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 - DFBPACEI1401(ACE-inhibitory peptide)

DFBP ID	DFBPACEI1401
Peptide sequence	YQEPVLGPVRGPFPIIV
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide, Peptide 7

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	Antihypertensive activity ^[D1], Antimicrobial activity ^[D2], Antithrombotic activity ^[D3], Immunomodulatory activity ^[D4], Multifunctional activity ^[D5]

Calculated physicochemical properties

Three-letter amino acid

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

Single-letter amino acid

YQEPVLGPVRGPFPIIV

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1880 Da	1881.24 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

6.88 ^c

IC₅₀

101 μM ^[3]

pIC₅₀

-2.004

GRAVY

0.4824^c

Hydrophilic residue ratio

76.47%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine milk protein
Precursor protein	β-Casein
Residue position	f(193-209)
Precursor protein(s) search	Source.1: DFBPPR7718 ---- Milk proteins ---- Beta-casein Source.2: DFBPPR8489 ---- Milk proteins ---- Beta-casein
Link-research Inductive analysis	Link 1: DFBPACEI0427----Bovine milk----β-Casein

Biological/Functional activity & target protein

ACE-inhibitory activity	(1) The peptide had an inhibition efficiency ratio for Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) of 0.14%/peptide concentration (μg/mL). (2) The peptide exhibited potent ACE-inhibitory activity with an IC₅₀ value of 101 μM ^[3].
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])(Cc1ccc(O)cc1)C(=O)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)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(C(C)C)C(=O)O

Preparation method

Mode of preparation	Fermentation
Enzyme(s)/starter culture	The peptides was released from bovine caseins during fermentation by Lactobacillus casei Shirota or Streptococcus thermophilus.

Stability & Cytotoxicity

Peptide stability

Literature report:	Using ExPASy PeptideCutter tool and departing from peptide 7 sequence, it was determined that pepsin and trypsin would hydrolyse this peptide in fragments GPFPIIV and QEPVLGPVR.
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	N.D
Prediction:	ToxinPred

Additional information

The results of the present work provide a basis for further applications of M. pomifera proteases in the food industry for the development of functional foods and nutraceuticals ^[4].

Database cross-references

DFBP

[D1]	DFBPANHY0117
[D2]	DFBPAMIC0198
[D3]	DFBPANTH0103
[D4]	DFBPIMMU0033
[D5]	DFBPMUFU0119

[D6]

[D7]

[D8]

[D9]

Reference(s)

Primary literature	Rojas-Ronquillo, R., Cruz-Guerrero, A., Flores-Nájera, A., Rodríguez-Serrano, G., Gómez-Ruiz, L., Reyes-Grajeda, J.P., et al. Antithrombotic and angiotensin-converting enzyme inhibitory properties of peptides released from bovine casein by Lactobacillus casei Shirota. International Dairy Journal. 2012, 26, 147-54. DOI: 10.1016/j.idairyj.2012.05.002
Other literature(s)	[1] Yamamoto, N., A. Akino, and T. Takano, Antihypertensive effect of the peptides derived from casein by an extracellular proteinase from Lactobacillus helveticus CP790. J Dairy Sci, 1994. 77(4): p. 917-22. [2] Cheng, S., et al., Food-derived antithrombotic peptides: Preparation, identification, and interactions with thrombin. Crit Rev Food Sci Nutr, 2019: p. 1-15. [3] Robert, M.C., et al., Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765. J Agric Food Chem, 2004. 52(23): p. 6923-31. [4] Corrons, María Alicia, Liggieri C S , Trejo, Sebastián Alejandro, et al. ACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latex[J]. Food Research International, 2017, 93:8-15.
PubDate	2012