Characterization of the activity of tyrosinase on betanidin

摘要

Betalains are an important class of water-soluble pigments, with radical scavenging capacity, which is characteristic of the order Caryophyllales. The structural unit of the violet betacyanins, betanidin is reported as a substrate for the enzyme tyrosinase (EC 1.14.18.1), which plays a key role in the betalains biosynthetic scheme. The compound was identified in Lampranthus productus violet flowers, from which it was extracted and purified. The tyrosinase-mediated oxidation of betanidin was characterized in depth and followed by high-performance liquid chromatography and spectrophotometry. The addition of ascorbic acid reversed the reaction product, betanidin-quinone, to the original pigment. Kinetic analysis revealed a Km = 0.66 mM. Betanidin degradation kinetics was also studied in the absence of the enzyme and demonstrated that pH values over 6.0 and high ionic strength reduce the pigment stability.