Acid–Heat-Induced Fabrication of Nisin-Loaded Egg White Protein Nanoparticles: Enhanced Structural and Antibacterial Stability

Abstract

As a natural cationic peptide, Nisin is capable of widely inhibiting the growth of Gram-positive bacteria. However, it also has drawbacks such as its antimicrobial activity being susceptible to environmental factors. Nano-encapsulation can improve the defects of nisin in food applications. In this study, nisin-loaded egg white protein nanoparticles (AH-NEn) were prepared in fixed ultrasound-mediated under pH 3.0 and 90 °C. Compared with the controls, AH-NEn exhibited smaller particle size (112.5 ± 2.85 nm), smaller PDI (0.25 ± 0.01), larger Zeta potential (24 ± 1.18 mV), and higher encapsulation efficiency (91.82%) and loading capacity (45.91%). The turbidity and Fourier transform infrared spectroscopy (FTIR) results indicated that there are other non-covalent bonding interactions between the molecules of AH-NEn besides the electrostatic forces, which accounts for the fact that it is structurally more stable than the controls. In addition, by the results of fluorescence intensity, differential scanning calorimetry (DSC), and X-ray diffraction (XRD), it was shown that thermal induction could improve the solubility, heat resistance, and encapsulation of nisin in the samples. In terms of antimicrobial function, acid–heat induction did not recede the antimicrobial activity of nisin encapsulated in egg white protein (EWP). Compared with free nisin, the loss rate of bactericidal activity of AH-NEn was reduced by 75.0% and 14.0% following treatment with trypsin or a thermal treatment at 90 °C for 30 min, respectively.