Abstract
This paper reports the inhibiting action of riboflavin in the light condition on the activity of tyrosinase, extracted from the potato tubers. Both riboflavin and its photolized products, i. e., lumiflavin and lumichrome, inhibit the tyrosinase activity in the light and each inhibiting effect is the following descending order : lumiflavin>riboflavin>lumichrome. The tyrosinase activity was inhibited by both Na-diethyldithiocarbamate and KCN, but not by Naethylenediaminetetraacetate, among the chelating reagents used in this experiment. The addition of Cu^<2+> reversed considerably the inhibition of tyrosinase activity by Na-diethyldithiocarbamate and KCN, but not by riboflavin.
