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 - DFBPACEI0065(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0065
Peptide sequence	DKIHPF
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

Asp-Lys-Ile-His-Pro-Phe

Single-letter amino acid

DKIHPF

Peptide length

Peptide mass

Experimental mass	Theoretical mass
755.3 Da	755.86 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

7.76 ^c

IC₅₀

193.9 mg/L (256.8 uM)

pIC₅₀

-2.288

GRAVY

-0.8167^c

Hydrophilic residue ratio

50%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein
Precursor protein	β-Casein
Residue position	f(47-52)
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	Link 1: DFBPACEI0062----Spanish cheeses (Manchego, Roncal, Idiazabal, Goat, Cabrales)----β-Casein Link 2: DFBPACEI1444----Caprine milk protein, Caprine kefir----β-Casein

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 193.9 mg/liter (256.8 umol/liter), and its ACE inhibitory pattern was shown by Lineweaver–Burk plots to be a competitive inhibition pattern.
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(=O)O)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CC1=CN=C-N1)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	L. lactis subsp. cremoris FT4 was used to produce fermented milk containing ACE-inhibitory peptides.

Stability & Cytotoxicity

Peptide stability

Literature report:	The peptide was completely resistant to hydrolysis by trypsin and chymotrypsin (data not shown).
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	Non-Toxin
Prediction:	ToxinPred

Additional information

Once the peptide was generated, the inhibitory peptide was resistant to further proteolysis either during dairy processing or by trypsin and chymotrypsin.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Gobbetti M, Ferranti P, Smacchi E, Goffredi F, Addeo F. Production of angiotensin-I-converting-enzyme-inhibitory peptides in fermented milks started by Lactobacillus delbrueckii subsp. bulgaricus SS1 and Lactococcus lactis subsp. cremoris FT4. Appl Environ Microbiol. 2000 Sep;66(9):3898-904. PMID: 10966406 DOI: 10.1128/AEM.66.9.3898-3904.2000
Other literature(s)	[1] Papadimitriou C G, Vafopoulou-Mastrojiannaki A, Silva S V, et al. Identification of peptides in traditional and probiotic sheep milk yoghurt with angiotensin I-converting enzyme (ACE)-inhibitory activity[J]. Food Chemistry, 2007, 105(2):647-656. [2] Gómez-Ruiz J ?, Taborda G, Amigo L, et al. Identification of ACE-inhibitory peptides in different Spanish cheeses by tandem mass spectrometry[J]. European Food Research (&) Technology, 2006, 223(5):595-601. [3] Ven, C. van der. Biochemical and functional characterisation of casein and whey protein hydrolysates: a study on the correlations between biochemical and functional properties using multivariate data analysis[J]. 2002. [4] Farvin K H S, Baron C P, Nielsen N S, et al. Antioxidant activity of yoghurt peptides: Part 2 – Characterisation of peptide fractions[J]. Food Chemistry, 2010, 123(4):1090-1097. [5] Ha G E , Chang O K , Jo S M , et al. Identification of Antihypertensive Peptides Derived from Low Molecular Weight Casein Hydrolysates Generated during Fermentation by Bifidobacterium longum KACC 91563[J]. Hangug chugsan sigpum haghoeji = Korean journal for food science of animal resources, 2015, 35(6):738-747.
PubDate	2000