Influence of environmental pH on the interaction properties of WP‐EGCG non‐covalent nanocomplexes

• Published in: Journal of the science of food and agriculture 2023-08, Vol.103 (11), p.5364-5375
• Main Authors: Zhang, Shuangling, Dongye, Zixuan, Wang, Li, Li, Zhenru, Kang, Mengchen, Qian, Yaru, Cheng, Xiaofang, Ren, Yuhang, Chen, Chengwang
• Format: Article
• Language: English
• Subjects: antioxidant; Antioxidants; Antioxidants - chemistry; Binding; Catechin - chemistry; Conjugates; Covalence; Emulsification; Epigallocatechin gallate; Fluorescence; Fluorescence recovery after photobleaching; Fourier transforms; Hydrogen bonding; Hydrogen-Ion Concentration; Hydrophobicity; Infrared spectra; interactions; Molecular docking; Molecular Docking Simulation; pH effects; Proteins; Whey; Whey protein; Whey Proteins - chemistry; whey protein‐epigallocatechin gallate nanocomplexes
• ISSN: 0022-5142; 1097-0010
• DOI: 10.1002/jsfa.12611

BACKGROUND Whey protein‐epigallocatechin gallate (WP‐EGCG) covalent conjugates and non‐covalent nanocomplexes were prepared and compared using Fourier‐transform infrared spectra. The effect of pH (at 2.6, 6.2, 7.1, and 8.2) on the non‐covalent nanocomplexes' functional properties and the WP‐EGCG interactions were investigated by studying antioxidant activity, emulsification, fluorescence quenching, and molecular docking, respectively. RESULTS With the formation of non‐covalent and covalent complexes, the amide band decreased; the ‐OH peak disappeared; the antioxidant activity of WP‐EGCG non‐covalent complexes was 2.59‐ and 2.61‐times stronger than WP‐EGCG covalent conjugates for 1‐diphenyl‐2‐picryl‐hydrazyl (DPPH) and ferric reducing ability of plasma (FRAP), respectively (particle size: 137 versus 370 nm). The antioxidant activity (DPPH 27.48–44.32%, FRAP 0.47–0.63) was stronger at pH 6.2–7.1 than at pH 2.6 and pH 8.2 (DPPH 19.50% and 26.36%, FRAP 0.39 and 0.41). Emulsification was highest (emulsifying activity index 181 m2 g−1, emulsifying stability index 107%) at pH 7.1. The interaction between whey protein (WP) and EGCG was stronger under neutral and weakly acidic conditions: KSV (5.11–8.95 × 102 L mol−1) and Kq (5.11–8.95 × 1010 L mol s−1) at pH 6.2–7.1. Binding constants (pH 6.2 and pH 7.1) increased with increasing temperature. Molecular docking suggested that hydrophobic interactions played key roles at pH 6.2 and pH 7.1 (∆H > 0, ∆S > 0). Hydrogen bonding was the dominant force at pH 2.6 and pH 8.2 (∆H