Production, health-promoting properties and characterization of bioactive peptides from cereal and legume grains.

The search for bioactive components for the development of functional foods and nutraceuticals has received tremendous attention. This is due to the increasing awareness of their therapeutic potentials, such as antioxidant, anti-inflammatory, antihypertensive, anti-cancer properties, etc. Food proteins, well known for their nutritional importance and their roles in growth and development, are also sources of peptide sequences with bioactive properties and physiological implications. Cereal and legume grains are important staples that are processed and consumed in various forms worldwide. However, they have received little attention compared to other foods. This review therefore is geared towards surveying the literature for an appraisal of research conducted on bioactive peptides in cereal and legume grains in order to identify what the knowledge gaps are. Studies on bioactive peptides from cereal and legume grains are still quite limited when compared to other food items and most of the research already carried out have been done without identifying the sequence of the bioactive peptides. However, the reports on the antioxidative, anticancer/inflammatory, antihypertensive, antidiabetic properties show there is much prospect of obtaining potent bioactive peptides from cereal and legume grains which could be utilized in the development of functional foods and nutraceuticals.

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.

In vitro antihypertensive and antioxidative properties of trypsin-derived Moringa oleifera seed globulin hydrolyzate and its membrane fractions.

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.

Amino acid composition and antioxidant properties of Moringa oleifera seed protein isolate and enzymatic hydrolysates.

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.