Discovery of peptides with saltiness-enhancing effects in enzymatic hydrolyzed Agaricus bisporus protein and evaluation of their salt-reduction property

Abstract

This study aimed to screen peptides with saltiness-enhancing effects from enzymatic hydrolyzed Agaricus bisporus protein and quantify their salt-reduction. The saltiness evaluation standard curve was first established to evaluate salinity. The peptide fractions (U-1, U-2, and U-3) were obtained from enzymatic hydrolyzed Agaricus bisporus protein by ultrafiltration. Quantitative calculations showed that the U-2 fraction (200-2000 Da) had the strongest saltiness-enhancing effect, and its perceived saltiness in 50 mmol NaCl solution was 60.24 ± 0.10 mmol/L. The peptide sequences were identified by liquid chromatography/mass spectrometry (LC-MS/MS). Results suggested that the potential peptides with saltiness-enhancing effects were umami peptides. Molecular docking with the umami receptor T1R1/T1R3 revealed that the key amino acid residues were Asp82, Glu392, Glu270, and Asp269. Furthermore, peptide YDPNDPEK (976.4138 Da), DDWDEDAPR(1117.4312 Da), and DVPDGPPPE (1058.4668 Da) were synthesized for salt-reduction quantification. 0.4 % peptide YDPNDPEK in NaCl solution was found to have a salt-reduction of 30 %, which provided the basic theory and data for the salt-reduction of peptide in enzymatic hydrolyzed Agaricus bisporus protein.

Keywords: Agaricus bisporus; Enzymatic hydrolyzation; Molecular docking; Salt-reduction; Saltiness-enhancing.