Non-covalent interaction between pea protein isolate and catechin: effects on protein structure and functional properties

The aim of this study was to investigate the effects of non-covalent interaction between pea protein isolate (PPI) and different concentrations (0.05-0.25%, w/v) of catechin (CT) on the structural and functional characteristics of protein. CT introduction changed the PPI secondary and tertiary structures. Hydrophobic actions were the major interaction forces of PPI-CT complexes. Surface hydrophobicity of PPI decreased as many hydrophobic groups were exposed to a more hydrophilic environment. The polyphenol bound equivalents, emulsifying properties, foaming stability, and antioxidant activities of PPI were improved after non-covalently interacting with CT. Therefore, the addition of CT to PPI is an effective approach to improve its structural and functional properties. These results provide a reference for using PPI-polyphenol complexes to develop functional food ingredients.

Automated summary

The aim of this study was to investigate the effects of non-covalent interaction between pea protein isolate (PPI) and catechin (CT) on the structural and functional characteristics of protein. The results showed that CT introduction changed the PPI secondary and tertiary structures and improved its emulsifying properties, foaming stability, and antioxidant activities.