Fractionation methods affect the gelling properties of pea proteins in emulsion-filled gels

Plant proteins, after extraction from sources such as pea can be used functional ingredients in emulsions and gels. However, the protein fractionation route affects functionality. We investigated differences rheological properties of emulsion-filled gel (EFGs) structured by isolate obtained using either isoelectric precipitation (PPIp) or diafiltration (PPId), at varying pH oil content. PPIp PPId had a content 75.3 77.7 wt %, respectively. first studied oil-water interfacial rheology composition emulsions, these emulsion influence EFG properties. Both formed viscoelastic, soft-solid layer around droplets both PPIs were able to stabilize with monomodal droplet size between 1 10 μm. Additional was added achieve final dry matter 15 % gelling induced heating protein-enriched rheometer 95 °C. At 5, EFGs comparable firmness (i.e. similar G’) heterogeneous microstructure. 7, less firm homogeneous gels compared PPId. The difference related solubility aggregation, caused different methods. In EFGs, presence did not reinforce structure, which could explained weak interactions interface matrix. Our results show that routes affect PPI EFGs. These insights may contribute is tailored specific structural requirements for gel-based foods.