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 - DFBPACEI0899(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0899
Peptide sequence	LLPSY
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	Anticancer activity ^[D1]

Calculated physicochemical properties

Three-letter amino acid

Leu-Leu-Pro-Ser-Tyr

Single-letter amino acid

LLPSY

Peptide length

Peptide mass

Experimental mass	Theoretical mass
591.327 Da	591.69 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.92 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.7800^c

Hydrophilic residue ratio

60%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Olive seed (Olea europaea)
Precursor protein	Olive seed protein
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR1450 ---- Plant proteins ---- Heat stress transcription factor C-1b Source.2: DFBPPR4674 ---- Plant proteins ---- Double-stranded RNA-binding protein 1 Source.3: DFBPPR8363 ---- Plant proteins ---- 13S globulin seed storage protein 1 Source.4: DFBPPR8365 ---- Plant proteins ---- 13S globulin seed storage protein 3 Source.5: DFBPPR8367 ---- Plant proteins ---- 13S globulin seed storage protein 2 Source.6: DFBPPR8484 ---- Milk proteins ---- Transforming growth factor beta-2 proprotein Source.7: DFBPPR17789 ---- Animal proteins ---- Secretory phospholipase A2 receptor Source.8: DFBPPR19475 ---- Animal proteins ---- Coronin-7 Source.9: DFBPPR19879 ---- Animal proteins ---- TBC1 domain family member 14 Source.10: DFBPPR8615 ---- Animal proteins ---- Transforming growth factor beta-2 proprotein Source.11: DFBPPR10010 ---- Animal proteins ---- Transforming growth factor beta-2 proprotein Source.12: DFBPPR11920 ---- Animal proteins ---- Transcription initiation factor TFIID subunit 2
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 thermolysin hydrolysate of the olive seed protein showed the highest ACE inhibiting ability (29 μg/ml), and the peptide LLPSY was isolated from the hydrolyzate (< 3 kDa fraction), and thus the peptide was a potential Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) 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])(CC(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Olive seed protein was hydrolyzed with Thermolysin.

Stability & Cytotoxicity

Peptide stability

Literature report:

The IC₅₀ value corresponding to the fraction < 3 kDa from the Thermolysin hydrolysate was slightly higher (36 μg/ml) after gastrointestinal digestion. Regarding % DH, as expected, it increased after the gastrointestinal digestion with 69.6 ± 3.6 for Thermolysin hydrolysates. These data revealed that ACE-inhibitory peptide extracted from olive seeds seemed to keep its bioactivity after in vitro gastrointestinal digestion.

EHP-Tool:

Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	N.D
Prediction:	ToxinPred

Additional information

N.D

Database cross-references

DFBP

[D1]	DFBPANCA0653

[D2]

[D3]

[D4]

[D5]

Reference(s)

Primary literature	Esteve C, Marina ML, García MC. Novel strategy for the revalorization of olive (Olea europaea) residues based on the extraction of bioactive peptides. Food Chem. 2015 Jan 15;167:272-80. PMID: 25148989 DOI: 10.1016/j.foodchem.2014.06.090
Other literature(s)	N.D
PubDate	2015