Identification of novel saltiness/saltiness enhancing peptides in egg proteins: Molecular docking, action mechanism and in vitro activity validation
In this study, novel saltiness/saltiness enhancing peptides VESQTNGIIR, NQITKPNDVY, and DEDTQAMP were identified from the hen egg proteins via virtual enzymatic, molecular docking, and electronic tongue analysis. Their saltiness enhancement effect was analyzed by e-tongue analysis. Saltiness enhance...
Saved in:
| Main Authors: | , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2025-02-01
|
| Series: | Food Chemistry: X |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2590157525001087 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| Summary: | In this study, novel saltiness/saltiness enhancing peptides VESQTNGIIR, NQITKPNDVY, and DEDTQAMP were identified from the hen egg proteins via virtual enzymatic, molecular docking, and electronic tongue analysis. Their saltiness enhancement effect was analyzed by e-tongue analysis. Saltiness enhancement rates of saltiness peptide VESQTNGIIR were 47.24 %, 95.28 % and 105.94 %, and those of the saltiness peptide NQITKPNDVY were 32.40 %, 70.16 %, and 71.25 % at the salt reduction concentrations of 25 %, 35 % and 45 %, respectively. Saltiness enhancement rates of saltiness enhancing peptide DEDTQAMP were 5.83 % and 11.24 % at 25 % and 35 % salt reduction concentrations, respectively. Molecular docking demonstrated that Glu286, Arg330, Arg424, and Arg583 may be the key amino acids interacting with TMC4, whereas that carbon hydrogen bond, conventional hydrogen bond, and attractive charge interactions were important forces in peptides-TMC interactions. The study indicated that the peptides VESQTNGIIR and NQITKPNDVY may be ideal saltiness/saltiness enhancing peptides. |
|---|---|
| ISSN: | 2590-1575 |