S. Day, ARYL MONOOXYGENASE - A DETOXIFYING ENZYME FROM CANDIDA-PULCHERRIMA MCMY2, Indian Journal of Biochemistry & Biophysics, 33(6), 1996, pp. 523-526
Characterization of partially purified aryl monooxygenase (1:14:14:1)
from Candida pulcherrima MCMY2 was achieved using standard purificatio
n protocol. The molecular weight of the enzyme was 110 kDa and contain
ed 3 subunits with pI 5.7, 7.4 and 7.6. The activity seemed to be rela
ted with pulcherrimin. The optimum pH and temperature for enzyme activ
ity were 6.8 and 30 degrees C respectively. Activity was not substrate
specific and Fe3+ FAD and NADH(+) enhanced the activity substantially
.