Pheromone hydrolysis by cuticular and interior esterases of the antennae, legs, and wings of the cabbage looper moth,Trichoplusia ni (Hübner).

Examination was made of the hydrolytic activities of esterases obtained from the antennae, legs, and wings of 3-day-old cabbage looper moths,Trichoplusia ni (Hübner), by elution and by homogenation of those appendages. Pheromone hydrolysis in 1-min assays was monitored by use of tritium-labeled (Z)-7-dodecen-1-ol acetate and thin-layer chromatography to separate the reaction products. Listed according to the activities of the esterases obtained by homogenation, the organs were antennae > legs > wings. In contrast, the order according to the activities of the eluted esterases was wings > legs > antennae. Also, the eluted enzymes were less active than the esterases obtained by homogenization. The relatively high pheromone-hydrolyzing activity present in homogenized antennae suggests that the esterases originated inside the antennae and lends support to the hypothesis proposed in earlier investigations that pheromone-inactivating enzymes may play an important role in the olfactory process, possibly by clearing pheromone from the vicinity of the olfactory receptors. The esterases detected on the cuticle, on the other hand, may function by preventing surface accumulation of pheromone. The higher measured esterase activity in homogenates of prothoracic legs than of mesothoracic or metathoracic legs suggests that the prothoracic legs, which are used to clean the antennae of debris, may function by removing and degrading pheromone from the surface of antennae.