Antioxidant Properties of Tripeptides Revealed by a Comparison of Six Different Assays

Ohashi, Yumi; Onuma, Ryo; Naganuma, Takako; Ogawa, Tomoya; Naudé, Ryno J.; Nokihara, Kiyoshi; Muramoto, Koji

doi:10.3136/fstr.21.695

Cited by 24 publications

(12 citation statements)

References 37 publications

(63 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The activity of LWC was highest (5296.8 μMTE) and was 3800‐fold higher than the lowest activity of EHV (1.4 μMTE). Thus, as reported previously, the strength of antioxidant activity of tripeptides depended on the constituent amino acids . In addition, even if the constituent amino acids of peptides were the same, their activity depended on the amino acid sequence; for instance, LFC (1780.3 μMTE) compared with CLF (434.8 μMTE) and WDY (390.6 μMTE) compared with DYW (131.0 μMTE).…”

Section: Resultssupporting

confidence: 71%

“…The majority of HAT‐based assays apply a competitive reaction in which the antioxidant and substrates compete for thermally generated peroxyl radicals, including the oxygen radical absorbance capacity and total radical trapping antioxidant parameter assays. Because the antioxidant activity assays are based on different chemical reactions, a tested sample can exhibit different antioxidant activities depending on the assay used …”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Quantitative analysis of the relationship between structure and antioxidant activity of tripeptides

Uno¹,

Kodama²,

Yukawa³

et al. 2020

Journal of Peptide Science

View full text Add to dashboard Cite

Funding information Kewpie Corporation, JapanPeptides from enzymatic hydrolysates of food proteins exhibit significant antioxidant activity. Several studies have attempted to determine the factors contributing to the antioxidant activity of peptides; however, the physicochemical properties and factors essential for the antioxidant activity of peptides are still unclear. In this study, in order to clarify the factors important for peptide antioxidant activity based on the properties of component amino acids, 55 tripeptides were synthesized from 20 natural amino acids and their antioxidant activity was measured using the Trolox equivalent antioxidant capacity (TEAC) assay system. The tripeptides were divided into two data sets: a training set comprising 50 compounds and a validated set comprising five compounds. The structure-activity relationship of the training set was then analyzed using classical quantitative structure-activity relationship (QSAR) analysis. The study findings demonstrate that the presence of a cysteine residue at any position, an aromatic amino acid at the C-terminus, higher hydrophobicity of the N-terminal residue, and smaller HOMO-LUMO energy gap of the middle residue can significantly enhance the antioxidant activity. The activities of the five validated compounds were predicted using the constructed QSAR model, and a good correlation between measured and predicted activities was observed. The information obtained from the QSAR model could be useful for effective production of antioxidant peptides from food proteins such as egg white proteins.

show abstract

Section: Resultssupporting

confidence: 71%

Section: Introductionmentioning

confidence: 99%

Quantitative analysis of the relationship between structure and antioxidant activity of tripeptides

Uno¹,

Kodama²,

Yukawa³

et al. 2020

Journal of Peptide Science

View full text Add to dashboard Cite

show abstract

“…With decreasing pH, the equilibrium protonation of the carbonyl oxygen increases, increasing the electrophilicity of the carbonyl carbon [51]. The occurrence of the deactivating protonated amino group and radical stabilizing clusters on side chains accounted for the positional selectivity and rates of radical assault on peptides [52]. As the pH was raised, the DPPH • scavenging activity declined marginally at pH 6-10 and increased at pH 11-13.…”

Section: Metal Chelating Activitymentioning

confidence: 99%

Characterization of Antioxidant Peptides from Thai Traditional Semi-Dried Fermented Catfish

et al. 2021

View full text Add to dashboard Cite

Herein, the antioxidant peptides from a Thai traditional semi-dried fermented farmed hybrid catfish (Clarias macrocephalus × Clarias gariepinus) catfish, Pla Duk Ra, were characterized. After extraction and deproteinization, Pla Duk Ra crude peptide extract (CPE) was fractioned using 2 connected Hitrap Sephadex-G25 columns, yielding two significant fractions, F1 with higher browning intensity (A420) and F2. CPE, F1, and F2 had different amino acid profiles, contents, and sequences evaluated by LC-MS/MS, which could be responsible for their antioxidant properties. F2 contained the highest numbers of hydrophobic amino acid (HBA) (47.45%) and aromatic amino acid (27.31%), followed by F1, and CPE. The peptides with 8–24 amino acid residues were detected in CPE and its fractions. In CPE, F1, and F2, there were 69, 68, and 85 peptides with varied HBA content, respectively. ARHSYGMLYCSCPPND (50% HBA), ALRKMGRK (37.5% HBA), and ANWMIPLM (87.5% HBA) were the most prevalent peptides found in CPE, F1, and F2. Overall, F2 was the most effective at inhibiting free radicals (DPPH● and ABTS●+) and reactive oxygen species (hydroxyl radical, singlet oxygen, and hydrogen peroxide), followed by F1 and CPE. The metal chelation of F1 was, however, superior to that of F2 and CPE. For the stability test, the effects of pH, heating temperature, and in vitro digestion on the DPPH● scavenging activity of F2 were investigated. The activity was boosted by lowering the pH and raising the heating temperature. In the gastrointestinal tract model system, however, roughly 50% of DPPH● scavenging activity reduced after digesting.

show abstract

“…With decreasing pH, the equilibrium protonation of the carbonyl oxygen increases, increasing the electrophilicity of the carbonyl carbon (Sun et al ., 2020). The occurrence of the deactivating protonated amino group and radical stabilising clusters on side chains accounted for the positional selectivity and degrees of radical assault on peptides (Ohashi et al ., 2015). As the pH raised, the DPPH • scavenging activity increased at pH 5–7, decreased marginally at pH 7–10 and decreased dramatically at pH 10–14.…”

Section: Resultsmentioning

confidence: 99%

Antioxidant activity and stability of endogenous peptides from farmed hybrid catfish (Clarias macrocephalus × Clarias gariepinus) muscle

Chaijan

Rodsamai

Charoenlappanit

et al. 2021

Int J of Food Sci Tech

View full text Add to dashboard Cite

Summary The antioxidant activity and stability of endogenous peptides isolated from farmed hybrid catfish (Clarias macrocephalus × Clarias gariepinus) muscle (EPC) were characterised. EPC contained 69 peptides with 8–24 amino acid residues, varying hydrophobic amino acid (HBA) content and distinct sequences. Among the top five, peptides discovered in EPC were ARHSYGMLYCSCPPND, DTQAARKSDDDD, AEFPCGDRRC, AAVTEELFFAGL and LILQRRKFLRMKREKYGFIYKTHL. Histidine (16.33%) and tryptophan (15.66%) were the most common amino acids found in EPC. EPC demonstrated concentration‐dependent free radical (DPPH•/ABTS•+) and hydroxyl radical (OH•) scavenging activities, as well as metal chelating ability. The effect of pH, heating temperature and in vitro digestion on EPC's DPPH• scavenging activity was studied. Lowering the pH and increasing the heating temperature to 90 °C increased the DPPH• inhibitory activity. However, after in vitro digestion, around 44% of DPPH• inhibition was reduced. The findings confirmed that farm‐raised hybrid catfish muscle contained endogenous peptides with antioxidant properties.

show abstract

Antioxidant Properties of Tripeptides Revealed by a Comparison of Six Different Assays

Cited by 24 publications

References 37 publications

Quantitative analysis of the relationship between structure and antioxidant activity of tripeptides

Quantitative analysis of the relationship between structure and antioxidant activity of tripeptides

Characterization of Antioxidant Peptides from Thai Traditional Semi-Dried Fermented Catfish

Antioxidant activity and stability of endogenous peptides from farmed hybrid catfish (Clarias macrocephalus × Clarias gariepinus) muscle

Contact Info

Product

Resources

About