On-line immobilized trypsin microreactor for evaluating inhibitory activity of phenolic acids by capillary electrophoresis and molecular docking
Autor: | Hao Zhang, Zhao-Yu Wu, Yin-Zhen Wang, Feng-Qing Yang, De-qiang Li, Dong-Dong Zhou |
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Rok vydání: | 2020 |
Předmět: |
Coumaric Acids
01 natural sciences Benzamidine Analytical Chemistry Catalysis Ferulic acid chemistry.chemical_compound Bioreactors Caffeic Acids 0404 agricultural biotechnology Capillary electrophoresis Gallic Acid Hydroxybenzoates medicine Caffeic acid Trypsin Gallic acid IC50 Binding Sites Chromatography Chemistry 010401 analytical chemistry Electrophoresis Capillary 04 agricultural and veterinary sciences General Medicine Enzymes Immobilized 040401 food science 0104 chemical sciences Molecular Docking Simulation Trypsin Inhibitors Food Science medicine.drug |
Zdroj: | Food Chemistry. 310:125823 |
ISSN: | 0308-8146 |
Popis: | Phenolic acids, which are important aromatic secondary metabolites, are widely distributed in plant foods. In this study, a simple, economical and fast on-line immobilized trypsin microreactor was developed for evaluating the inhibitory activity of phenolic acids by capillary electrophoresis. The Michaelis-Menten constant (Km) of immobilized trypsin was determined as 0.99 mM, and the half-maximal inhibitory concentration (IC50) and inhibition constant (Ki) of benzamidine were measured as 3.39 and 1.68 mM, respectively. Then, the developed strategy was applied to investigate the inhibitory activity of six phenolic acids on trypsin. The results showed that gallic acid, caffeic acid and ferulic acid had high inhibitory activity at concentration of 150 μM. Molecular docking results illustrated that gallic acid, caffeic acid and ferulic acid can interact indirectly with the catalytic and substrate-binding sites of trypsin. The developed strategy is an effective tool for evaluating inhibitory activity of phenolic acids on trypsin. |
Databáze: | OpenAIRE |
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