DFBP ID - DFBPGAGP0009(γ-Glutamyl peptides)

DFBP ID DFBPGAGP0009 Peptide sequence γ-EL Type Native peptide Peptide/Function name γ-Glutamyl peptide

Function-activity relationship

Main bioactivity Calcium-sensing receptor (CaSR) activation Otheir bioactivity DPP IV-inhibitory activity [D1], Multifunctional activity [D2]

Calculated physicochemical properties

Three-letter amino acid γ-Glu-Leu Single-letter amino acid γ-EL Peptide length 2 Peptide mass Experimental mass Theoretical mass N.D 260.28 Da c Net charge 0.00 c Isoelectric point (pI) 3.34 c IC50 N.D pIC50 N.D GRAVY 0.1500 c Hydrophilic residue ratio 50% c Peptide calculator To calculate the physicochemical properties of bioactive peptide.

Peptide source & Food-borne protein(s) search

Classification Animal Organism/Source Fermented food (cheese) Precursor protein N.D Residue position N.D Precursor protein(s) search No matching precursor protein found Link-research Inductive analysis Link 1: DFBPGAGP0001----Legumes, Edible beans (Phaseolus vulgaris L.)----N.D Link 2: DFBPGAGP0018----Fermented food (Soy sauce)----N.D Link 3: DFBPGAGP0034----Fermented food (Parmesan Cheese)----N.D Link 4: DFBPGAGP0044----Fermented food (Sourdough Fermentation)----N.D Link 5: DFBPGAGP0049----Synthesis peptide----Synthesis peptide

Biological/Functional activity & target protein

Calcium-sensing receptor (CaSR) activation N.D Specific target protein(s) N.D

Taste properties & Structure

Bitterness Literature report (1) The γ-Glu-Leu exhibited threshold concentration for an unspecific, slightly astringent mouth coating at 9.4 mmol/kg. (2) The bitterness of the cheese matured for 44 weeks was found to be induced by CaCl2 and MgCl2, as well as various bitter-tasting free amino acids, whereas bitter peptides were found to influence more the bitterness quality rather than the bitter intensity of the cheese [1]. Bitter prediction tools Bitter taste prediction SMILES N.D

Preparation method

Mode of preparation Fermentation Enzyme(s)/starter culture (1) The γ-glutamyl dipeptides might be enzymatically generated by a γ-glutamyl transpeptidase or γ-glutamyl transferase (GGT) from amino acids released upon protein hydrolysis. (2) Although the presence of GGT in cheese was suggested earlier [2], there is a study experimentally confirming the GGT activity in cheese [3].

Stability & Cytotoxicity

Peptide stability Literature report: The orosensory activity of these peptides is strongly dependent on the pH value. EHP-Tool: Enzymatic Hydrolysis Prediction Tool (EHP-Tool) Peptide cytotoxicity Literature report: N.D Prediction: ToxinPred

Additional information

Additional information (1) Gouda cheese samples ripened under controlled standard conditions for 4 weeks (GC4) and 44 weeks (GC44),  were confirmed to represent the characteristic flavor profiles of a young and a matured Gouda cheese, respectively. (2) The γ-Glu-Leu in 44-week-matured Gouda cheese (GC44) had a range of 7.10 μmol/kg which was given on a dry weight basis. (3) NaCl and amino acids are the congruent basic tastants required for the kokumi-enhancing activity of the γ-glutamyl peptides, thus confirming recent findings on the mouthfulness-enhancing activity of γ-glutamyl peptides on sodium chloride/L-glutamate mixtures in beans [4].

Database cross-references

DFBP [D1] DFBPDPIV0242 [D2] DFBPMUFU0739

BIOPEP-UWM [D3] -

APD [D4] -

BioPepDB [D5] -

MBPDB [D6] -

Reference(s)

Primary literature Toelstede S, Dunkel A, Hofmann T. A series of kokumi peptides impart the long-lasting mouthfulness of matured Gouda cheese. J Agric Food Chem. 2009 Feb 25;57(4):1440-8. PMID: 19170504 DOI: 10.1021/jf803376d Other literature(s) [1] Toelstede S, Hofmann T. Quantitative studies and taste re-engineering experiments toward the decoding of the nonvolatile sensometabolome of Gouda cheese. J Agric Food Chem. 2008 Jul 9;56(13):5299-307. doi: 10.1021/jf800552n. Epub 2008 Jun 17. PMID: 18557618. [2] Fox P F, Kelly A L. Indigenous enzymes in milk: Overview and historical aspects—Part 2[J]. International Dairy Journal, 2006, 16(6): 517-532. [3] Blel M, Guingamp M F, Gaillard J L, et al. Studies on the thermal sensitivity of γ-glutamyl transpeptidase measured with a modified test procedure and compared with that of alkaline phosphatase and lactoperoxidase in milk[J]. Le Lait, 2002, 82(5): 555-566. [4] Dunkel A, Köster J, Hofmann T. Molecular and sensory characterization of gamma-glutamyl peptides as key contributors to the kokumi taste of edible beans (Phaseolus vulgaris L.). J Agric Food Chem. 2007 Aug 8;55(16):6712-9. doi: 10.1021/jf071276u. Epub 2007 Jul 7. PMID: 17616213. PubDate 2009