Separation, identification, and molecular docking of tyrosinase inhibitory peptides from the hydrolysates of defatted walnut (Juglans regia L.) meal
| Autor: | Zi-Chun Wang, Jia-xin Chen, Yan-bing Wang, Yan-xia Feng, Di-Feng Ren, Jun Lu, Hai-rong Li |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
chemistry.chemical_classification
Binding Sites Chromatography Monophenol Monooxygenase Plant Extracts Hydrolysis Tyrosinase Juglans Peptide General Medicine Hydrolysate Analytical Chemistry Molecular Docking Simulation Kinetics Ultrafiltration (renal) chemistry Sephadex Nuts Digestion Tyrosine Peptides Food Science |
| Zdroj: | Food Chemistry. 353:129471 |
| ISSN: | 0308-8146 |
| Popis: | Defatted walnut meal protein was hydrolyzed using alcalase to yield tyrosinase inhibitory peptides. After separation by ultrafiltration and Sephadex G-25, the fraction with the highest tyrosinase inhibitory activity was identified using liquid chromatography-tandem mass spectrometry and 606 peptides were obtained. Then, molecular docking was used to screen for tyrosinase inhibitory peptides and to clarify the theoretical interaction mechanism between the peptides and tyrosinase. A peptide with the sequence Phe-Pro-Tyr (FPY, MW: 425.2 Da) was identified and the synthesized peptide inhibited tyrosine monophenolase and diphenolase with IC50 values of 1.11 ± 0.05 and 3.22 ± 0.09 mM, respectively. The inhibition of tyrosinase by FPY was competitive and reversible. Good stability of FPY toward digestion was observed in an in vitro gastrointestinal digestion simulation experiment. These results indicated that FPY can be used as a potential tyrosinase inhibitor in the food, medicine, and cosmetics industries. |
| Databáze: | OpenAIRE |
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