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Updated: Aug 18, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
Aryl monooxygenase: a detoxifying enzyme from Candida pulcherrima MCMY2
1Division of Microbial Sciences, Agharkar Research Institute, Pune, India.
Abstract:
Characterization of partially purified aryl monooxygenase (1:14:14:1) from Candida pulcherrima MCMY2 was achieved using standard purification protocol. The molecular weight of the enzyme was 110 kDa and contained 3 subunits with pI 5.7, 7.4 and 7.6. The activity seemed to be related with pulcherrimin. The optimum pH and temperature for enzyme activity were 6.8 and 30 degrees C respectively. Activity was not substrate specific and Fe3+ FAD and NADH+ enhanced the activity substantially.
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