Structure, stability, rheology, and texture properties of ε-polylysine-whey protein complexes

Abstract

ε-Polylysine (ε-PL) is a natural preservative of antimicrobial peptides with broad spectrum and high antibacterial properties. The electrostatic complex delivery system formed by ε-PL and whey protein can be used to maintain the stability of ε-PL and solve the problem of limited application of protein-based food. This work aimed to study the interaction between ε-PL and whey protein by multiple characterization methods. The spectroscopy results showed static quenching type and new stretching of C=O for ε-PL-whey protein complexes. Microstructure studies showed that the combination of ε-PL and whey protein made the structure of the complexes become rough and dense. The interaction between ε-PL and whey protein could improve the stability of the complexes system during storage. Additionally, the interaction affected critical gel temperatures and gel texture properties of complexes with change of whey protein concentration, mass ratio of ε-PL to whey protein, pH value in alkaline solutions, and ion concentration. Overall, this study confirmed the interaction between ε-PL and whey protein, and it will provide a reference for the application of ε-PL in protein food matrix.