Modification of pulse proteins for improved functionality and flavor profile: A comprehensive review

Abstract

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.

Binding of dual‐flavour compounds by soy protein isolate in aqueous model systems

“… where h is the Hill coefficient reflecting interactions between individual binding sites within their population; h is not necessarily an integer. The double‐reciprocal form of the Hill equation was used to determine the binding parameters (Zha et al ., 2021).…”

Effect of differences preheating temperatures on the functional and physical properties of soy protein concentrate

“…Interactions that can occur include the formation of cross-links between protein molecules, including hydrophobic and electrostatic interactions, hydrogen bonds, and disulfide-sulfhydryl exchanges. This interaction encourages the formation of aggregates with higher molecular weights, resulting in decreased solubility, and precipitation occurs [29,30].…”

Effect of industrial process conditions of fava bean (Vicia faba L.) concentrates on physico-chemical and functional properties

“…Since fava concentrate is a complex matrix of macro-and microconstituents, other non-protein associated reactions could influence the inter-dependence between the properties. Therefore, it might be essential to monitor protein as well as nonprotein interactions and reactions during modification and utilization of the ingredients (Carbonaro, Virgili, & Carnovale, 1996;Singhal, Karaca, Tyler, & Nickerson, 2016;Zha et al, 2021).…”

“…In addition, fava bean contain not only proteins but also various non-protein constituents, including starch, dietary fibers and fats, along with certain anti-nutritional factors (Multari et al, 2015;Sharan, Zanghelini, et al, 2021). Hence the reactions occurring during ingredient processing may be a result of proteins and/ or non-protein constituents (Kosińska, Karamać, Penkacik, Urbalewicz, & Amarowicz, 2011;Zha, Rao, & Chen, 2021). For now, there is no clear overview of all the possible reactions occurring during processing of fava ingredients that can evidently explain the changes in functional and physico-chemical properties.…”