ABSTRACT
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.
Subject(s)
Globulins , Moringa oleifera , Humans , alpha-Amylases/metabolism , alpha-Glucosidases/metabolism , Amino Acids/metabolism , Antioxidants/chemistry , Hypoglycemic Agents/pharmacology , Hypoglycemic Agents/metabolism , Minerals , Peptides/chemistry , Protein Hydrolysates/chemistry , Seeds/metabolism , Superoxides/metabolismABSTRACT
Moringa oleifera seed globulin was hydrolyzed with trypsin and fractionated to produce <1, 1-3, and 3-5 kDa peptide sizes. These were evaluated for antioxidant properties: DPPH, hydroxyl radical scavenging assays, FRAP, and metal chelation tests; and in vitro antihypertensive properties: ACE and renin inhibition. Membrane fractionation led to improved antioxidative properties of 29.13% (<1 kDa), 180% (<1 kDa), and 30.58% (1-3 kDa) for DPPH, FRAP, and metal iron chelation, respectively. There was however 48.77% reduction (1-3 kDa) in hydroxyl radical scavenging activity. There was also improvement in ACE inhibitory potentials of the peptides with the 1-3 kDa peptide showing significantly highest ACE inhibition (72.48%)but very low (17.64%, 1-3 kDa) inhibition against the renin. It was concluded that hydrolysis of M oleifera seed globulin with trypsin produced peptides and peptide fractions with potential antioxidant and antihypertensive properties.
ABSTRACT
The aim of this work was to compare the antioxidant and angiotensin converting enzyme (ACE) inhibitory properties of Moringa oleifera seed protein isolate (ISO) and its enzymatic protein hydrolysates. ISO was subjected to enzymatic (alcalase, pepsin and trypsin) hydrolysis to obtain alcalase isolate, pepsin isolate and trypsin isolate hydrolysates (AIH, PIH, TIH). Amino acid composition was similar for the samples except that TIH had lower Sulphur-containing amino acids while PIH was lower in tryptophan. All the samples were tested for antioxidant properties through free radical scavenging abilities such as 2,2 diphenyl-1-picrylhydrazyl (DPPH) and hydroxyl radical scavenging assays as well as ferric reducing antioxidant power (FRAP) and metal ion chelation assays. The maximum percentage inhibition obtained for the samples from the different assays are: DPPH, 36% (PIH); FRAP, 0.04% (PIH); hydroxyl radical scavenging activity, 42.98% (ISO); and inhibition of metal ion chelation, 29.46% (AIH). AIH (79.3%) had the highest ACE-inhibitory activity followed by TIH (75.1%) while PIH (43.0%) had the least. Generally, the hydrolysis process produced hydrolysates with improved antioxidant and ACE-inhibitory properties when compared to the isolate. We conclude that enzymatic hydrolysis with alcalase, pepsin and trypsin may be used to produce M. oleifera seed protein hydrolysates with potential to be used as ingredients for the formulation of functional foods and nutraceuticals.
ABSTRACT
Pigeon pea was treated by blanching and used to supplement acha flour for the development of functional cracker biscuits. The flour ratios for acha and pigeon pea were 100:0 (ACC), 80:20 (APC1), and 70:30 (APC2), respectively. The developed cracker biscuits were evaluated for chemical acid compositions, antioxidant, as well as antidiabetic properties. Protein contents of the formulated crackers increased with increase in supplementation with pigeon pea flour. The antinutrient content of the formulated snack was low hence may not adversely affect nutrient bioavailability. Glutamic and aspartic acids were the predominant amino acids while methionine and lysine significantly increased as a result of supplementation with pigeon pea flour. The biscuit exhibited good antioxidant properties indicated by its strong ability to scavenge hydroxyl, superoxide, DPPH radicals, and reduced Fe3+ to Fe2+. The formulated snack especially APC2 possessed low glycemic index (47.95%) and significantly inhibited the key digestive enzymes (α-amylase and α-glucosidase). All parameters evaluated indicated that APC2 could serve as a functional snack in the management of hyperglycemia (diabetes) and prevention of associated degenerative diseases.
