Pea proteins have gained significant interest in recent years. The objective of this study was to enhance pea protein functional properties through enzymatic and/or conjugation modifications and understand the physicochemical… Click to show full abstract
Pea proteins have gained significant interest in recent years. The objective of this study was to enhance pea protein functional properties through enzymatic and/or conjugation modifications and understand the physicochemical properties of the modified proteins. Molecular changes of the proteins were characterized, and protein functionality, in vitro digestibility, and sensory properties were analyzed. The proteins crosslinked with transglutaminase showed significantly improved water holding capacity (5.2-5.6 g/g protein) compared with the control pea protein isolate (2.8 g/g). The pea proteins conjugated with guar gum showed exceptional emulsifying capacity (EC) and stability (ES) of up to 100% compared with the control protein (EC of 58% and ES of 48%). Some sequentially modified pea proteins, such as transglutaminase crosslinking followed by guar gum conjugation had multiple functional enhancement (water holding, oil holding, emulsifying, and gelation). The functionally enhanced pea proteins had comparable sensory scores as the control protein.
               
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