On the photoinactivation of alcohol oxidase from alkane-grown Candida tropicalis

The process of photoinactivation of alcohol oxidase is insensitive to oxygen and to temperature in the range 0–25°C. The process is, however, wavelength dependent. Irradiation and inactivation do not cause any significant change to the visible absorption spectrum. Reaction of the enzyme with sodium sulfite or photoreduction in the presence of EDTA and either 5′-deazaflavin or lumiflavin 3-acetate under anaerobic conditions causes extensive bleaching of the visible spectrum of the enzyme and also protects it from photoinactivation. The presence of substrate under anaerobic conditions also provides very effective protection, but in this case there is no detectable change in the visible spectrum of the enzyme associated with the increase in stability to light.