Intestinal Proteases of Moneilema Armatum (Coleoptera: Cerambycidae) Fed With Opuntia Cladodes

Abstract

This work provides an overview of proteolytic activity in the intestine of Moneilema armatum (Coleoptera: Cerambycidae) adults and inhibition of such enzymes by proteins obtained from the cladodes of Opuntia ficus-indica. Active intestinal proteases were detected at a neutral and slightly alkaline pH through zymography and spectrophotometric assays using synthetic substrates. These enzymes were susceptible to a specific serine protease inhibitor (PMSF). It was also demonstrated that trypsin-, chymotrypsin-, and elastase-like activities were present. Although the cladodes of O. ficus-indica possess endogenous inhibitors of serine proteases, it appears that not all proteases of M. armatum were affected, particularly those with elastase-like activity. The results indicated that M. armatum exhibits a variety of serine protease activities, and some of these proteolytic activities were insensitive to endogenous O. ficus-indica protease inhibitors.