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 - DFBPANOX0751(Antioxidative peptide)

DFBP ID	DFBPANOX0751
Peptide sequence	RDMPIQ
Type	Native peptide
Peptide/Function name	Antioxidative peptide

Function-activity relationship

Main bioactivity	Antioxidative activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Arg-Asp-Met-Pro-Ile-Gln

Single-letter amino acid

RDMPIQ

Peptide length

Peptide mass

Experimental mass	Theoretical mass
760 Da	758.88 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

6.74 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-1.1167^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(183-188)
Precursor protein(s) search	Source.1: DFBPPR7681 ---- Milk proteins ---- Beta-casein Source.2: DFBPPR7692 ---- Milk proteins ---- Beta-casein Source.3: DFBPPR7700 ---- Milk proteins ---- Beta-casein Source.4: DFBPPR7718 ---- Milk proteins ---- Beta-casein Source.5: DFBPPR8489 ---- Milk proteins ---- Beta-casein Source.6: DFBPPR13067 ---- Animal 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

Antioxidative activity

The F17 fraction of casein hydrolysates showed potent antioxidant activity, as shown in Table 1. The peptide RDMPIQ was isolatd from the fraction, so the peptide was a potentail antioxidant peptide.

Table 1. Peptides identified in the RP-HPLC F17 fraction with high radical scavenging capacity from the 25 °C 24 h casein hydrolysate made with A. ikkense supernatant. Peptides are mentioned in order of decreasing abundance as judged from peak height.
RP-HPLC fraction ^a	Antioxidant activity		Peptide	Orign
	ABTS radical scvenging ^b	Inhibition of lipid oxidation in liposomes ^c
F17	65	22	VLSRYPS	κ-Casein (31-37)
			TIASGEP	κ-Casein (124-130)
			YQLD	α_s1-Casein (154-157)
			GYLEQ	α_s1-Casein (93-97)
			RDMPIQ	β-Casein (183-188)
			YPELF	α_s1-Casein (146-150)
^a Collected RP-HPLC fractions were lyophilised and redissolved in 500 μL of milliQ water and further diluted before each test. ^bc Samples were diluted 10 times before the measurement.

Specific target protein(s)

N.D

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])(CC(=O)O)C(=O)N[C@@]([H])(CCSC)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CCC(=O)N)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

[D1]

[D2]

[D3]

[D4]

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