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 - DFBPANOX0769(Antioxidative peptide)

DFBP ID	DFBPANOX0769
Peptide sequence	RYPS
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

Arg-Tyr-Pro-Ser

Single-letter amino acid

RYPS

Peptide length

Peptide mass

Experimental mass	Theoretical mass
522.4 Da	521.56 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

9.82 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-2.0500^c

Hydrophilic residue ratio

25%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein
Precursor protein	κ-Casein
Residue position	f(34-37)
Precursor protein(s) search	Source.1: DFBPPR1293 ---- Plant proteins ---- Copper-transporting ATPase HMA5 Source.2: DFBPPR1377 ---- Plant proteins ---- Calcium-dependent protein kinase 6 Source.3: DFBPPR2141 ---- Plant proteins ---- Beta-amylase 1, chloroplastic Source.4: DFBPPR2201 ---- Plant proteins ---- Aspartyl protease 37 Source.5: DFBPPR4610 ---- Plant proteins ---- Protein LOL3 Source.6: DFBPPR4681 ---- Plant proteins ---- Acidic leucine-rich nuclear phosphoprotein 32-related protein 2 Source.7: DFBPPR4945 ---- Plant proteins ---- Beta-amylase 2, chloroplastic Source.8: DFBPPR4967 ---- Plant proteins ---- Beta-amylase Source.9: DFBPPR5791 ---- Plant proteins ---- Uroporphyrinogen decarboxylase, chloroplastic Source.10: DFBPPR5986 ---- Plant proteins ---- Beta-amylase Source.11: DFBPPR6304 ---- Plant proteins ---- Porphobilinogen deaminase, chloroplastic Source.12: DFBPPR6768 ---- Plant proteins ---- Eukaryotic translation initiation factor 4B1 Source.13: DFBPPR6826 ---- Plant proteins ---- Beta-amylase Tri a 17 Source.14: DFBPPR7043 ---- Plant proteins ---- Beta-amylase Source.15: DFBPPR7527 ---- Plant proteins ---- Serine/threonine-protein phosphatase PP1 Source.16: DFBPPR7663 ---- Milk proteins ---- Kappa-casein Source.17: DFBPPR7686 ---- Milk proteins ---- Kappa-casein Source.18: DFBPPR7695 ---- Milk proteins ---- Kappa-casein Source.19: DFBPPR7715 ---- Milk proteins ---- Kappa-casein Source.20: DFBPPR8492 ---- Milk proteins ---- Kappa-casein Source.21: DFBPPR16208 ---- Animal proteins ---- Ammonium transporter Rh type B Source.22: DFBPPR16269 ---- Animal proteins ---- Ammonium transporter Rh type C Source.23: DFBPPR16553 ---- Animal proteins ---- Tapasin Source.24: DFBPPR17646 ---- Animal proteins ---- NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial Source.25: DFBPPR17793 ---- Animal proteins ---- Interleukin-17A Source.26: DFBPPR18240 ---- Animal proteins ---- Dual specificity protein kinase CLK3 Source.27: DFBPPR18323 ---- Animal proteins ---- Transcription factor E2F7 Source.28: DFBPPR18735 ---- Animal proteins ---- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1 Source.29: DFBPPR18761 ---- Animal proteins ---- Cytosolic non-specific dipeptidase Source.30: DFBPPR19020 ---- Animal proteins ---- Ammonium transporter Rh type B Source.31: DFBPPR19681 ---- Animal proteins ---- Fibroleukin Source.32: DFBPPR22686 ---- Animal proteins ---- Vertnin Source.33: DFBPPR8567 ---- Animal proteins ---- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1 Source.34: DFBPPR9343 ---- Animal proteins ---- Alpha-1-antitrypsin Source.35: DFBPPR9378 ---- Animal proteins ---- Ammonium transporter Rh type C Source.36: DFBPPR9446 ---- Animal proteins ---- Ammonium transporter Rh type B Source.37: DFBPPR9948 ---- Animal proteins ---- Vertnin Source.38: DFBPPR10058 ---- Animal proteins ---- Prospero homeobox protein 1 Source.39: DFBPPR10436 ---- Animal proteins ---- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1 Source.40: DFBPPR10680 ---- Animal proteins ---- Hemoglobin subunit pi Source.41: DFBPPR10753 ---- Animal proteins ---- Hypermethylated in cancer 1 protein Source.42: DFBPPR10796 ---- Animal proteins ---- Protrudin Source.43: DFBPPR11036 ---- Animal proteins ---- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1 Source.44: DFBPPR11622 ---- Animal proteins ---- Ammonium transporter Rh type C Source.45: DFBPPR11825 ---- Animal proteins ---- Solute carrier family 35 member B1 Source.46: DFBPPR11921 ---- Animal proteins ---- GATOR complex protein WDR59 Source.47: DFBPPR11988 ---- Animal proteins ---- Transmembrane channel-like protein 3 Source.48: DFBPPR12184 ---- Animal proteins ---- GRIN2-like protein Source.49: DFBPPR12518 ---- Animal proteins ---- Oxidized low-density lipoprotein receptor 1 Source.50: DFBPPR12839 ---- Animal proteins ---- Ammonium transporter Rh type B Source.51: DFBPPR12942 ---- Animal proteins ---- Ammonium transporter Rh type C Source.52: DFBPPR14022 ---- Animal proteins ---- Transcriptional regulator Myc-1 Source.53: DFBPPR14023 ---- Animal proteins ---- Transcriptional regulator Myc-2 Source.54: DFBPPR14563 ---- Marine protein ---- Beta-2 adrenergic receptor Source.55: DFBPPR14683 ---- Marine protein ---- Ammonium transporter Rh type C Source.56: DFBPPR15029 ---- Microorganism protein ---- Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase Source.57: DFBPPR15190 ---- Microorganism protein ---- Pescadillo homolog Source.58: DFBPPR8036 ---- Plant protein ---- Pectinesterase 3
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 RYPS 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])(CCCNC(=N)N)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CO)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]	DFBPACEI0912
[D2]	DFBPMUFU0560

[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