Nanocomplex formation between β-lactoglobulin or caseinomacropeptide and green tea polyphenols: Impact on protein gelation and polyphenols antiproliferative activity

The development of milk functional foods including health-promoting green tea polyphenols represents a challenge for the food industry since the formation of protein–polyphenol complexes may affect both protein technological properties and polyphenols biological activity. The present work aimed at the characterization of complexes formed between green tea polyphenols and either β-lactoglobulin (β-lg) or caseinomacropeptide (CMP), as well as to evaluate how this complexation may impact on protein gelation and polyphenol antiproliferative activity against tumor cell lines.Particle size and charge of protein–polyphenol complexes depend on protein nature and pH. At pH 6 they had the smallest size and were soluble. The presence of polyphenols accelerated the gelation of both β-lg and CMP, and mainly affected viscoelasticity of β-lg gels. Polyphenol complexation by proteins did not inhibit its anti-proliferative activity. Moreover, they exerted a better performance on some particular tumor cell lines.

► Whey proteins–polyphenols complexation was studied at different pHs.
► Protein–polyphenol complexes formation accelerates the gelation of whey proteins.
► Polyphenols within the complexes retain their antiproliferative activity.
► Synergistic effects were obtained on some particular tumor cell lines.