Abstract
In this paper, the inhibitory effects of 4-chlorocinnamaldehyde on mushroom tyrosinase were investigated. The results showed that 4-chlorocinnamaldehyde had a significant inhibitory effect on monophenolase and diphenolase in tyrosinase. 4-Chlorocinnamaldehyde could obviously prolong the lag phase of monophenolase and it decreased the steady-state rate of both monophenolase and diphenolase. The IC50 values were found to be 0.07 and 0.3 mM for monophenolase and diphenolase, respectively. The kinetic studies showed that the inhibitory mechanism of mushroom tyrosinase by 4-chlorocinnamaldehyde was the reversible competitive inhibition. The inhibition constant (K I) was measured to be 0.17 mM. The experimental research demonstrated that 4-chlorocinnamaldehyde was an effective tyrosinase inhibitor and the research results may offer the theoretical basis for designing and synthesizing safer and more efficient tyrosinase inhibitors in future.
Published Version
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