The structural and functional properties of hemp protein isolate‐epigallocatechin‐3‐gallate biopolymer covalent complex during heating.

BACKGROUND: It is well known that hemp proteins have the disadvantages of poor solubility and poor emulsification. To improve these shortcomings, an alkali covalent cross‐linking method was used to prepare hemp protein isolate‐epigallocatechin‐3‐gallate biopolymer (HPI‐EGCG) and the effects of different heat treatment conditions on the structure and emulsifying properties of the HPI‐EGCG covalent complex were studied. RESULTS: The secondary and tertiary structures, solubility, and emulsification ability of the HPI‐EGCG complexes were evaluated using particle size, zeta potential, circular dichroism (CD), and fluorescence spectroscopy indices. The results showed that the absolute value of zeta potential of HPI‐EGCG covalent complex was the largest, 18.6 mV, and the maximum binding amount of HPI to EGCG was 29.18 μmol g−1. Under heat treatment at 25–35 °C, the α‐helix content was reduced from 1.87% to 0%, and the β‐helix content was reduced from 82.79% to 0% after the covalent binding of HPI and EGCG. The solubility and emulsification properties of the HPI‐EGCG covalent complexes were improved significantly, and the emulsification activity index (EAI) and emulsion stability index (ESI) were increased by 2.77‐fold and 1.21‐fold, respectively. CONCLUSION: A new HPI‐EGCG covalent complex was developed in this study to provide a theoretical basis for the application of HPI‐EGCG in food industry. © 2023 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]