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 - DFBPANOX0773(Antioxidative peptide)

DFBP ID	DFBPANOX0773
Peptide sequence	YAKP
Type	Native peptide
Peptide/Function name	Antioxidative peptide

Function-activity relationship

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

Calculated physicochemical properties

Three-letter amino acid

Tyr-Ala-Lys-Pro

Single-letter amino acid

YAKP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
478.4 Da	477.55 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

9.70 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-1.2500^c

Hydrophilic residue ratio

50%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein
Precursor protein	κ-Casein
Residue position	f(61-64)
Precursor protein(s) search	Source.1: DFBPPR1082 ---- Plant proteins ---- DNA polymerase alpha catalytic subunit Source.2: DFBPPR1528 ---- Plant proteins ---- Cyclin-dependent kinase C-2 Source.3: DFBPPR1569 ---- Plant proteins ---- 2-oxoglutarate-dependent dioxygenase 33 Source.4: DFBPPR1721 ---- Plant proteins ---- Cyclin-dependent kinase C-1 Source.5: DFBPPR2359 ---- Plant proteins ---- Probable ion channel CASTOR Source.6: DFBPPR2839 ---- Plant proteins ---- Multicopper oxidase LPR1 homolog 2 Source.7: DFBPPR3575 ---- Plant proteins ---- Kinesin-like protein KIN-10B Source.8: DFBPPR6723 ---- Plant proteins ---- Ubiquitin-conjugating enzyme E2-23 kDa Source.9: DFBPPR7455 ---- Plant proteins ---- Phosphoglucomutase, chloroplastic Source.10: DFBPPR7663 ---- Milk proteins ---- Kappa-casein Source.11: DFBPPR7686 ---- Milk proteins ---- Kappa-casein Source.12: DFBPPR7695 ---- Milk proteins ---- Kappa-casein Source.13: DFBPPR7715 ---- Milk proteins ---- Kappa-casein Source.14: DFBPPR8492 ---- Milk proteins ---- Kappa-casein Source.15: DFBPPR17587 ---- Animal proteins ---- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial Source.16: DFBPPR17802 ---- Animal proteins ---- Peptidyl-prolyl cis-trans isomerase FKBP4 Source.17: DFBPPR19364 ---- Animal proteins ---- Actin-related protein 2/3 complex subunit 3 Source.18: DFBPPR20847 ---- Animal proteins ---- Protein SHQ1 homolog Source.19: DFBPPR22318 ---- Animal proteins ---- Transmembrane protein 218 Source.20: DFBPPR22759 ---- Animal proteins ---- Uncharacterized protein C1orf141 homolog Source.21: DFBPPR12761 ---- Animal proteins ---- Trichohyalin Source.22: DFBPPR13716 ---- Animal proteins ---- Trichohyalin Source.23: DFBPPR14389 ---- Marine protein ---- 60 kDa chaperonin, chloroplastic
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 F9-10 fraction of casein hydrolysates showed potent antioxidant activity, as shown in Table 1. The peptide YAKP was isolatd from the fraction, so the peptide was a potentail antioxidant peptide.

Table 1. Peptides identified in the RP-HPLC F9-10 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
F9-10	66	62	RYPS	κ-Casein (34-37)
			SRYPS	κ-Casein (33-37)
			VY	Multiple
			AYPS	α_s1-Casein (158-161)
			GTQY	α_s1-Casein (170-173)
			YAKP	κ-Casein (61-64)
			ARHPHP	κ-Casein (96-101)
^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	Bitter taste ^prediction

SMILES

N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CCCCN)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]	DFBPACEI0916
[D2]	DFBPMUFU0562

[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