Non-thermal plasma modulation of the interaction between whey protein isolate and ginsenoside Rg1 to improve the rheological and oxidative properties of emulsion.

Molecular interaction forces regulate the interfacial properties of oil-in-water emulsion and play a key role in the rheology and stability of the emulsion in the food industry. In this study, the effects of non-thermal plasma (NTP) treatment on the structural and functional properties of whey protein isolate (WPI) and its binding interaction with ginsenoside Rg1 (GR1) were investigated. The results based on surface hydrophobicity, infrared spectroscopy and fluorescence spectroscopy test showed that the NTP treatment induced the unfolding of the structure of WPI and promoted the binding affinity between WPI and GR1. By comparing with untreated WPI (an α-helix content of 19.63 % and a β-sheet content of 31.66 %), there was a greater decrease in α-helix content and an increase in β-sheet content of WPI in N20-WPI (α-helix = 9.63 %, β-sheet = 39.63 %) and N20-WPI-GR1 (α-helix = 4.98 %, β-sheet = 48.66 %) groups. Importantly, the NTP treatment increased the interfacial adsorption and antioxidant capacity of the WPI-GR1 complexes, which contributed to the improvement of the rheological properties and oxidation stability of the emulsion. As a result, the NTP treatment could markedly improve the rheological and antioxidative properties of the WPI-GR1 complexes and the NTP-treated WPI-GR1 emulsions was more stable than that untreated. The present research indicated that NTP-treated formation of protein-saponin complexes could enhance the functional properties of the proteins, thus expanding their application as functional ingradients in nutritionally fortified food.