Pea protein hydrolysate (PPH) is successfully conjugated with gum arabic (GA) through Maillard-driven chemistry. The effect of cross-linking conjugation on the structure, solubility, volatile substances, emulsification, and antioxidative activity of… Click to show full abstract
Pea protein hydrolysate (PPH) is successfully conjugated with gum arabic (GA) through Maillard-driven chemistry. The effect of cross-linking conjugation on the structure, solubility, volatile substances, emulsification, and antioxidative activity of glyco-PPH is investigated, and found to improve all properties. The formation of glyco-PPH is confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), Fourier-transform infrared (FTIR), and scanning electron microscopy (SEM). Size exclusion chromatography-multi angle light scattering (SEC-MALS) unveils that the maximum molecular mass of glyco-PPH occurs after 1 day of conjugation and approximately 1.2 mole of gum arabic conjugates on one mole of PPH. Headspace solid-phase microextraction gas chromatography-mass spectrometry (HS-SPME-GC-MS) reveals the odor changes of glycoprotein before and after cross-linking. We have also prepared oil-in-water emulsions using glyco-PPH which have enhanced physical stability against pH changes and chemical stability against lipid oxidation. The mechanism proposed involves Maillard-driven synthesis of the cross-linked PPH-GA conjugates which increase the surface hydrophilicity and steric hindrance of glyco-PPH. These findings could provide a rational foundation for tailoring the physicochemical properties and functionalities of plant-based protein, which are attractive for food and functional materials applications.
               
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