Substrate specificity of membrane-bound alcohol oxidase from the tobacco hornworm moth (Manduca sexta) female pheromone glands

A putative alcohol oxidase (AO) from abdominal tips (ATs) of Manduca sexta virgin females was studied in a biphasic system hexane/aqueous phosphate buffer. The pH optimum closest to neutral range (6.8) and the temperature optimum closest to room temperature (25 ± 3 °C) were measured for the highest AO activity. AOs that are in intact membranes have long lifespans and may oxidize repeatedly. A high selectivity for primary alcohols of benzylic, saturated, and allylic type was observed. Neither the secondary alcohols nor the primary alcohols with bulky alkyl groups on C2-carbon are oxidized. This pronounced substrate specificity can be used for specific oxidation of alcohols in mixtures.