Physico-chemical, functional, and structural properties of un-defatted, cold and hot defatted yellow lupin protein isolates.

This study investigates the structure, physico-chemical and functional properties of yellow lupin isolate protein (YLPI) obtained by different processes (conventional wet and purely aqueous fractionation) from un-defatted (YLPIU), and hot (YLPIHD) and cold (YLPICD) defatted flour. The defatting process modified the physical, structural and functional characteristics of lupin protein isolates. Indeed, a decrease of α-helix, free sulfhydryl groups amount and an increase of disulfide bond levels were observed for defatted samples, improving their emulsifying stability.