Sustainable conversion of coconut meal globulin into a high‐performance emulsifier via non‐covalent modification with gum arabic

BACKGROUND: Coconut meal globulin (CMG) is a sustainable protein derived from coconut meal. However, the inherent poor solubility and stability of CMG impose limitations on its application in the food industry. In this study, the functional properties of CMG were enhanced through non-covalent modification with gum arabic (GA). RESULTS: The CMG-GA complex was successfully prepared at a pH and CMG/GA mass ratio of 3.5 and 2:1, respectively. It was clarified that hydrophobic interactions and hydrogen bonds were the primary interaction forces between CMG and GA. Hydrogen bonds were observed between GA and the CMG residues Gln151, Gln153, Asp156, Arg300, and Arg301. The CMG-GA complex exhibited superior emulsifying capacity and stability at a concentration of 0.7%, showing performance comparable to that of sodium caseinate. The emulsions exhibited a 10.06% increase in adsorbed protein and an 89% decrease in creaming index, corresponding to a minimized droplet size and improved uniformity, as confirmed by confocal laser scanning microscopy. Meanwhile, the thermal and storage stability of the emulsion were significantly improved. Rheologically, the emulsion displayed shear-thinning behavior and weak gel-like properties, while the critical strain of emulsion increased from 3.08% (native CMG) to 13.03% (CMG-GA). CONCLUSION: GA markedly enhanced the functional properties of CMG via non-covalent modification. The CMG-GA complex displayed favorable emulsifying capacity and stability, comparable to those of the commercial emulsifier, sodium caseinate. Therefore, the CMG-GA complex shows potential as a novel plant protein-based emulsifier for application in the food industry, while promoting the high-value utilization of coconut meal. © 2026 Society of Chemical Industry.