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 - DFBPACEI1435(ACE-inhibitory peptide)

DFBP ID	DFBPACEI1435
Peptide sequence	HKEMPFPKYPVEPF
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

His-Lys-Glu-Met-Pro-Phe-Pro-Lys-Tyr-Pro-Val-Glu-Pro-Phe

Single-letter amino acid

HKEMPFPKYPVEPF

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1746.1 Da	1746.05 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

7.71 ^c

IC₅₀

> 1000 μM

pIC₅₀

> -3.0

GRAVY

-1.0000^c

Hydrophilic residue ratio

57.14%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein
Precursor protein	β-Casein
Residue position	f(121-134)
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 exhibited very weak Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of > 1000 μM.
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])(CC1=CN=C-N1)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CCSC)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)O

Preparation method

Mode of preparation	Fermentation
Enzyme(s)/starter culture	Milk proteins was fermented with Lactobacillus (Lb.) helveticus NCC 2765.

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

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Robert MC, Razaname A, Mutter M, Juillerat MA. Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765. J Agric Food Chem. 2004 Nov 17;52(23):6923-31. PMID: 15537298 DOI: 10.1021/jf049510t
Other literature(s)	N.D
PubDate	2004