Abstract

This study reported that fibrillar bridges (whey protein isolate nanofibrils, WPNs) were used to associate the casein (CA) nanoparticles through the pH-driven method to obtain the self-assembled WPN-CA complexes. Then, a novel technology involving cold plasma (CP) was innovatively proposed to enhance the protective properties of complexes. The confirmation of structural transitions and interactions resulting from the adjustment of WPN-to-CA ratios (WtCs) led to the identification of the complexes named WPCA (WtC1.0:1). Next, the results showed a rapid conjugation between WPCA and fucoidan (FD) with a degree of grafting of 16.03 % after 10 min CP treatment. The coupling of WPCA with FD to form conjugates was confirmed by SDS-PAGE analysis, indicating covalent bonds' formation. FTIR spectroscopy revealed an augmentation in the intensity of the OH stretching vibration of the WPCA-FD conjugate, concomitant with a decrease in β-turns and an elevation in β-sheets content. Furthermore, the application of glycosylation treatment to WPCA-FD resulted in a noteworthy enhancement of both the thermal stability and antioxidant activity characteristics of WPCA. Our findings move a step forward, as CP-assisted Maillard reaction has shown potential as an efficient and energy-saving method to enhance the functional properties of milk-derived proteins in the food industry.

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