Effect of de-phenolization on protein-phenolic interactions of sunflower protein isolate.

Proteins and phenolic compounds are significant components of foods that can interact, and this interaction can impact the functional properties of proteins and the bioactivity of phenolic compounds. Sunflower meal, which has a high potential to be an important alternative protein source, contains phenolic compounds mostly bonded with proteins. In this study, the interaction between proteins and phenolic compounds which naturally exist in sunflower and prone to oxidation during alkaline treatment (for protein isolation) was investigated. There was a significant decrease up to 96.21% in the content of total phenolics by methanol washing. Chlorogenic acid, cryptochlorogenic acid and caffeic acid were detected in the phenolic extract obtained from sunflower protein isolate, and they exhibited different levels of reduction after methanol washing. For the total antioxidant capacity analysis, a decrease by 50% was observed after 4hwashing with methanol solution, and there was no significant decrease afterwards. In addition, the fluorescence intensity of sunflower protein was diminished with reduced washing time, which was mostly attributed to the protein-phenolic interaction. According to hydrodynamic parameters, the main force of the sunflower protein-phenolic complex formation was assumed to be hydrophobic attraction. The Stern-Volmer plot indicated that the main quenching mechanism was only static at all temperature conditions.