Complexation of trans- and cis-resveratrol with bovine serum albumin, β-lactoglobulin or α-lactalbumin. (August 2018)

• Record Type: Journal Article
• Authors: Cheng, Hao; Fang, Zheng; Wusigale, ; Bakry, Amr M.; Chen, Yantao; Liang, Li
• Is Part Of: Food hydrocolloids. Volume 81(2018)
• Page Start: 242
• Page End: 252
• Publication Date: 2018-08
• Subjects: Resveratrol -- Ligand-binding protein -- Isomerization -- Interaction -- Antioxidant activity; Hydrocolloids -- Periodicals; Food additives -- Periodicals; Colloïdes -- Périodiques; Aliments -- Additifs -- Périodiques; Colloids; Food additives; Periodicals; Electronic journals; 664.06
• DOI: 10.1016/j.foodhyd.2018.02.037
• Languages: English
• ISSNs: 0268-005X

Abstract

Abstract: Clarification of the mechanism of protein-ligand interaction is important for the encapsulation of bioactive components. Trans -resveratrol is labile to convert to cis -isomer during fermentation and storage, but the cis -isomer interaction with proteins has not yet gained as much attention as that of trans -isomer. The influence of resveratrol's isomerization on interaction with ligand-binding proteins was investigated here. Cis -resveratrol exhibited higher affinity for bovine serum albumin than trans -isomer, but the isomerization to cis -isomer decreased the polyphenol affinity for α-lactalbumin and β-lactoglobulin. For each protein, trans - and cis -resveratrol shared the same optimal docking site but showed clear diversity in the second best site. Protein ternary complex could be formed when trans -/ cis -resveratrol were added in the sequence. Moreover, photostability of resveratrol and antioxidant activity of the polyphenol-protein mixtures were also discussed. The results gathered here should provide further insight into protein-polyphenol interactions and be useful for the development of protein-based carriers for the polyphenols. Graphical abstract: Image 1 Highlights: C is -resveratrol had higher affinity to BSA but less to α-LA or β-LG than trans -isomer. Trans - and cis -resveratrol shared the optimal site but not the secondary site. Protein ternary complex formed when trans -/ cis -resveratrol added in the sequence. The hydrophobicity of bound resveratrol ranked in the order BSA > β-LG > α-LA. Protein-resveratrol showed greater antioxidant activity than free polyphenol.