A comparison of β-casein complexes and micelles as vehicles for trans-/cis-resveratrol.

Bovine β-casein is an amphiphilic protein that exists as a monomer and self-organizes into micelles in aqueous solution. The protein has been used as natural vehicles for bioactives. Trans-resveratrol has received significant attention due to its vast health benefits and conversion to cis-isomer during processing and storage. However, cis-isomer has not yet gained as much attention as that of trans-isomer. In this study, the interaction of β-casein with trans- and cis-resveratrol was characterized. Trans-resveratrol exhibited a higher affinity for β-casein than cis-isomer, and β-casein could bind two isomers simultaneously to form protein-diligand complexes. Both trans- and cis-isomers could be encapsulated into β-casein micelles with encapsulation efficiencies of ~69% and ~57%, respectively. The β-casein micelles could delay photo-isomerization of trans-isomer to cis-isomer, while β-casein-ligand complex showed a better protective effect for both isomers during storage than β-casein micelles. These results might be useful for the development of protein-based carriers for the polyphenols.