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 - DFBPANOX0161(Antioxidative peptide)

DFBP ID	DFBPANOX0161
Peptide sequence	VLEANPRSF
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

Val-Leu-Glu-Ala-Asn-Pro-Arg-Ser-Phe

Single-letter amino acid

VLEANPRSF

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1038.09 Da	1032.15 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

6.95 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.1444^c

Hydrophilic residue ratio

55.56%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Crude rice bran protein (Oryza sativa)
Precursor protein	Phytate-free rice bran protein
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR2672 ---- Plant proteins ---- 63 kDa globulin-like protein Source.2: DFBPPR5788 ---- Plant proteins ---- Globulin-1 S allele
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 antioxidative activity was determined using the ferric thiocyanate method and the peptide VLEANPRSF was isolated from the highest antioxidant fraction in phytate-free rice bran protein hydrolysate (data not shown).
Specific target protein(s)	N.D

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Non-bitter taste ^prediction

SMILES

N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CC(=O)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	The phytate-free rice bran protein was hydrolysed with proteases P under optimal conditions for 4 h.

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

Peptide has 100% homologies with the putative globulin-like Oryza sativa japonica cultivar group.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Adebiyi, A.P., Adebiyi, A.O., Ogawa, T., Muramoto, K. Purification and characterisation of antioxidative peptides from unfractionated rice bran protein hydrolysates. International Journal of Food Science & Technology. 2008, 43, 35-43. DOI: 10.1111/j.1365-2621.2006.01379.x
Other literature(s)	N.D
PubDate	2008