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 - DFBPACEI2120(ACE-inhibitory peptide)

DFBP ID	DFBPACEI2120
Peptide sequence	LLYQEPVLGPVR
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

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

Single-letter amino acid

LLYQEPVLGPVR

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1383.63 Da	1383.64 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

6.88 ^c

IC₅₀

872.4 ± 11.79 μM

pIC₅₀

-2.941

GRAVY

0.2833^c

Hydrophilic residue ratio

66.67%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Horse gram (Macrotyloma uniflorum)
Precursor protein	Horse gram flour protein
Residue position	N.D
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 showed very weak Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 872.4 ± 11.79 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])(CC(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)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)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Horse gram flour was hysrolyzed with alcalase at 55 °C for 3 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 ACE inhibitory peptides identified from horse gram hydrolysate shows promise to be used as a functional food ingredient for controlling hypertension.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Bhaskar, B., Ananthanarayan, L., Jamdar, S. Purification, identification, and characterization of novel angiotensin I-converting enzyme (ACE) inhibitory peptides from alcalase digested horse gram flour. Lwt. 2019, 103, 155-61. DOI: 10.1016/j.lwt.2018.12.059
Other literature(s)	N.D
PubDate	2019