Peptide properties

1Top 2Function-activity relationship 3Calculated physicochemical properties 4Peptide source & Food-borne protein(s) search 5Biological/Functional activity & target protein 6Taste properties & Structure 7Preparation method 8Stability & Cytotoxicity 9Additional information 10Database cross-references 11Reference(s)

List of peptide properties

DFBP ID - DFBPANOX0304(Antioxidative peptide)

DFBP ID	DFBPANOX0304
Peptide sequence	VDYP
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

Val-Asp-Tyr-Pro

Single-letter amino acid

VDYP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
544 Da	492.52 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.13 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.5500^c

Hydrophilic residue ratio

50%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal, Fish, Marine
Organism/Source	Tuna
Precursor protein	Tuna cooking juice
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR1005 ---- Plant proteins ---- Cellulose synthase A catalytic subunit 7 [UDP-forming] Source.2: DFBPPR1006 ---- Plant proteins ---- Cellulose synthase A catalytic subunit 4 [UDP-forming] Source.3: DFBPPR1008 ---- Plant proteins ---- Cellulose synthase A catalytic subunit 9 [UDP-forming] Source.4: DFBPPR1171 ---- Plant proteins ---- Delta-1-pyrroline-5-carboxylate synthase 2 Source.5: DFBPPR1277 ---- Plant proteins ---- Probable cellulose synthase A catalytic subunit 8 [UDP-forming] Source.6: DFBPPR1369 ---- Plant proteins ---- Probable cellulose synthase A catalytic subunit 1 [UDP-forming] Source.7: DFBPPR1452 ---- Plant proteins ---- Probable cellulose synthase A catalytic subunit 2 [UDP-forming] Source.8: DFBPPR1455 ---- Plant proteins ---- Probable cellulose synthase A catalytic subunit 5 [UDP-forming] Source.9: DFBPPR1461 ---- Plant proteins ---- Probable cellulose synthase A catalytic subunit 3 [UDP-forming] Source.10: DFBPPR1462 ---- Plant proteins ---- Probable cellulose synthase A catalytic subunit 6 [UDP-forming] Source.11: DFBPPR2091 ---- Plant proteins ---- Cellulose synthase-like protein D3 Source.12: DFBPPR2436 ---- Plant proteins ---- NADH dehydrogenase [ubiquinone] iron-sulfur protein 3 Source.13: DFBPPR2549 ---- Plant proteins ---- Heat stress transcription factor C-2a Source.14: DFBPPR2691 ---- Plant proteins ---- Achilleol B synthase Source.15: DFBPPR2802 ---- Plant proteins ---- UDP-glucose 4-epimerase 3 Source.16: DFBPPR3076 ---- Plant proteins ---- GTP-binding nuclear protein Ran-1 Source.17: DFBPPR3539 ---- Plant proteins ---- GTP-binding nuclear protein Ran-2 Source.18: DFBPPR3892 ---- Plant proteins ---- DEAD-box ATP-dependent RNA helicase 26 Source.19: DFBPPR3982 ---- Plant proteins ---- DEAD-box ATP-dependent RNA helicase 25 Source.20: DFBPPR4028 ---- Plant proteins ---- DEAD-box ATP-dependent RNA helicase 31 Source.21: DFBPPR4460 ---- Plant proteins ---- Protein argonaute 3 Source.22: DFBPPR4939 ---- Plant proteins ---- Telomere-binding protein 1 Source.23: DFBPPR5034 ---- Plant proteins ---- 15-cis-phytoene desaturase, chloroplastic/chromoplastic Source.24: DFBPPR7419 ---- Plant proteins ---- Cytochrome b Source.25: DFBPPR8190 ---- Plant proteins ---- Acyl-coenzyme A oxidase, peroxisomal Source.26: DFBPPR16131 ---- Animal proteins ---- Pyruvate kinase PKLR Source.27: DFBPPR16259 ---- Animal proteins ---- Galactocerebrosidase Source.28: DFBPPR18988 ---- Animal proteins ---- Lysosomal Pro-X carboxypeptidase Source.29: DFBPPR19535 ---- Animal proteins ---- Probable 18S rRNA (guanine-N(7))-methyltransferase Source.30: DFBPPR19621 ---- Animal proteins ---- Aspartoacylase Source.31: DFBPPR21939 ---- Animal proteins ---- Inter-alpha-trypsin inhibitor heavy chain H5 Source.32: DFBPPR22396 ---- Animal proteins ---- Actin-related protein 10 Source.33: DFBPPR22571 ---- Animal proteins ---- Gypsy retrotransposon integrase-like protein 1 Source.34: DFBPPR9676 ---- Animal proteins ---- Pregnancy-associated glycoprotein 2 Source.35: DFBPPR10284 ---- Animal proteins ---- Non-specific lipid-transfer protein Source.36: DFBPPR10690 ---- Animal proteins ---- V(D)J recombination-activating protein 1 Source.37: DFBPPR10725 ---- Animal proteins ---- Cryptochrome-2 Source.38: DFBPPR11291 ---- Animal proteins ---- Activating signal cointegrator 1 complex subunit 3 Source.39: DFBPPR12525 ---- Animal proteins ---- Coagulation factor VII Source.40: DFBPPR12823 ---- Animal proteins ---- Pepsin F Source.41: DFBPPR14994 ---- Microorganism protein ---- Serine/threonine-protein kinase MEC1 Source.42: DFBPPR15032 ---- Microorganism protein ---- Pyruvate kinase Source.43: DFBPPR7966 ---- Plant protein ---- GTP-binding nuclear protein Ran/TC4
Link-research Inductive analysis	There are no literature reports on the discovery of this sequence in other food-source proteins.

Biological/Functional activity & target protein

Antioxidative activity	The peptide showed potent 1,1-diphenyl-2-picrylhydrzyl (DPPH) scavenging activity with a scavenging effect of 74% at concentration of 89 μg/mL.
Specific target protein(s)	N.D

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Bitter taste ^prediction

SMILES

N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N1[C@@]([H])(CCC1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Protease XXIII, from Aspergillus oryzae, was used to hydrolyze tuna cooking juice at 37 ℃ for up to 6 h.

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

Hydrolyzates from tuna cooking juice, and the fractions derived from them, can be incorporated into lipid-containing foods as chain-breaking antioxidants to minimize free radical-mediated lipid peroxidation. These hydrolyzates can also be used as alternatives to conventional drugs for treating human diseases associated with free radical-mediated tissue damage.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Jao, C.-L., Ko, W.-C. 1,1-Diphenyl-2-picrylhydrazyl (DPPH) radical scavenging by protein hydrolyzates from tuna cooking juice. Fisheries Science. 2002, 68, 430-5. DOI: 10.1046/j.1444-2906.2002.00442.x
Other literature(s)	N.D
PubDate	2002