Résumé
In this study, a 4% (w/w) dispersion of a commercial patatin‐rich potato protein isolate (Po‐PI) was pressurised at 400 MPa up to 48 h at 20 °C. Protein aggregation induced by high‐pressure processing (HHP) was followed by dynamic light scattering, intrinsic fluorescence ( in‐situ or ex‐situ ) or SAXS analysis. Surface properties (surface hydrophobicity and interfacial properties) of the HHP‐induced aggregates were also investigated. A gradual dimer dissociation/protein unfolding was observed under pressure. Po‐PI exhibited a slow relaxation time under pressure. Long‐time HHP (>4 h) induced significant modification of the Po‐PI protein structure with partial non‐reversible unfolding. After 48 h of pressurisation at 400 MPa, large aggregates (160 nm) were obtained and a monomodal distribution in intensity and in number frequency was observed indicating a controlled aggregation. Up to 24 h of pressurisation at 400 MPa, intermediate states were obtained after high‐pressure release. SDS‐PAGE profiles showed that HHP‐induced aggregation of Po‐PI was driven by non‐covalent interactions. All high‐pressure processed dispersions displayed a higher surface hydrophobicity as compared to non‐treated Po‐PI. Po‐PI dispersion treated for 8 h at 400 MPa presented the lowest adsorption rate, the highest final surface tension and formed the most rigid interfacial film. Po‐PI showed resistance to moderate pressure levels (400 MPa) and long pressure application times were required to induce significant protein denaturation/aggregation (≥24 h) and to optimally modify its interfacial properties (8 h).