[Chaperone-like activity of beta-casein and thermal stability of alcohol dehydrogenase].

To elucidate the correlation of structural peculiarities of beta-casein and their chaperon-like activity the modified forms of the protein (with cysteinyl residues introduced in polypeptide chain) were investigated. The aggregation of native and recombinant beta-caseins was studied as well as their chaperon-like activity towards alcohol dehydrogenase thermal aggregation. It was shown that physico-chemical and chaperone-like properties ofdimeric and oligomeric forms ofbeta-casein (which formation is due to intermolecular disulfide bonds) differ significantly from monomeric forms. It was found that thermal stability of alcohol dehydrogenase depends on beta-casein concentration.