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...
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| Format: | Article |
| Language: | English |
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Elsevier
2025-02-01
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| Series: | Food Chemistry: X |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2590157525001087 |
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| author | Yaxin Cao Linyuezhi Yan Di Liu Qian Zhang Wenzhu Zhao Lin Yuan Yiding Yu Zhipeng Yu |
| author_facet | Yaxin Cao Linyuezhi Yan Di Liu Qian Zhang Wenzhu Zhao Lin Yuan Yiding Yu Zhipeng Yu |
| author_sort | Yaxin Cao |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-de5471999b1f4c078629ea41e3cd0f90 |
| institution | Kabale University |
| issn | 2590-1575 |
| language | English |
| publishDate | 2025-02-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Food Chemistry: X |
| spelling | doaj-art-de5471999b1f4c078629ea41e3cd0f902025-02-09T05:01:08ZengElsevierFood Chemistry: X2590-15752025-02-0126102261Identification of novel saltiness/saltiness enhancing peptides in egg proteins: Molecular docking, action mechanism and in vitro activity validationYaxin Cao0Linyuezhi Yan1Di Liu2Qian Zhang3Wenzhu Zhao4Lin Yuan5Yiding Yu6Zhipeng Yu7School of Food Science and Engineering, Hainan University, Haikou 570228, PR ChinaSchool of Food Science and Engineering, Hainan University, Haikou 570228, PR ChinaCollege of Food Science and Engineering, Bohai University, Jinzhou 121013, PR ChinaCollege of Food Science and Engineering, Bohai University, Jinzhou 121013, PR ChinaSchool of Food Science and Engineering, Hainan University, Haikou 570228, PR ChinaSchool of Food Science and Engineering, Hainan University, Haikou 570228, PR ChinaSchool of Food Science and Engineering, Hainan University, Haikou 570228, PR China; Corresponding author at: Haikou City, Hainan Province, PR China.School of Food Science and Engineering, Hainan University, Haikou 570228, PR China; Corresponding author at: Haikou City, Hainan Province, PR China.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.http://www.sciencedirect.com/science/article/pii/S2590157525001087OvalbuminMolecular dockingElectronic tongueAlphafold2Saltiness/saltiness enhancing peptides |
| spellingShingle | Yaxin Cao Linyuezhi Yan Di Liu Qian Zhang Wenzhu Zhao Lin Yuan Yiding Yu Zhipeng Yu Identification of novel saltiness/saltiness enhancing peptides in egg proteins: Molecular docking, action mechanism and in vitro activity validation Food Chemistry: X Ovalbumin Molecular docking Electronic tongue Alphafold2 Saltiness/saltiness enhancing peptides |
| title | Identification of novel saltiness/saltiness enhancing peptides in egg proteins: Molecular docking, action mechanism and in vitro activity validation |
| title_full | Identification of novel saltiness/saltiness enhancing peptides in egg proteins: Molecular docking, action mechanism and in vitro activity validation |
| title_fullStr | Identification of novel saltiness/saltiness enhancing peptides in egg proteins: Molecular docking, action mechanism and in vitro activity validation |
| title_full_unstemmed | Identification of novel saltiness/saltiness enhancing peptides in egg proteins: Molecular docking, action mechanism and in vitro activity validation |
| title_short | Identification of novel saltiness/saltiness enhancing peptides in egg proteins: Molecular docking, action mechanism and in vitro activity validation |
| title_sort | identification of novel saltiness saltiness enhancing peptides in egg proteins molecular docking action mechanism and in vitro activity validation |
| topic | Ovalbumin Molecular docking Electronic tongue Alphafold2 Saltiness/saltiness enhancing peptides |
| url | http://www.sciencedirect.com/science/article/pii/S2590157525001087 |
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