Study on the structural characteristics and emulsifying properties of chickpea protein isolate-citrus pectin conjugates prepared by Maillard reaction

Chickpea protein isolate (CPI) typically exhibits limited emulsifying properties under various food processing conditions, including pH variations, different salt concentrations, and elevated temperatures, which limits its applications in the food industry. In this study, CPI-citrus pectin (CP) conjugates were prepared through the Maillard reaction to investigate the influence of various CP concentrations on the structural and emulsifying properties of CPI. With the CPI/CP ratio of 1:2, the degree of graft reached 35.54 %, indicating the successful covalent binding between CPI and CP. FT-IR and intrinsic fluorescence spectroscopy analyses revealed alterations in the secondary and tertiary structures of CPI after glycosylation modification. The solubility of CPI increased from 81.39 % to 89.59 % after glycosylation. Moreover, freshly prepared CPI emulsions showed an increase in interfacial protein adsorption (70.33 % to 92.71 %), a reduction in particle size (5.33 μm to 1.49 μm), and a decrease in zeta-potential (–34.9 mV to –52.5 mV). Simultaneously, the long-term stability of the emulsions was assessed by employing a LUMiSizer stability analyzer. Furthermore, emulsions prepared with CPI:CP 1:2 exhibited excellent stability under various environmental stressors. In conclusion, the results of this study demonstrate that the glycosylation is a valuable approach to improve the emulsifying properties of CPI. • The chemical structures of CPI were changed after glycosylation modification. • Appropriate addition of pectin was beneficial for the glycosylation of CPI. • Glycosylation enhanced adsorption capacity of CPI at the oil-water interface. • Glycosylation degree of CPI was directly related to its emulsifying properties. • Glycosylation modification of CPI enhanced the stability of its emulsions.