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

• Published in: Food & function Vol. 13; no. 23; pp. 1228 - 12218
• Main Authors: Zhang, Na, Zhang, Xuping, Zhang, Yan, Li, Yonglin, Gao, Yuan, Li, Qi, Yu, Xiuzhu
• Format: Journal Article
• Language: English
• Published: Cambridge Royal Society of Chemistry 28.11.2022
• Subjects: Catechin; Covalence; Foaming; Functional foods & nutraceuticals; Hydrophobicity; Peas; Protein structure; Proteins; Structure-function relationships
• ISSN: 2042-6496; 2042-650X; 2042-650X
• DOI: 10.1039/d2fo01549h

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. 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.