Citation

Garcia-Jimenez A, Teruel-Puche JA, García-Ruiz PA, Saura-Sanmartin A, Berna J, Rodriguez-Lopez JN, García-Cánovas F. Int. J. Biol. Macromol. 2018; 107(Pt B): 2650-2659.

Copyright

(Copyright © 2018, Elsevier Publishing)

DOI

10.1016/j.ijbiomac.2017.10.151

PMID

29080822

Abstract

Different mechanisms for inhibiting tyrosinase can be designed to avoid postharvest quality losses of fruits and vegetables. The action of tyrosinase on caffeic acid and its n-nonyl ester (n-nonyl caffeate) was characterized kinetically in this work. The results lead us to propose that both compounds are suicide substrates of tyrosinase, for which we establish the catalytic and inactivation efficiencies. The ester is more potent as inactivator than the caffeic acid and the number of turnovers made by one molecule of the enzyme before its inactivation (r) is lower for the ester. We proposed that the anti-browning and antibacterial properties may be due to suicide inactivation processes.

Language: en

Keywords

Kinetics; Catalysis; Tyrosinase; Substrate Specificity; Levodopa; Tyrosine; Molecular Docking Simulation; Esters; Monophenol Monooxygenase; Quinones; Carbon-13 Magnetic Resonance Spectroscopy; Caffeic acid; Caffeic Acids; n-Nonyl caffeate