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 - DFBPACEI0908(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0908
Peptide sequence	RHPHP
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

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

Calculated physicochemical properties

Three-letter amino acid

Arg-His-Pro-His-Pro

Single-letter amino acid

RHPHP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
643.8 Da	642.72 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

11.04 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-2.8200^c

Hydrophilic residue ratio

40%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein
Precursor protein	κ-Casein
Residue position	f(97-101)
Precursor protein(s) search	Source.1: DFBPPR7686 ---- Milk proteins ---- Kappa-casein Source.2: DFBPPR7695 ---- Milk proteins ---- Kappa-casein Source.3: DFBPPR7715 ---- Milk proteins ---- Kappa-casein Source.4: DFBPPR8492 ---- Milk proteins ---- Kappa-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 F9 fraction of casein hydrolysates showed inhibition of 100% against Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1). The peptide RHPHP was isolated from the F9, so the peptide was a potential ACE-inhibitory peptide (Undetermined valid IC₅₀ value).
Specific target protein(s)	Specific Target Protein(s): Angiotensin-converting enzyme

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	No prediction can be made about the peptide bitterness. ^prediction

SMILES

N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N1[C@@]([H])(CCC1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Proteolytic enzymes secreted by the cold-adapted microorganism Arsukibacterium ikkense were tested for their ability to degrade caseins at low temperature and produce bioactive peptides. The caseins were extensively degraded (90%) after 24 h of hydrolysis at 5 °C and completely degraded at 25 °C, and many novel peptides were formed.

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

Secreted enzymes from cultures of A. ikkense could be a valuable enzyme preparation for inexpensive, energy-efficient production of potent bioactive peptides from caseins in milk at low temperatures.

Database cross-references

DFBP

[D1]	DFBPANOX0768
[D2]	DFBPMUFU0558

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	De Gobba C, Tompa G, Otte J. Bioactive peptides from caseins released by cold active proteolytic enzymes from Arsukibacterium ikkense. Food Chem. 2014 Dec 15;165:205-15. PMID: 25038668 DOI: 10.1016/j.foodchem.2014.05.082
Other literature(s)	N.D
PubDate	2014