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 - DFBPANOX0757(Antioxidative peptide)

DFBP ID	DFBPANOX0757
Peptide sequence	YGLN
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-Gly-Leu-Asn

Single-letter amino acid

YGLN

Peptide length

Peptide mass

Experimental mass	Theoretical mass
466.4 Da	465.50 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.92 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.3500^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(38-41)
Precursor protein(s) search	Source.1: DFBPPR1147 ---- Plant proteins ---- ABC transporter C family member 13 Source.2: DFBPPR1622 ---- Plant proteins ---- ATP synthase subunit alpha, mitochondrial Source.3: DFBPPR1832 ---- Plant proteins ---- ATP-dependent zinc metalloprotease FTSH 7, chloroplastic Source.4: DFBPPR1947 ---- Plant proteins ---- Calcium-transporting ATPase 10, plasma membrane-type Source.5: DFBPPR2277 ---- Plant proteins ---- Protein TOC75, chloroplastic Source.6: DFBPPR2792 ---- Plant proteins ---- Probable cinnamyl alcohol dehydrogenase 8A Source.7: DFBPPR2814 ---- Plant proteins ---- Probable cinnamyl alcohol dehydrogenase 8D Source.8: DFBPPR2936 ---- Plant proteins ---- Putative germin-like protein 2-1 Source.9: DFBPPR3415 ---- Plant proteins ---- Expansin-A33 Source.10: DFBPPR3456 ---- Plant proteins ---- Maturase K Source.11: DFBPPR4787 ---- Plant proteins ---- 60S ribosomal protein L7a-1 Source.12: DFBPPR4814 ---- Plant proteins ---- Zinc finger CCCH domain-containing protein 47 Source.13: DFBPPR4823 ---- Plant proteins ---- 60S ribosomal protein L7a-2 Source.14: DFBPPR5021 ---- Plant proteins ---- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic Source.15: DFBPPR5064 ---- Plant proteins ---- ATP synthase subunit alpha, mitochondrial Source.16: DFBPPR5354 ---- Plant proteins ---- Protein P21 Source.17: DFBPPR5522 ---- Plant proteins ---- ABC transporter C family MRP4 Source.18: DFBPPR5696 ---- Plant proteins ---- ATP synthase subunit alpha, mitochondrial Source.19: DFBPPR5946 ---- Plant proteins ---- Maturase K Source.20: DFBPPR6214 ---- Plant proteins ---- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic Source.21: DFBPPR6398 ---- Plant proteins ---- ATP synthase subunit alpha, mitochondrial Source.22: DFBPPR6809 ---- Plant proteins ---- ATP synthase subunit alpha, mitochondrial Source.23: DFBPPR6882 ---- Plant proteins ---- Maturase K Source.24: DFBPPR7170 ---- Plant proteins ---- Maturase K Source.25: DFBPPR7470 ---- Plant proteins ---- ATP synthase subunit alpha, mitochondrial Source.26: DFBPPR7686 ---- Milk proteins ---- Kappa-casein Source.27: DFBPPR7695 ---- Milk proteins ---- Kappa-casein Source.28: DFBPPR7715 ---- Milk proteins ---- Kappa-casein Source.29: DFBPPR7744 ---- Plant proteins ---- Maturase K Source.30: DFBPPR8492 ---- Milk proteins ---- Kappa-casein Source.31: DFBPPR16248 ---- Animal proteins ---- Abnormal spindle-like microcephaly-associated protein homolog Source.32: DFBPPR17089 ---- Animal proteins ---- Neuronal acetylcholine receptor subunit alpha-7 Source.33: DFBPPR18901 ---- Animal proteins ---- Nuclear factor of activated T-cells, cytoplasmic 1 Source.34: DFBPPR19794 ---- Animal proteins ---- Bone morphogenetic protein 15 Source.35: DFBPPR20550 ---- Animal proteins ---- G-protein coupled receptor family C group 6 member A Source.36: DFBPPR20734 ---- Animal proteins ---- Probable imidazolonepropionase Source.37: DFBPPR20963 ---- Animal proteins ---- Protein kintoun Source.38: DFBPPR21279 ---- Animal proteins ---- 40S ribosomal protein S29 Source.39: DFBPPR21587 ---- Animal proteins ---- Abnormal spindle-like microcephaly-associated protein homolog Source.40: DFBPPR9102 ---- Animal proteins ---- Nuclear factor of activated T-cells, cytoplasmic 1 Source.41: DFBPPR9500 ---- Animal proteins ---- 40S ribosomal protein S29 Source.42: DFBPPR9723 ---- Animal proteins ---- SLA class II histocompatibility antigen, DQ haplotype D alpha chain Source.43: DFBPPR9735 ---- Animal proteins ---- SLA class II histocompatibility antigen, DQ haplotype C alpha chain Source.44: DFBPPR10084 ---- Animal proteins ---- Nuclear factor 1 B-type Source.45: DFBPPR10197 ---- Animal proteins ---- Neuronal acetylcholine receptor subunit alpha-7 Source.46: DFBPPR10526 ---- Animal proteins ---- LIM domain kinase 2 Source.47: DFBPPR11333 ---- Animal proteins ---- Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1 Source.48: DFBPPR11699 ---- Animal proteins ---- NEDD8-activating enzyme E1 regulatory subunit Source.49: DFBPPR11777 ---- Animal proteins ---- Homeobox protein Hox-B3 Source.50: DFBPPR13266 ---- Animal proteins ---- Deoxyribonuclease-1 Source.51: DFBPPR13482 ---- Animal proteins ---- N-acetylglucosamine-6-sulfatase Source.52: DFBPPR13785 ---- Animal proteins ---- Bone morphogenetic protein 15 Source.53: DFBPPR13936 ---- Animal proteins ---- Abnormal spindle-like microcephaly-associated protein homolog Source.54: DFBPPR14901 ---- Microorganism protein ---- Plasma membrane ATPase Source.55: DFBPPR15105 ---- Microorganism protein ---- Arginase Source.56: DFBPPR15499 ---- Microorganism protein ---- Mediator of RNA polymerase II transcription subunit 12 Source.57: DFBPPR15550 ---- Microorganism protein ---- COPII coat assembly protein SEC16 Source.58: DFBPPR15734 ---- Microorganism protein ---- 40S ribosomal protein S29 Source.59: DFBPPR15795 ---- Microorganism protein ---- L-lactate dehydrogenase Source.60: DFBPPR7856 ---- Plant protein ---- Maturase K Source.61: DFBPPR8093 ---- Plant protein ---- ATP synthase subunit alpha, mitochondrial Source.62: DFBPPR8230 ---- Plant protein ---- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic Source.63: DFBPPR8240 ---- Plant protein ---- ATP synthase subunit alpha, mitochondrial
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 F16 fraction of casein hydrolysates showed potent antioxidant activity, as shown in Table 1. The peptide YGLN was isolatd from the fraction, so the peptide was a potentail antioxidant peptide.

Table 1. Peptides identified in the RP-HPLC F16 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
F16	72	31	YGLN	κ-Casein (38-41)
			YYQQKPV	κ-Casein (42-48)
			FL	Multiple
^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])(Cc1ccc(O)cc1)C(=O)NCC(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(=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