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 - DFBPANOX0766(Antioxidative peptide)

DFBP ID	DFBPANOX0766
Peptide sequence	GTQY
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

Gly-Thr-Gln-Tyr

Single-letter amino acid

GTQY

Peptide length

Peptide mass

Experimental mass	Theoretical mass
468.9 Da	467.48 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.92 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-1.4750^c

Hydrophilic residue ratio

25%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein
Precursor protein	α_s1-Casein
Residue position	f(170-173)
Precursor protein(s) search	Source.1: DFBPPR1215 ---- Plant proteins ---- Peptide methionine sulfoxide reductase A4, chloroplastic Source.2: DFBPPR3570 ---- Plant proteins ---- Peptide methionine sulfoxide reductase A2-1 Source.3: DFBPPR3634 ---- Plant proteins ---- Peptide methionine sulfoxide reductase A2-2 Source.4: DFBPPR4656 ---- Plant proteins ---- SPX domain-containing membrane protein Os09g0521800 Source.5: DFBPPR5398 ---- Plant proteins ---- Sulfite reductase [ferredoxin], chloroplastic Source.6: DFBPPR5977 ---- Plant proteins ---- Putative AC transposase Source.7: DFBPPR6027 ---- Plant proteins ---- Phosphoenolpyruvate carboxykinase (ATP) Source.8: DFBPPR6162 ---- Plant proteins ---- Putative AC9 transposase Source.9: DFBPPR7688 ---- Milk proteins ---- Alpha-S1-casein Source.10: DFBPPR7694 ---- Milk proteins ---- Alpha-S1-casein Source.11: DFBPPR7717 ---- Milk proteins ---- Alpha-S1-casein Source.12: DFBPPR8488 ---- Milk proteins ---- Alpha-S1-casein Source.13: DFBPPR16462 ---- Animal proteins ---- Pantetheinase Source.14: DFBPPR17403 ---- Animal proteins ---- Insulin-degrading enzyme Source.15: DFBPPR17917 ---- Animal proteins ---- Poly(ADP-ribose) glycohydrolase Source.16: DFBPPR18457 ---- Animal proteins ---- Histone-lysine N-methyltransferase SUV39H2 Source.17: DFBPPR18815 ---- Animal proteins ---- Pantetheinase Source.18: DFBPPR20122 ---- Animal proteins ---- Mediator of RNA polymerase II transcription subunit 25 Source.19: DFBPPR20523 ---- Animal proteins ---- Vacuolar protein-sorting-associated protein 36 Source.20: DFBPPR21269 ---- Animal proteins ---- TOX high mobility group box family member 4 Source.21: DFBPPR21902 ---- Animal proteins ---- Centromere protein N Source.22: DFBPPR22517 ---- Animal proteins ---- F-box only protein 15 Source.23: DFBPPR9265 ---- Animal proteins ---- Pantetheinase Source.24: DFBPPR9495 ---- Animal proteins ---- Complement factor B Source.25: DFBPPR10843 ---- Animal proteins ---- Histone-lysine N-methyltransferase SUV39H2 Source.26: DFBPPR11222 ---- Animal proteins ---- FACT complex subunit SSRP1 Source.27: DFBPPR13037 ---- Animal proteins ---- Sodium-dependent multivitamin transporter Source.28: DFBPPR13092 ---- Animal proteins ---- Testin Source.29: DFBPPR13639 ---- Animal proteins ---- Carbonic anhydrase 6 Source.30: DFBPPR13826 ---- Animal proteins ---- Translocator protein Source.31: DFBPPR8145 ---- Plant protein ---- Luminal-binding protein
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 and F9-10 fractions of casein hydrolysates showed potent antioxidant activities, as shown in Table 1. The peptide GTQY was isolatd from the two fractions, so the peptide was a potentail antioxidant peptide.

Table 1. Peptides identified in the RP-HPLC fractions 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	85	66	YAKPA	κ-Casein (61-65)
			GTQY	α_s1-Casein (170-173)
			ARHPHP	κ-Casein (96-101)
			RHPHP	κ-Casein (97-101)
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	Non-bitter taste ^prediction

SMILES

NCC(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)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]	DFBPACEI0906
[D2]	DFBPMUFU0556

[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