Plant protein-quercetin complexation in food product development

The increasing demand for sustainable food ingredients has stimulated research into plant protein modification strategies for product development. Interactions between edible plant proteins and quercetin, mediated by both covalent and non-covalent bonds, significantly influence protein functionality in food formulations. Emerging food processing technologies present promising approaches to enhance these interactions in food matrices; however, understanding their mechanisms remains crucial for industrial applications. This review examines food processing technologies related to plant protein-quercetin interactions, with a focus on molecular mechanisms and functional enhancements in food systems. It analyzes pH-dependent binding mechanisms, structure-function relationships, and processing strategies, including self-assembly, physical treatments, chemical modifications, and polysaccharide incorporation, while evaluating applications in functional food development. Plant protein-quercetin interactions exhibit pH-dependent mechanisms, which determine protein structural modifications and properties in the final products. The effectiveness of these interactions depends on the dietary protein sources due to their unique molecular architectures. Advanced technologies demonstrate complementary effects: physical treatments enhance binding site accessibility, while chemical modifications control conjugation specificity in food ingredients. Polysaccharide incorporation creates hierarchical structures that enhance stability in complex systems. These findings establish a framework for designing targeted modifications and provide insights for developing next-generation functional foods, emphasizing the importance of structure-function relationships in optimizing processing approaches.