Enhancement of hydrogen bonds between proteins and polyphenols through magnetic field treatment: Structure, interfacial properties, and emulsifying properties.

ABSTRACT

In food systems, proteins and polyphenols typically coexist in a non-covalent manner. However, the inherent rigid structure of proteins may hinder the binding sites of polyphenols, thereby limiting the strength of their interaction. In the study, magnetic field (MF) treatment was used to enhance non-covalent interactions between coconut globulin (CG) and tannic acid (TA) to improve protein flexibility, enhancing their functional properties without causing oxidation of polyphenols. Based on protein structure results, the interaction between CG and TA caused protein structure to unfold, exposing hydrophobic groups. Treatment with a MF, particularly at 3 mT, further promoted protein unfolding, as evidenced by a decrease in α-helix structure and an increase in coil random. These structural transformations led to the exposure of the internal binding site bound to TA and strengthening the CG-TA interaction (polyphenol binding degree increased from 62.3 to 68.2%). The characterization of molecular forces indicated that MF treatment strengthened hydrogen bonding-dominated non-covalent interactions between CG and TA, leading to improved molecular flexibility of the protein. Specifically, at a MF treatment at 3 mT, CG-TA colloidal particles with small size and high surface hydrophobicity exhibited optimal interfacial activity and wettability (as evidenced by a three-phase contact angle of 89.0°). Consequently, CG-TA-stabilized high internal phase Pickering emulsions (HIPPEs) with uniform droplets and dense gel networks at 3 mT. Furthermore, the utilization of HIPPEs in 3D printing resulted in consistent geometric shapes, uniform surface textures, and distinct printed layers, demonstrating superior printing stability. As a result, MF treatment at 3 mT was identified as the most favorable. This research provides novel insights into how proteins and polyphenols interact, thereby enabling natural proteins to be utilized in a variety of food applications.