Maillard-driven chemistry to tune the functionality of pea protein: Structure characterization, site-specificity, and aromatic profile

Pea protein has trickled into the protein demand aisles, owing to its exceptional nutritional benefits and functional attributes. The Achilles' heel of pea protein is its inferior solubility and beany flavor. Structure-based design of food proteins with specific techno-functional characteristics exhibits high potency. Glycation via Maillard-driven chemistry is a valuable in-depth toolkit for fabricating protein-based conjugates with superior functions and flavor profile. Herein, we comprehensively review the potential of applying glycation via Maillard-driven chemistry to tailor protein architectures for amending protein functional attributes and flavor profile. We start by summarizing the principles and kinetics of Maillard-driven chemistry. We then highlight the structural characteristics and site-specificity of protein-based conjugates deciphered from various techniques. Moreover, specific highlights are focused on the impact of elements of interest on protein-based conjugates functions and flavors. In combination with our recent research findings, it would bring forth an enlightenment in probing the fundamental relationship between the structure and the functionality of pea protein. The preparation methods and native of saccharides play a vital role in pea protein modification. Although exciting progress has been made in protein chemistry, the site-specificity of glycating pea protein with various saccharides still remains previously unexplored especially when polysaccharides are employed. This is because of the difficulty in mass analysis. A relevant study is urgently essential to probe specific glycation sites of pea protein, which would be helpful to precisely design the molecular function by incorporating the functional groups at the targeted sites.