Amino acid composition, mineral profile, free radical scavenging ability, and carbohydrase inhibitory properties of Moringa oleifera seed globulin, hydrolysates, and membrane fractions.

The nutritional-amino acid profile and mineral element of Moringa oleifera seed globulin (GLO) and its hydrolysates as well as the in vitro bioactive properties-antioxidant, alpha-amylase, and alpha-glucosidase inhibition of the GLO, hydrolysates, and membrane fractions were reported. The results showed that M. oleifera contained significant amounts of essential amino acids (EAA), which are more than the minimum required by the Food and Agricultural Organization for children, except for tryptophan, which was the limiting amino acid. However, hydrolysis mostly led to a reduction in the contents of the EAA. While the process of hydrolysis and the subsequent membrane fractionation produced peptides with improved activities in 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulphonic acid radical scavenging ability and oxygen radical absorbance capacity, this process produced no activities in superoxide radical scavenging ability, α-amylase, and α-glucosidase inhibitory potentials of some of the hydrolysates and peptides fractions. In summary, M. oleifera seed peptide fraction (<3 kDa) from the alcalase-derived hydrolysate contains potent antioxidants but relatively low in vitro antidiabetic properties. PRACTICAL APPLICATIONS: Several studies have established the ability of proteins, including hydrolysate and peptide fractions to provide some bioactive properties such as antioxidant, antidiabetic, anti-inflammatory among others. However, because protein functionalities are influenced by several factors such as the source, type, processing method employed among others, research has continued to evaluate the bioactivities of proteins under different conditions. In this study, therefore, we reported the impact of processing methods (hydrolysis, enzyme type, and peptide size) on the nutritional, antioxidant, and in vitro antidiabetic properties of M. oleifera seed globulin, its hydrolysates, and membrane fractions. This information plays an important role in the further exploitation of M. oleifera seed proteins in the development of functional foods and nutraceuticals.