Chaperone-like activity of β-casein and thermal stability of alcohol dehydrogenase

Correlation between structural peculiarities of beta-casein and its chaperon-like activity was investigated using the recombinant forms of the protein containing the cysteine residues in the polypeptide chain. Aggregation of native and modified forms of β-casein was studied, as well as their chaperon-like activity towards alcohol dehydrogenase thermal aggregation. It has been shown that dimeric and oligomeric forms of β-casein, which are formed due to intermolecular disulfide bonds, significantly differ in their physicochemical and chaperon-like properties from monomeric forms. The thermal stability of alcohol dehydrogenase has been found to depend on the β-casein concentration.