Evaluation of inhibitory effects of some novel phenolic derivatives on the mushroom tyrosinase activity: Insights from spectroscopic analyses, molecular docking and in vitro assays. (1st September 2022)

• Record Type: Journal Article
• Authors: Mahdavi, Atiyeh; Mohammadsadeghi, Nahid; Mohammadi, Fakhrossadat; Saadati, Fariba; Nikfard, Somayeh
• Is Part Of: Food chemistry. Volume 387(2022)
• Publication Date: 2022-09-01
• Subjects: Phenolic compounds -- Tyrosinase inhibitor -- Inhibition mechanism -- Mixed inhibition -- Fluorescence quenching -- Molecular docking; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2022.132938
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Developing new tyrosinase inhibitors is very important in food and agriculture. New derivatives were synthesized from phenolic compounds used in food industry. They had potent inhibitory effects on mushroom tyrosinase in low concentrations. They might be as anti-browning candidates for food and agriculture industries. The compound, 4-(4-Hydroxyphenyl)butan-2-one (1b) was the most potent inhibitor. Abstract: Tyrosinase plays determinant role in enzymatic browning of vegetables and fresh-cut fruits. Development of new tyrosinase inhibitors is of great concern in food and agriculture. To discover new inhibitors, novel phenolic derivatives were synthesized and their inhibitory effects were investigated on activity of mushroom tyrosinase. All compounds showed potent inhibitory activities in their low concentrations and compound 4-(4-hydroxyphenyl)butan-2-one (1b) was found to be the most potent inhibitor (73.75% inhibition, IC50 value 5.6 μmol L −1 ). This ligand inhibited enzyme activity in a mixed pattern and kinetic parameters were also determined. In vitro assays revealed that this compound has not cytotoxicity/hemolytic effects and can be considered as safe for further investigations. Analysis of fluorescence spectra showed that all ligands quenched enzyme intrinsic fluorescence. The quenching mode and important binding parameters were also calculated. Enzyme-ligands interactions were also theoretically analyzed by molecular docking and results showed that the ligands interact with structurally/functionally critical residues.