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 - DFBPALGL0031(α-Glucosidase inhibitory peptide)

DFBP ID	DFBPALGL0031
Peptide sequence	LAHMIVAGA
Type	Native peptide
Peptide/Function name	α-Glucosidase inhibitory peptide, Anti-diabetic peptide

Function-activity relationship

Main bioactivity	α-Glucosidase inhibitory activity
Otheir bioactivity	ACE-inhibitory activity ^[D1], Multifunctional activity ^[D2]

Calculated physicochemical properties

Three-letter amino acid

Leu-Ala-His-Met-Ile-Val-Ala-Gly-Ala

Single-letter amino acid

LAHMIVAGA

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	882.08 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

7.79 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

1.8000^c

Hydrophilic residue ratio

88.89%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Quinoa seeds (Mengli 2 cultivar)
Precursor protein	Quinoa yoghurt beverage proteins
Residue position	N.D
Precursor protein(s) search	No matching precursor protein found
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

α-Glucosidase inhibitory activity	The peptide was purified from quinoa yoghurt beverages inoculated with Lactobacillus casei. It's a potential α-Glucosidase (AGI, EC 3.2.1.20) inhibitory peptide (IC₅₀ value of synthetic peptide was not determined).
Specific target protein(s)	Specific Target Protein(s): Lysosomal alpha-glucosidase

Taste properties & Structure

Bitterness

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

SMILES

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

Preparation method

Mode of preparation	Fermentation
Enzyme(s)/starter culture	At germination times of 0 h, 24 h and 72 h, quinoa milk substitutes were separately extracted and inoculated with the strains of LAB (Lactobacillus casei SY13) using a concentration of 6 log CFU/mL. They were then fermented for 8 h at 42 ℃ for the production of quinoa yoghurt beverage.

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

Dietary protein peptides obtained from quinoa yoghurt beverage fermented with probiotic Lactobacillus casei strains could play a protective role against diabetes and hypertension.

Database cross-references

DFBP

[D1]	DFBPACEI2067
[D2]	DFBPMUFU0611

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Obaroakpo JU, Liu L, Zhang S, Lu J, Pang X, Lv J. α-Glucosidase and ACE dual inhibitory protein hydrolysates and peptide fractions of sprouted quinoa yoghurt beverages inoculated with Lactobacillus casei. Food Chem. 2019 Nov 30;299:124985. PMID: 31279127 DOI: 10.1016/j.foodchem.2019.124985
Other literature(s)	N.D
PubDate	2019