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.

This study used polysaccharide degrading enzymes and protein precipitation to extract polyphenols from oats and to determine their bioactivity. Duplicate oat brans were treated with viscozyme (Vis), cellulase (Cel) or no enzyme (control, CTL) then, proteins were removed in one set (Vis1, Cel1, CTL1) and not in the other (Vis2, Cel2, CTL2). HPLC analyses showed that for cellulase treated brans, precipitation of proteins increased phenolic acids and avenanthramides by 14%. Meanwhile, a decreased of 67% and 20% respectively was found for viscozyme and control brans. The effect of protein precipitation on soluble polyphenols is therefore dependent of the carbohydrase, as proteins with different compositions will interact differently with other molecules. Radical scavenging data showed that Cel1 and Vis1 had higher quenching effects on ROO• radicals with activities of 22.1 ± 0.8 and 23.5 ± 1.2 μM Trolox Equivalents/g defatted brans. Meanwhile, CTL2 had the highest HO• radicals inhibition (49.4 ± 2.8%) compared to 10.8-32.3% for others. Samples that highly inhibited lipoxygenase (LOX), an enzyme involved in lipid oxidation were Cel1 (23.4 ± 2.3%) and CTL1 (18 ± 0.4%).

The aim of this work was to determine the physicochemical and biological activities of hydrolyzed proteins from sonicated oat brans. In addition to the control bran sample, two types of pre-treatment procedures—namely, ultrasonic bath and probe-type sonication—were performed to extract proteins, followed by hydrolysis with various proteases. Physicochemical analyses showed that Flavourzyme-hydrolysates had greater amounts of aromatic amino acids, Papain-hydrolysates low surface charges (−0.78 to −1.32 mV) compared to the others (−3.67 to −9.17 mV), and Alcalase-hydrolysates a higher surface hydrophobicity. The hydrolysates had good radical scavenging activities but, as the ultrasonic pre-treatment of the brans showed, in certain cases there was a reduction in activities of up to 22% for ROO^• and HO^• and 15% for O₂^•− radicals. In anti-diabetic tests, the maximum inhibition of α-amylase was 31.8%, while that of dipeptidyl peptidase-4 was 53.6%. In addition, the secretion of glucagon-like peptide-1 in NCI-H716 cells was enhanced by 11.5% in the presence of hydrolysates.