Protein-protein interactions of a whey-pea protein co-precipitate

The aim of this study was to investigate the mechanisms behind protein-protein interactions in a co-precipitate of whey protein isolate (WPI) and pea protein isolate (PPI). A co-precipitate and blend, consisting of 80% WPI and 20% PPI, were compared. Covalent disulphide interactions were studied by blocking of free thiols with N-Ethylmaleimide (NEM), while electrostatic interactions were studied in systems with 0.5 m NaCl and hydrophobic interactions with 0.2% SDS. Protein solubility, stability and secondary, tertiary and quaternary protein structures were analysed. Co-precipitation did not introduce different protein-protein interactions than the direct blending of proteins. SDS affected solubility (P < 0.05), secondary and tertiary structure. However, the effects of NEM and NaCl were significant greater (P < 0.05) on the same parameters and thermal stability, especially when combined (P < 0.01). Thus, the protein-protein interactions in a whey-pea co-precipitate and protein blend consisted of disulphide bonds and electrostatic interactions.

Automated summary

The study compared a blend and co-precipitate of whey protein isolate and pea protein isolate, finding that protein-protein interactions in both consisted mainly of disulphide bonds and electrostatic interactions. The effects of NEM and NaCl on protein structure and stability were greater than those of SDS.