Antioxidant, Physicochemical, and Cellular Secretion of Glucagon-Like Peptide-1 Properties of Oat Bran Protein Hydrolysates.

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.

Room Temperature Synthesis and Characterization of Novel Bi(III) Complex with 2-Amino-3- Carbomethoxy-4,5,6,7-Tetrahydrobenzo[B]Thiophene as Potential Antimicrobial Agent.

A novel bismuth(III) complex with 2-amino-3-carbomethoxy-4,5,6,7-tetrahydrobenzo[b]thiophene (ACTT) as a ligand have been synthesized. The novel complex was characterized on the basis of its IR, NMR, elemental analysis and MS spectral data. It was found that the ligand behaves as a monodentate chelating agent and bonds to the metal ion through the nitrogen atom of the amino group to form the [BiIII(ACTT)6]Cl3 complex. The new complex compound displayed significant antimicrobial activity (MIC = 8-32 µg/mL) against Bacillus subtilis, Staphylococcus aureus, Escherichia coli, Pseudomonas aeruginosa, Shigella flexneri, Candida albicans, Candida tropicalis and Cryptococcus neoformans.

Antioxidant properties and potential mechanisms of hydrolyzed proteins and peptides from cereals.

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.

Potential of Food Hydrolyzed Proteins and Peptides to Chelate Iron or Calcium and Enhance their Absorption.

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.