Abstract
Whey protein (WP) is ubiquitously applied in food products, but its sensitivity to food processing conditions has limited its application. Herein, we chose propylene glycol alginate (PGA) to combine with WP to enhance its stability. The ideal ratio of WP/PGA for coacervation was 3:1, and the soluble complex and insoluble complex were formed at pH 5.2 (pHc) and pH 4.4 (pHφ1) at this ratio, respectively. The UV absorption spectra, fluorescence spectra, and XRD results revealed that the interaction between PGA and WP changed the tertiary conformation of WP. The FTIR and molecular docking results suggested electrostatic interactions, hydrogen bonding and hydrophobic interactions were all involved in the formation of WP-PGA complexes, and the thermal stability of WP was improved based on the DSC results. These findings supported PGA to keep dairy products stable and transparent at the isoelectric point and WP-PGA complexes could be applied in encapsulating bioactive substances.
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