The mechanism of the heat-induced gelation of ovalbumin (OVA) under acidic conditions and the effect of amphiphilic peptide additives on gelation were investigated using dynamic light scattering (DLS) and small-angle neutron scattering (SANS). The molecular morphology and structure probed by DLS and SANS suggest that the heat-induced gelation of OVA solution forms a phase-separated structure. Heating of the solution of OVA and the peptide resulted in effective distribution of the peptide in the matrix of the heat-induced OVA gels and endowed the gel with increased strength.
- Takashi Hiroi
- Kazu Hirosawa
- Mitsuhiro Shibayama