Β-lactoglobulin and resveratrol nanocomplex formation is driven by solvation water release. (August 2022)

• Record Type: Journal Article
• Authors: do Vale, Rafaela Teixeira Rodrigues; de Paula, Hauster Maximiler Campos; Coelho, Yara Luiza; Rezende, Jaqueline De Paula; Vidigal, Márcia Cristina Teixeira Ribeiro; Da Silva, Luis Henrique Mendes; Pires, Ana Clarissa Dos Santos
• Is Part Of: Food research international. Volume 158(2022)
• Publication Date: 2022-08
• Subjects: Protein -- Polyphenol -- Intermolecular interaction -- Nanocarrier; Food -- Analysis -- Periodicals; Food industry and trade -- Periodicals; Food industry and trade -- Canada -- Periodicals; Food Technology -- Periodicals; Food -- Periodicals; Food-Processing Industry -- Periodicals; Aliments -- Industrie et commerce -- Périodiques; Aliments -- Industrie et commerce -- Canada -- Périodiques; Aliments -- Recherche -- Périodiques; Food industry and trade; Canada; Periodicals; Electronic journals; 664.005
• DOI: 10.1016/j.foodres.2022.111567
• Languages: English
• ISSNs: 0963-9969

Abstract

Graphical abstract: Highlights: Thermodynamically stable complexes are formed through activated complexes. The water molecules of the desolvation layer influence the association. The interaction causes a conformational change at the beta-lactoglobulin site. At the low temperature (285.15 K) the hydrophobic interaction prevails. At high temperatures (301.15 K), hydrophilic interactions are dominant. Abstract: Despite some thermodynamics studies about β-lactoglobulin (βLG) and resveratrol (RES) interactions, there is a gap regarding kinetics data about βLG-RES complex formation. Here, we determined the kinetic and thermodynamic parameters of βLG-RES interactions by using surface plasmon resonance (SPR). The kinetic association parameters were dependent on the 3D water structure present on the solvation shell of both interacting molecules. At lower temperature (285.15 K), all activation energies were positive ( E a c t a ‡ = 82.86 kJ.mol −1, T Δ S a ‡ = 32.26 kJ.mol −1, and Δ C p a ‡ = 4.15 kJ.mol −1 K −1 ) due to the higher water structuration on the RES and βLG solvation shell. All these energetic barriers become mainly from the energetic cost for the desolvation process of RES and βLG. At higher temperature (301.15 K), the solvation water structure decreases and all the above activation energies become negative ( E a c t a ‡ = - 121.58 kJ.mol −1, T Δ S a ‡ = - 173.59 kJ.mol −1, and Δ C p a ‡ = - 29.92 kJ.mol −1 K −1 ) because the direct interaction between desolvated RES and βLG molecules released more energy than it is absorbed by desolvation process. However, kinetic dissociation parameters were not dependent on the hydrogen bond density of the water solvation shell as showed by the temperature independence of dissociation energetic parameters. This non-dependence of the dissociation process from the desolvation step probably is because the water molecules interacting with the βLG-RES complex is not concentrated around/inside the protein site of interaction. The association of free molecules was 1.5 times faster than the dissociation of the thermodynamically stable complex ( Δ G ( a ) ‡ ≅ 48.15 kJ.mol −1, Δ G ( d ) ‡ ≅ 73.10 kJ.mol −1 ). The lower free energy barrier observed for the association came from an isokinetic process where entropic and enthalpic parameters compensated for each other. The ΔG° values indicate that the thermodynamically stable complex predominates over free molecules. At low temperature (285.15 K), the hydrophobic interaction ( Δ H° = 73.06 kJ.mol −1 ; T Δ S° = 99.60 kJ.mol −1 ) drove the βLG-RES complex formation while at high temperature (301.15 K), hydrophilic interactions became dominant ( Δ H° = −142.50 kJ.mol −1 ; T Δ S° = −118.18 kJ.mol −1 ).