Amino acid profile, protein digestibility, thermal and functional properties of Conophor nut (Tetracarpidium conophorum) defatted flour, protein concentrate and isolates

Abstract

Functional properties, amino acid compositions, in vitro protein digestibility, electrophoretic and thermal characteristics of conophor defatted flour (CDF), conophor protein concentrate (CPC), isoelectric protein isolate (CII) and neutral protein isolate (CNI) were evaluated. The isolates (CII and CNI) showed significantly lower (P < 0.05) water and oil absorption capacities, emulsifying and gelling capacities, but higher emulsion stability and foaming capacity. In vitro protein digestibility, enthalpy and denaturation temperature varied between 52.28% and 73.4%, 1.62–4.04 J g)1 protein and 79.7–89.3 °C, respectively. The native proteins were comprised of subunits with molecular weights ranging between 15.3 and 129.3 kDa. The major amino acids in all the samples were aspartic acid, glutamic acid and arginine, whereas the percentages of essential amino acids in CDF, CPC, CII and CNI were 39.35%, 40.46%, 44.54% and 46.04%, respectively. Conophor protein products could be used as functional ingredients in food formulations and for enriching low quality protein diets.