We have located links that may give you full text access.
Discovery of peptides with saltiness-enhancing effects in enzymatic hydrolyzed Agaricus bisporus protein and evaluation of their salt-reduction property.
Food Research International 2024 Februrary
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.
Full text links
Related Resources
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app
All material on this website is protected by copyright, Copyright © 1994-2024 by WebMD LLC.
This website also contains material copyrighted by 3rd parties.
By using this service, you agree to our terms of use and privacy policy.
Your Privacy Choices
You can now claim free CME credits for this literature searchClaim now
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app