A Novel Insight into Screening for Antioxidant Peptides from Hazelnut Protein: Based on the Properties of Amino Acid Residues

Abstract

This study used the properties of amino acid residues to screen antioxidant peptides from hazelnut protein. It was confirmed that the type and position of amino acid residues, grand average of hydropathy, and molecular weight of a peptide could be comprehensively applied to obtain desirable antioxidants after analyzing the information of synthesized dipeptides and BIOPEP database. As a result, six peptides, FSEY, QIESW, SEGFEW, IDLGTTY, GEGFFEM, and NLNQCQRYM were identified from hazelnut protein hydrolysates with higher antioxidant capacity than reduced Glutathione (GSH) against linoleic acid oxidation. The peptides having Tyr residue at C-terminal were found to prohibit the oxidation of linoleic acid better than others. Among them, peptide FSEY inhibited the rancidity of hazelnut oil very well in an oil-in-water emulsion. Additionally, quantum chemical parameters proved Tyr-residue to act as the active site of FSEY are responsible for its antioxidation. This is the first presentation of a novel approach to excavating desired antioxidant peptides against lipid oxidation from hazelnut protein via the properties of amino acid residues.

Stability, Bioavailability, and Structure–Activity Relationship of Casein-Derived Peptide YPVEPF with a Sleep-Enhancing Effect

“…This indicated that YPVEPF and YPVEP might have the potential to improve neuron inflammation against oxidant stress. Many studies showed that the presence of a Tyr residue with electron/hydrogen-donating ability was the driving force for peptides to scavenge radicals. , Therefore, the calculation results further highlighted the fact that the Tyr residue should act as a bioactive site, and QM is a useful assay to explore the structure–activity relationship. As previously described, the YXXY pattern in peptides could be the vital potential of the BZD site affinity, as the distance between the centers of the two tyrosine aromatic rings is similar to that between the centers of the aromatic rings in nitrazepam .…”

Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion—Peanuts as Our Antioxidant Friend or Foe in Allergies

“…Hydrophobic amino acid residues, such as His, Trp, Phe, Pro, Gly, Lys, Ile and Val, are attributed to strong radical scavenging activity in oxidative reactions, especially for enzyme-catalysed reactions, due to the imidazole ring from histidine as a vital proton donor [ 134 ]. In addition, the indole and pyrrolidine rings in Trp and Pro and Tyr, Cys and Met can also serve as hydrogen donors through their hydroxyl and thiol groups, thus acting as scavengers of hydroxyl and other free radicals [ 134 , 135 ]. Peptides obtained by simulated gastrointestinal digestion of hemp seeds, WVYY and PSLPA, showed the best antioxidant and antihypertensive properties, pointing to the presence of three aromatic amino acids, Trp, Tyr and Pro, in acquiring the pronounced antioxidative peptide properties [ 136 ].…”

Evaluation of Plant Protein Hydrolysates as Natural Antioxidants in Fish Oil-In-Water Emulsions

“…OSM–H considerably increases the AV after 7 days of storage but without surpassing NC. Shi et al [ 67 ] mention that Tyr, Trp, Met and Cys amino acids confer excellent antioxidant capacities to hazelnut protein peptides, acting as important hydrogen donors for free radicals. Among these amino acid residues, they found that Tyr-containing peptides exert a significant antioxidant activity.…”