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 - DFBPANOX0373(Antioxidative peptide)

DFBP ID	DFBPANOX0373
Peptide sequence	VPYPQ
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-Pro-Tyr-Pro-Gln

Single-letter amino acid

VPYPQ

Peptide length

Peptide mass

Experimental mass	Theoretical mass
603.3 Da	602.69 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.92 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.7600^c

Hydrophilic residue ratio

60%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein, Yoghurt
Precursor protein	β-Casein
Residue position	f(178-182)
Precursor protein(s) search	Source.1: DFBPPR7605 ---- Milk proteins ---- Beta-casein Source.2: DFBPPR7665 ---- Milk proteins ---- Beta-casein Source.3: DFBPPR7668 ---- Milk proteins ---- Beta-casein Source.4: DFBPPR7681 ---- Milk proteins ---- Beta-casein Source.5: DFBPPR7718 ---- Milk proteins ---- Beta-casein Source.6: DFBPPR8489 ---- Milk proteins ---- Beta-casein Source.7: DFBPPR13067 ---- Animal proteins ---- Beta-casein
Link-research Inductive analysis	Link 1: DFBPANOX0372----Human milk----β-Casein

Biological/Functional activity & target protein

Antioxidative activity	The peptide was a potential antioxidant peptide (data not shown).
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)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)O

Preparation method

Mode of preparation	Fermentation
Enzyme(s)/starter culture	Yoghurt samples were stripped from sugars and lactic acid and subsequently fractionated by ultra filtration using membranes with cut off sizes of 30, 10 and 3 kDa.

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

The presence of antioxidant peptides and free amino acids in fish oil-enriched yoghurt may have significantly contributed to its high oxidative stability. These results also demonstrate the applicability of these naturally occurring antioxidant peptides as an ingredient in foods in order to increase their oxidative stability.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Sabeena Farvin, K.H., Baron, C.P., Nielsen, N.S., Otte, J., Jacobsen, C. Antioxidant activity of yoghurt peptides: Part 2 – Characterisation of peptide fractions. Food Chem. 2010, 123, 1090-7. DOI: 10.1016/j.foodchem.2010.05.029
Other literature(s)	[1] Tsopmo A, Romanowski A, Banda L, et al. Novel anti-oxidative peptides from enzymatic digestion of human milk[J]. Food Chemistry, 2011, 126(3):1138-1143.
PubDate	2010