Abstract
Hyaluronic acid (HA) used as a food ingredient is gaining acceptance and popularity. However, the studies available for the effect of HA concentrations on the properties of β-lactoglobulin (β-LG) were limited. In this study, we investigated that the molecular characterization and functional properties of the complex formed by the non-covalent binding of β-LG and HA, as well as the ultrasound-assisted treatment at acidic pH. The optimal pH and ratio of β-LG/HA were set as 7 and 4:1, respectively. The fluorescence spectroscopy, circular dichroism spectroscopy, and molecular docking results revealed that the addition of HA and ultrasound induced a decrease in random coil and α-helix and an increase in β-sheet contents in β-LG. By the complexation with HA, the thermal stability, freezing stability, and antioxidant properties of β-LG were all improved under ultrasound treatment. The results of the present study can be useful for the modulation of HA based biopolymer complexes and the exploitation as encapsulating or structuring agents in food industry.
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