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 - DFBPANOX0125(Antioxidative peptide)

DFBP ID	DFBPANOX0125
Peptide sequence	VKEAMAPK
Type	Native peptide
Peptide/Function name	Antioxidative peptide

Function-activity relationship

Main bioactivity	Antioxidative activity
Otheir bioactivity	Antithrombotic activity ^[D1], Multifunctional activity ^[D2]

Calculated physicochemical properties

Three-letter amino acid

Val-Lys-Glu-Ala-Met-Ala-Pro-Lys

Single-letter amino acid

VKEAMAPK

Peptide length

Peptide mass

Experimental mass	Theoretical mass
873.5 Da	873.07 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

9.84 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.4000^c

Hydrophilic residue ratio

62.5%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protien
Precursor protein	β-Casein
Residue position	f(98-105)
Precursor protein(s) search	Source.1: DFBPPR7718 ---- Milk proteins ---- Beta-casein Source.2: DFBPPR8489 ---- Milk proteins ---- Beta-casein
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	Inhibition activity against Lox-catalyzed linoleate oxidation (initial rate kinetics) amounted to 16%.
Specific target protein(s)	N.D

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	No prediction can be made about the peptide bitterness. ^prediction

SMILES

N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CCSC)C(=O)N[C@@]([H])(C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCCN)C(=O)O

Preparation method

Mode of preparation	Fermentation and Enzymatic hydrolysis
Enzyme(s)/starter culture	(1) Peptide obtained by hydrolysis of bovine β-casein (Eurial, Rennes, France) by use of trypsin according to Rival et al. (2) Fermented by Lb. rhamnosus + digestion with pepsin and COROLASE PP ^[2].

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

N.D

Database cross-references

DFBP

[D1]	DFBPANTH0153
[D2]	DFBPMUFU0657

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Rival SG, Fornaroli S, Boeriu CG, Wichers HJ. Caseins and casein hydrolysates. 1. Lipoxygenase inhibitory properties. J Agric Food Chem. 2001 Jan;49(1):287-94. PMID: 11170590 DOI: 10.1021/jf000392t
Other literature(s)	[1] Pihlanto A. Antioxidative peptides derived from milk proteins[J]. International Dairy Journal, 2006, 16(11):1306-1314. [2] Korhonen H, Pihlanto A. Technological options for the production of health-promoting proteins and peptides derived from milk and colostrum[J]. Curr Pharm Des, 2007, 13(8):-. [3] Rival S G , Boeriu C G , Wichers H J . Caseins and casein hydrolysates. 2. Antioxidative properties and relevance to lipoxygenase inhibition[J]. J Agric Food Chem, 2001, 49(1):295-302.
PubDate	2001