Cereals like wheat, rice, corn, barley, rye, oat, and millet are staple foods in many regions around the world and contribute to more than half of human energy requirements. Scientific publications contain evidence showing that apart from energy, the regular consumption of whole grains is useful for the prevention of many chronic diseases associated with oxidative stress. Biological activities have mostly been attributed to the presence of glucans and polyphenols. In recent years however, food proteins have been investigated as sources of peptides that can exert biological functions, promote health and prevent oxidative stress. This review focuses on the role of hydrolyzed proteins and peptides with antioxidant properties in various models and their mechanisms which include hydrogen or electron transfer, metal chelating, and regulation of enzymes involved in the oxidation-reduction process.
Iron and calcium are two essential micronutrients that have strong effects on nutrition and human health because of their involvement in several biological and redox processes. Iron is responsible for electron and oxygen transport, cell respiration, and gene expression, whereas calcium is responsible for intracellular metabolism, muscle contraction, cardiac function, and cell proliferation. The bioavailability of these nutrients in the body is dependent on enhancers and inhibitors, some of which are found in consumed foods. Hydrolyzed proteins and peptides from food proteins can bind these essential minerals in the body and facilitate their absorption and bioavailability. The binding is also important because excess free iron will increase oxidative stress and the risks of developing chronic diseases. This paper provides an overview of the function of calcium and iron, and strategies to enhance their absorption with an emphasis on hydrolyzed proteins and peptides from foods. It also discusses the relationship between the structure of peptides and their potential to act as transition metal ligands.
The purpose of this study was to determine, for the first time, antioxidant activities of seven peptides (P1–P7) derived from hydrolysis of oat proteins in a cellular model. In the oxygen radical absorbance capacity (ORAC) assay, it was found that P2 had the highest radical scavenging activity (0.67 ± 0.02 µM Trolox equivalent (TE)/µM peptide) followed by P5, P3, P6, P4, P1, and P7 whose activities were between 0.14–0.61 µM TE/µM). In the hepatic HepG2 cells, none of the peptides was cytotoxic at 20–300 µM. In addition to having the highest ORAC value, P2 was also the most protective (29% increase in cell viability) against 2,2′-azobis(2-methylpropionamidine) dihydrochloride -induced oxidative stress. P1, P6, and P7 protected at a lesser extent, with an 8%–21% increase viability of cells. The protection of cells was attributed to several factors including reduced production of intracellular reactive oxygen species, increased cellular glutathione, and increased activities of three main endogenous antioxidant enzymes.
Oxidative stress and the dysregulation of metabolism can affect the enzyme functions and are associated with pathological conditions such as obesity, hypertension, cardiovascular diseases, and diabetes (Lay et al., 2014). The prevalence of these chronic conditions has been increasing worldwide, and there are ongoing research works to find active molecules in foods to reduce their risk factors. The causes of obesity include disruption to metabolic pathways, energy imbalance, and genetic predisposition (González-Muniesa et al., 2017). Strategies
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