Yi-Hsin Liu's research while affiliated with Hungkuang University and other places

The chemical composition and functional activities of cold-pressed and water distilled peel essential oils of Citrus paradisi ( C. paradisi ) and Citrus grandis (L.) Osbeck ( C. grandis ) were investigated in present study. Yields of cold-pressed oils were much higher than those of distilled oils. Limonene was the primary ingredient of essential oils of C. paradisi (cold 92.83%; distilled 96.06%) and C. grandis (cold 32.63%; distilled 55.74%). In addition, C. grandis oils obtained were rich in oxygenated or nitrogenated compounds which may be involved in reducing cardiovascular diseases or enhancing sleep effectiveness. The order of free radical scavenging activities of 4 citrus oils was distilled C. paradisi oil > cold-pressed C. paradisi oil > distilled C. grandis oil > cold-pressed C. grandis oil. Cold-pressed C. grandis oil exhibited the lowest activity in all antioxidative assays. The order of antimicrobial activities of 4 citrus oils was distilled C. grandis oil, cold-pressed C. paradisi oil > distilled C. paradisi oil > cold-pressed C. paradisi oil. Surprisingly, distilled C. grandis oil exhibited better antimicrobial activities than distilled C. paradisi oil, especially against Escherichia coli and Salmonella enterica subsp. The results also indicated that the antimicrobial activities of essential oils may not relate to their antioxidative activities.

The native amino acid ergothioneine, a thiourea derivative of histidine, inhibits mushroom tyrosinase activity in a dose-dependent manner, with an IC(50) value of 1.025 mg/ml (4.47 mM). By contrast, histidine exhibited no inhibitory effect on mushroom tyrosinase activity. We characterized ergothioneine as a noncompetitive tyrosinase inhibitor using a Lineweaver-Burk plot of experimental kinetic data. The IC(50) value for ergothioneine scavenging of 2,2-diphenyl-1-picrylhydrazyl was 6.110 ± 0.305 mg/ml, much higher than the IC(50) for inhibition of tyrosinase activity which indicating ergothioneine on tyrosinase shows a weak correlation to its antioxidative activity. The results demonstrated that ergothioneine has a potent inhibition effect on tyrosinase enzyme activity, resulting from the presence of the sulfur substituted imidazole ring in ergothioneine.