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 - DFBPHYCP0019(Hypocholesterolemic peptide)

DFBP ID	DFBPHYCP0019
Peptide sequence	GQEQSHQDEGVIVR
Type	Native peptide
Peptide/Function name	Hypocholesterolemic peptide

Function-activity relationship

Main bioactivity	Hypocholesterolemic activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Gly-Gln-Glu-Gln-Ser-His-Gln-Asp-Glu-Gly-Val-Ile-Val-Arg

Single-letter amino acid

GQEQSHQDEGVIVR

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1581.67 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

4.47 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-1.2429^c

Hydrophilic residue ratio

35.71%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Freshwater clams (Corbicula fluminea)
Precursor protein	Freshwater clam muscle protein
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR0009 ---- Plant protein ---- Conglutin beta 1
Link-research Inductive analysis	Link 1: DFBPHYCP0021----Lupin----β-conglutin

Biological/Functional activity & target protein

Hypocholesterolemic activity

The bile-acid-binding capacity and inhibition of cholesterol micelle formation were subsequently investigated using pepsin-digested freshwater clam hydrolysate through ultrafiltration (UF) fractionation or size exclusion chromatography. Fraction f showed the highest inhibitory efficiency ratio (IER), and its inhibition- peptide content percentage was 831.5% mg/mL. The amino acid sequences of two hypocholesterolemic peptides were Val–Lys–Pro and Val–Lys–Lys, with IERs of 64.8% and 10.2% mg/mL, respectively.

TABLE 1 Peptide sequences and inhibition against the cholesterol micelle formation of peaks of f-1 and f-2 from fraction f of freshwater clam hydrolysate after digestion with pepsin
Peak	Sequence	Peptide concentration (mg/mL)	Inhibition (%)	IER (%/mg/mL)
f-1	Val-Lys-Pro	0.5	32.4	64.8
f-2	Val-Lys-Lys	0.5	5.1	10.2

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])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)NCC(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	The muscles of freshwater clams were extracted separately using hot water. Subsequently, the edible muscle part was freeze-dried, hydrolyzed at 50 ℃ using Protamex to obtain the freshwater clam hydrolysate, and then digested with pepsin.

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

This freshwater clam hydrolysate is expected to be a useful ingredient in physiologically functional foods for the prevention of hypertension and hypercholesterolemia.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Lin, Y.-H., Tsai, J.-S., Chen, G.-W. Purification and identification of hypocholesterolemic peptides from freshwater clam hydrolysate with in vitro gastrointestinal digestion. Journal of Food Biochemistry. 2017, 41. DOI: 10.1111/jfbc.12385
Other literature(s)	N.D
PubDate	2017