Journal of Food Bioactives, ISSN 2637-8752 print, 2637-8779 online
Journal website www.isnff-jfb.com

Original Research

Volume 22, June 2023, pages 36-42

Influence of self-assembly on the reactive sulfhydryl and antioxidant activity of aggregation-prone ovalbumin-derived peptides

Figures

Figure 1.
Figure 1. (a) Thioflavin T fluorescence data, and (b) flow sweep experiment of viscosity as a function of shear rate response of the ovalbumin-derived peptides and glutathione (GSH) at 400 μM after 24 h. Different lowercase letters represent significant differences at the p < 0.05 level.
Figure 2.
Figure 2. Free sulfhydryl group content of self-assembling ovalbumin peptides and reduced glutathione at 400 μM. Different lowercase letters represent significant differences at the p < 0.05 level.
Figure 3.
Figure 3. Particle characteristics of self-assembling ovalbumin peptides and reduced glutathione at 400 μM. (a) Average particle size (nm) and (b) polydispersity index of the peptide fibrils. Different lowercase letters represent significant differences at the p < 0.05 level.
Figure 4.
Figure 4. Antioxidant assays of the self-assembling peptides. (a) Ferric Reducing Antioxidant Power (FRAP) (b) DPPH radical scavenging activity and (c) ABTS radical scavenging activity. Different lowercase letters represent significant differences at the p < 0.05 level.