Alpha casein micelles show not only molecular chaperone-like aggregation inhibition properties but also protein refolding activity from the denatured state.

Casein micelles are a major component of milk proteins. It is well known that casein micelles show chaperone-like activity such as inhibition of protein aggregation and stabilization of proteins. In this study, it was revealed that casein micelles also possess a high refolding activity for denatured proteins.

Enzyme-mediated protein refolding.

We employed a urease-catalyzed reaction to gradually remove a high concentration of a chaotropic agent (urea) from a denatured protein solution and demonstrated that efficient protein refolding can be achieved by the urease-catalyzed reaction, without large-volume dilution.

Solubilization of n-alkylbenzenes into decanoyl-N-methylglucamide (Mega-10) solution.

Solubilization of benzene, toluene, ethylbenzene, n-propylbenzene, n-butylbenzene, n-pentylbenzene, and n-hexylbenzene into micelles of decanoyl-N-methylglucamide (Mega-10) was studied, where equilibrium concentrations of the above solubilizates were determined spectrophotometrically at 303.2 K. The concentration of the above solubilizates remained constant below the critical micelle concentration (cmc) and increased linearly with an increase in Mega-10 concentration above the cmc.