Improvement of quercetin bioaccessibility by whey protein isolate/D-tagatose conjugates: Effect on the structural characterization through simultaneous rheological and FTIR techniques

Abstract

To improve the performance of whey protein isolates (WPI) as an encapsulation agent in the food industry, we investigated the formation mechanism of WPI and D-tagatose (DT) conjugates using simultaneous rheological and Fourier-Transform infrared spectroscopy (FTIR) techniques, and analysed its effects in encapsulating quercetin (Que). The degree of glycosylation of the conjugates increased to 18 % after heating treatment, whereas particle size and potential decreased to 64 nm and −39 mV, with WPI/D10 showing the lowest value. Simultaneous rheological and Fourier transform infrared analyses showed that the structure of the WPI/DT complexes changed, and the gel properties were much better than those of WPI. Several new peaks appeared at 2961, 1525, 1450, 1392, and 1236 cm-1, indicating that adding DT affected the structure of WPI. DT promoted secondary structural changes in WPI by increasing the degree of hydrocarbon chain, O-H group vibration, and C-O stretching. The WPI/DT conjugates increased the solubility of Que to 60.74 % and ABTS clearance to 73.98 %. The study may offer a theoretical foundation for using WPI/DT-encapsulated Que in food industry.