changes in the molecular structure of β-casein was observed from the results of optical rotatory dispersion, and the changes occured is influenced by pH value and temperature and may partially affect on the ability of polymerisation.
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