| Autor: |
Jie Zhao, Shuaiqian Wang, Diandian Jiang, Yan Lu, Yu Chen, Yong Tang, Jie Tang, Zhenju Jiang, Hongbin Lin, Wei Dong |
| Jazyk: |
angličtina |
| Rok vydání: |
2023 |
| Předmět: |
|
| Zdroj: |
Food Chemistry: X, Vol 20, Iss , Pp 100986- (2023) |
| Druh dokumentu: |
article |
| ISSN: |
2590-1575 |
| DOI: |
10.1016/j.fochx.2023.100986 |
| Popis: |
This work systematically investigated the dose–response interaction between hydroxy-α-sanshool (α-SOH) and pork myofibrillar proteins (MPs) via spectroscopy, molecular docking, and molecular dynamics simulation methods. Results showed that MPs bound with low α-SOH can enhance the surface hydrophobicity and particle size of MPs, whereas high concentrations were exactly the opposite. The main interaction force in α-SOH/MPs complex changed from hydrophobic to hydrogen bonding with increased α-SOH. α-SOH causes tryptophan quenching and bring about a red shift at low concentration, as well as to promote α-helix conversion into β-sheet in MPs. Simultaneously, molecular docking and dynamics simulations verified that hydrogen bonding and hydrophobic forces were the main contributors to α-SOH/MPs complex, indicating that the binding of α-SOH with MPs proceeded spontaneously with high intensity, in which TYR286 contributed the most significant energy. Therefore, revealing the binding mechanism of α-SOH and MPs can contribute to the deep processing of numbing meat products. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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