Consumers' preference to have a healthy eating pattern has led to an increasing demand for more nutrient-dense and healthier plant-based foods. Pulse proteins are exceptional quality ingredients with potential nutritional benefits, and might act as health-promoting agents for addressing the new-generation foods. However, the utilization of pulse protein in foods has been hampered by its relatively poor functionality and unpleasant flavor. Protein structure modification has been proved to be a useful means to improve the functionality and flavor profile of pulse protein. This paper begins with a brief introduction of hierarchical structure of pulse protein materials to better understand the structure characteristics. A comprehensive review is presented on the current techniques including chemical and enzymatic modifications and molecular breeding on pulse protein structure and functionality/flavor. The mechanism and the limitations and the toxicological concerns of these approaches are discussed. We conclude that understanding protein structure-functionality relationship is extremely valuable in tailoring proteins for specific functional outcomes and expanding the availability of pulse proteins. Furthermore, selective protein modification is a valuable in-depth toolkit for generating novel protein constructs with preferable functional attributes and flavor profiles. Innovative structure modification with special focus on the molecular basis for the exquisite protein designs is a pillar of pulse protein access to the desired functionality.
Keywords: Maillard reaction; chemical modification; enzymatic modification; flavor profiles; protein functionality; pulse protein; site-selective modification; structure-function.
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