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Sahar Delkash-Roudsari,Arash Zibaee,Mohammad Reza Abbci-Mozhdehi 한국응용곤충학회 2014 Journal of Asia-Pacific Entomology Vol.17 No.3
Digestive proteolytic activity in larvae and adults of Bactrocera oleae was studied using specific substrates andinhibitors. The optimal pH for general proteolytic activity was 4 and 10 for soluble and membrane-bound fractionsof larvae, and 9 for the soluble fraction of adults. The highest activities of general proteases were revealed attemperatures of 25 °C and 45 °C for both the soluble andmembrane-bound fractions of larvae as well as the solublefraction of adults. Determination of the specific protease activities demonstrated the presence of serine and cysteineproteases in addition to two exopeptidases in the larvae and adults. However, trypsin-like protease, chymotrypsinlikeprotease, and two exopeptidases of larvae, and chymotrypsin-like protease as well as cathepsin L of adults hadno activity in the soluble fraction. The presence of specific proteases was verified by using specific inhibitors such asPMSF, TLCK, TPCK, E-64, EDTA, phenanthroline, and DTT. Finally, feeding of B. oleae larvae on different olive varietiesrevealed the highest trypsin-like protease, chymotrypsin-like protease, elastase, cathepsin B, cathepsin L, andcathepsin D on Amigdalifolia, Coratina, Baladi, Mari, Conservalia, Baladi, and Arbequina, respectively. These resultsshowed digestive proteolytic activities in B. oleae for the first time, and could be the basic knowledge required forfinding a control procedure to decrease the damage of this destructive pest around the world.
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