E-mail:gzliang@cqu.edu.cn    Tel: (86)2365102507

List of peptide properties
DFBP ID - DFBPANOX1079(Antioxidative peptide)
DFBP ID DFBPANOX1079
Peptide sequence FDTADLPSGKGYL
Type Native peptide
Peptide/Function name Antioxidative peptide
Function-activity relationship
Main bioactivity Antioxidative activity
Otheir bioactivity N.D
Calculated physicochemical properties
Three-letter amino acid Phe-Asp-Thr-Ala-Asp-Leu-Pro-Ser-Gly-Lys-Gly-Tyr-Leu
Single-letter amino acid FDTADLPSGKGYL
Peptide length 13
Peptide mass
Experimental mass Theoretical mass
1383.68 Da 1383.50 Da c
Net charge 0.00 c
Isoelectric point (pI) 3.92 c
IC50 N.D
pIC50 N.D
GRAVY -0.3000 c
Hydrophilic residue ratio 53.85% c
Peptide calculator
To calculate the physicochemical properties of bioactive peptide.
Peptide source & Food-borne protein(s) search
Classification Plant
Organism/Source Thai brown rice (Khao Dawk Mali 105)
Precursor protein Thai brown rice glutelin
Residue position N.D
Precursor protein(s) search
Link-research
There are no literature reports on the discovery of this sequence in other food-source proteins.
Biological/Functional activity & target protein
Antioxidative activity

The F4 fraction of glutelin hydrolysates showed ABTS•+ scavenging (14.03 ± 0.14 mM trolox) and copper chelating (33.65 ± 0.44 mg EDTA) activity (Table 1). The peptide FDTADLPSGKGYL was purified from F4 fraction, so is a potential antioxidant peptide (Inhibitory activity of synthetic peptide was not determined).

Table 1. Amino acid sequence, ABTS•+ scavenging activity and Cu2+ chelating activity of peptides from brown rice glutelin hydrolysed using bromelain and determined by LC-MS/MS.
Fraction no.SequenceABTS•+ scavenging activity
Cu2+ chelating activity
F4
GKGEGGGGLA
14.03 ± 0.1433.65 ± 0.44
EFFDVSNEQ
SPFWNINAHS
HIAGKSSIFRA
MPVDVIANAYR
VVYFDQTQAQA
TAGTGGGQFQPMR
KEFLLAGNNNRA
FDTADLPSGKGYL
AVYVYDVNNNANQ
Specific target protein(s) N.D
Taste properties & Structure
Bitterness
Literature report N.D
Bitter prediction tools Non-bitter taste prediction
SMILES N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CO)C(=O)NCC(=O)N[C@@]([H])(CCCCN)C(=O)NCC(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CC(C)C)C(=O)O
Preparation method
Mode of preparation

Enzymatic hydrolysis

Enzyme(s)/starter culture

Sample solutions were heated to 50 ℃ for 10 min to reach efficient enzymatic hydrolysis at the start of the reaction, and then submitted to enzymatic hydrolysis using bromelain at concentration of 202, 404, 606 and 808 CDU/g of brown rice protein. Hydrolysis was conducted at 50 ℃ for 0, 3, and 6 h and inactivated by heating at 75 ℃ for 15 min.

Stability & Cytotoxicity
Peptide stability
Literature report: N.D
EHP-Tool: Enzymatic Hydrolysis Prediction Tool (EHP-Tool)
Peptide cytotoxicity
Literature report: N.D
Prediction: ToxinPred
Additional information
Additional information

Results suggested that brown rice (Khao Dawk Mali 105) glutelin fractions hydrolysed with bromelain at concentration of 606 CDU/g of brown rice protein and its purified peptides could be used as nutraceutical ingredients in foods to boost antioxidant activity.

Database cross-references
BIOPEP-UWM [D1] -
APD [D2] -
BioPepDB [D3] -
MBPDB [D4] -
Reference(s)
Primary literature Selamassakul O, Laohakunjit N, Kerdchoechuen O, Yang L, Maier CS. Isolation and characterisation of antioxidative peptides from bromelain-hydrolysed brown rice protein by proteomic technique. Process Biochem. 2018 Jul;70:179-187.
PMID: 31031560
Other literature(s) N.D
PubDate 2018
Copyright © 2020. Record / license number: Chongqing ICP No. 2000214