It was found that kojic acid, which is used in cosmetics for its excellent whitening effect, inhibits catecholase activity of tyrosinase in a non-classical manner. A decrease in the initial velocity to a steady-state inhibited velocity can be observed over a few minutes. This time-dependence, which is unaltered by prior incubation of the enzyme with the inhibitor, is consistent with a first-order transition. The kinetic data obtained correspond to those for a postulated mechanism that involves the rapid formation of an enzyme inhibitor complex that subsequently undergoes a relatively slow reversible reaction. Kinetic parameters characterizing this type of inhibition were evaluated by means of nonlinear regression of product accumulation curves.
Quinoa was the traditional grain crop used by the prehispanic civilizations in America. Grains are white, black, yellow, and red-violet and plants are cultivated in vast areas of Peru, Bolivia and Ecuador. The recent description of the betacyanin pigment betanin in red-violet varieties is here further analyzed detecting the presence of amaranthin not previously identified in quinoa grains. Yellow-orange grains are characterized for the first time and up to four different betaxanthins are found to be responsible for this coloration. The native fluorescence of the identified betaxanthins makes the surface of the yellow quinoa grains glow with green fluorescent light. The presence of betalains is correlated with high antioxidant and free radical scavenging activities measured under the FRAP, ABTS and ORAC assays in grain extracts of 29 Peruvian varieties. TEAC equivalence is as high as 44.1 and 47.4mmol Trolox/kg for the yellow and red-violet varieties analyzed respectively.
A kinetic study of the inhibition of mushroom tyrosinase by 4-substituted benzaldehydes showed that these compounds behave as classical competitive inhibitors, inhibiting the oxidation of L-3,4-dihydroxyphenylalanine (L-DOPA) by mushroom tyrosinase (o-diphenolase activity). The kinetic parameter (K(I)) characterizing this inhibition was evaluated for all of the seven compounds assayed. Cuminaldehyde showed the most potent inhibitory activity (K(I) = 9 microM). It also inhibited the oxidation of L-tyrosine by mushroom tyrosinase (o-monophenolase activity) in a competitive manner. The corresponding kinetic parameter for this inhibition was evaluated (K(I) = 0.12 mM).
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