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 - DFBPANOX0749(Antioxidative peptide)

DFBP ID	DFBPANOX0749
Peptide sequence	YQLD
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

Tyr-Gln-Leu-Asp

Single-letter amino acid

YQLD

Peptide length

Peptide mass

Experimental mass	Theoretical mass
538.6 Da	537.56 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.13 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-1.1250^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(154-157)
Precursor protein(s) search	Source.1: DFBPPR0913 ---- Plant proteins ---- Endoribonuclease Dicer homolog 4 Source.2: DFBPPR1016 ---- Plant proteins ---- Calcium-dependent protein kinase 12 Source.3: DFBPPR1830 ---- Plant proteins ---- Endoribonuclease Dicer homolog 3a Source.4: DFBPPR2215 ---- Plant proteins ---- ABC transporter G family member 50 Source.5: DFBPPR2913 ---- Plant proteins ---- DNA damage-binding protein 1 Source.6: DFBPPR2993 ---- Plant proteins ---- Beta-glucosidase 5 Source.7: DFBPPR4586 ---- Plant proteins ---- Protein MEI2-like 2 Source.8: DFBPPR4590 ---- Plant proteins ---- Protein MEI2-like 5 Source.9: DFBPPR4899 ---- Plant proteins ---- Casein kinase 1 Source.10: DFBPPR5368 ---- Plant proteins ---- Desiccation protectant protein Lea14 homolog Source.11: DFBPPR7680 ---- Milk proteins ---- Alpha-S1-casein Source.12: DFBPPR7688 ---- Milk proteins ---- Alpha-S1-casein Source.13: DFBPPR7694 ---- Milk proteins ---- Alpha-S1-casein Source.14: DFBPPR7717 ---- Milk proteins ---- Alpha-S1-casein Source.15: DFBPPR8488 ---- Milk proteins ---- Alpha-S1-casein Source.16: DFBPPR16954 ---- Animal proteins ---- Alpha-2-antiplasmin Source.17: DFBPPR17936 ---- Animal proteins ---- Tyrosine-protein kinase receptor Tie-1 Source.18: DFBPPR18189 ---- Animal proteins ---- Palmitoyltransferase ZDHHC6 Source.19: DFBPPR18340 ---- Animal proteins ---- Voltage-dependent anion-selective channel protein 2 Source.20: DFBPPR19372 ---- Animal proteins ---- Epithelial cell adhesion molecule Source.21: DFBPPR19593 ---- Animal proteins ---- DNA-directed RNA polymerase III subunit RPC1 Source.22: DFBPPR19692 ---- Animal proteins ---- Basal cell adhesion molecule Source.23: DFBPPR19925 ---- Animal proteins ---- Complement factor H Source.24: DFBPPR20859 ---- Animal proteins ---- Trafficking protein particle complex subunit 4 Source.25: DFBPPR21010 ---- Animal proteins ---- Store-operated calcium entry-associated regulatory factor Source.26: DFBPPR21268 ---- Animal proteins ---- Mitochondrial import receptor subunit TOM40 homolog Source.27: DFBPPR21596 ---- Animal proteins ---- Origin recognition complex subunit 2 Source.28: DFBPPR21742 ---- Animal proteins ---- Proteasomal ATPase-associated factor 1 Source.29: DFBPPR22009 ---- Animal proteins ---- p21-activated protein kinase-interacting protein 1 Source.30: DFBPPR9241 ---- Animal proteins ---- Epithelial cell adhesion molecule Source.31: DFBPPR9329 ---- Animal proteins ---- Voltage-dependent anion-selective channel protein 2 Source.32: DFBPPR9357 ---- Animal proteins ---- Interleukin-4 receptor subunit alpha Source.33: DFBPPR9997 ---- Animal proteins ---- Aryl hydrocarbon receptor nuclear translocator-like protein 1 Source.34: DFBPPR10210 ---- Animal proteins ---- Fibroblast growth factor receptor 1 Source.35: DFBPPR10234 ---- Animal proteins ---- Fibroblast growth factor receptor 3 Source.36: DFBPPR11633 ---- Animal proteins ---- DNA-directed RNA polymerase III subunit RPC1 Source.37: DFBPPR12095 ---- Animal proteins ---- Proteasomal ATPase-associated factor 1 Source.38: DFBPPR13049 ---- Animal proteins ---- Alpha-S1-casein Source.39: DFBPPR14103 ---- Marine protein ---- Proteasome subunit beta type-9 Source.40: DFBPPR14607 ---- Marine protein ---- Proteasome subunit beta type-9 Source.41: DFBPPR15156 ---- Microorganism protein ---- Vacuolar protein sorting/targeting protein 10 Source.42: DFBPPR15190 ---- Microorganism protein ---- Pescadillo homolog Source.43: DFBPPR15373 ---- Microorganism protein ---- Protoheme IX farnesyltransferase, mitochondrial Source.44: DFBPPR15454 ---- Microorganism protein ---- Beta-galactosidase Source.45: DFBPPR15558 ---- Microorganism protein ---- Protein CFT1 Source.46: DFBPPR15593 ---- Microorganism protein ---- SWR1-complex protein 3 Source.47: DFBPPR15733 ---- Microorganism protein ---- J protein JJJ2
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 YQLD 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	Bitter taste ^prediction

SMILES

N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(=O)O)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