Inhibitory effect and molecular mechanism on tyrosinase and browning of fresh-cut apple by longan shell tannins

Tyrosinase is a biological macromolecule closely related to browning of fruit and vegetables, melanin production, and tyrosinase inhibitors are usually used to prevent browning and pigmentation. In this study, longan shell tannins (LSTs) were screened as tyrosinase inhibitors and their structures were proved to be mixtures of procyanidins (condensed tannins) and ellagitannins (hydrolyzed tannins). Enzymatic experiments verified that LSTs were efficient inhibitors, and the IC50 values for monophenolase and bisphenolase were 176.04 +/- 10 and 59.94 +/- 5 mu g mL-1, respectively. Fluorescence detections and molecular docking revealed that the combination of LSTs to tyrosinase was mainly driven by hydrogen bonding, hydrophobic interaction, as well as van der Waals force, which changed the microenvironment of tyrosine and tryptophan residues as well as enzyme conformation. Circular dichroism and molecular dynamics simulation showed that LSTs affected secondary structures of tyrosinase, resulting in structural stretching and conformational modification of the enzyme. In addition, preservation studies demonstrated that LSTs owned the ability to delay the browning of fresh-cut apples by inhibiting phenolic metabolism, strengthening the antioxidant system, and reducing lipid peroxidation. This paper testified that LSTs are exteaordinary tyrosinase inhibitors, and offered a scientific foundation for the application of LSTs in food industry and medicine.