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 - DFBPACEI1104(ACE-inhibitory peptide)

DFBP ID	DFBPACEI1104
Peptide sequence	LVYPFP
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	Antihypertensive activity ^[D1], Multifunctional activity ^[D2]

Calculated physicochemical properties

Three-letter amino acid

Leu-Val-Tyr-Pro-Phe-Pro

Single-letter amino acid

LVYPFP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	734.88 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.92 ^c

IC₅₀

132 uM

pIC₅₀

-2.121

GRAVY

1.0500^c

Hydrophilic residue ratio

83.33%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Probiotic fermented milk
Precursor protein	β-Casein
Residue position	f(58-63)
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

ACE-inhibitory activity	The peptide exhibited potent Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 132 uM.
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])(CC(C)C)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=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 by Bifidobacterium bifidum MF 20/5.

Stability & Cytotoxicity

Peptide stability

Literature report:	The peptide LVYPFP showed cleavage sites by pepsin releasing L + VYPFP at pH = 1.3, and L + VY + LVY + PFP as subproducts at pH > 2
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	N.D
Prediction:	ToxinPred

Additional information

This finding showed the potential for the use of this probiotic strain to produce fermented milk with a wider range of health benefits including reduction of blood pressure.

Database cross-references

DFBP

[D1]	DFBPANHY0114
[D2]	DFBPMUFU0219

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Gonzalez-Gonzalez C, Gibson T, Jauregi P. Novel probiotic-fermented milk with angiotensin I-converting enzyme inhibitory peptides produced by Bifidobacterium bifidum MF 20/5. Int J Food Microbiol. 2013 Oct 15;167(2):131-7. PMID: 24135669 DOI: 10.1016/j.ijfoodmicro.2013.09.002
Other literature(s)	[1] Ha, G.E., et al., Identification of Antihypertensive Peptides Derived from Low Molecular Weight Casein Hydrolysates Generated during Fermentation by Bifidobacterium longum KACC 91563. Korean Journal for Food Science of Animal Resources, 2015. 35(6): p. 738-747.
PubDate	2013