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 - DFBPACEI1130(ACE-inhibitory peptide)

DFBP ID	DFBPACEI1130
Peptide sequence	QEPVLGPVRGPFP
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Gln-Glu-Pro-Val-Leu-Gly-Pro-Val-Arg-Gly-Pro-Phe-Pro

Single-letter amino acid

QEPVLGPVRGPFP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1392.73 Da	1392.62 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

6.95 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.2846^c

Hydrophilic residue ratio

76.92%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein
Precursor protein	β-Casein
Residue position	f(194-206)
Precursor protein(s) search	Source.1: DFBPPR7692 ---- Milk proteins ---- Beta-casein Source.2: DFBPPR7700 ---- Milk proteins ---- Beta-casein Source.3: DFBPPR7718 ---- Milk proteins ---- Beta-casein Source.4: 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

ACE-inhibitory activity	The peptide was isolated from the beta 20 fraction with 98.61% Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibition, so the peptide was a potential ACE-inhibitory peptide (data not shown).
Specific target protein(s)	Specific Target Protein(s): Angiotensin-converting enzyme

Taste properties & Structure

Bitterness

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

SMILES

N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)NCC(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)NCC(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N1[C@@]([H])(CCC1)C(=O)O

Preparation method

Mode of preparation	Fermentation
Enzyme(s)/starter culture	Milk proteins were fermented with Lactobacillus delbrueckii subsp. lactis CRL 581 at 40 ℃ for 4 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

The bioactive peptides released by CRL 581 strain may be used in the formulation of functional foods and nutraceuticals, representing a healthier and natural alternative for regulating blood pressure.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Villegas, J.M., Picariello, G., Mamone, G., Espeche Turbay, M.B., Savoy de Giori, G., Hebert, E.M. Milk-derived angiotensin-I-converting enzymeinhibitory peptides generated by Lactobacillus delbrueckii subsp. lactis CRL 581. Peptidomics. 2014, 1. DOI: 10.2478/ped-2014-0002
Other literature(s)	N.D
PubDate	2014