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α-Amylase isoforms of Cerambyx cerdo larvae from the wild (ML and SL) and reared in the laboratory (ADL) were compared. Three amylase isoforms were presented in the SL and ML extracts while two isoforms were presented in the ADL according to zymogram after isoelectric focusing (IEF). All C. cerdo amylase isoforms were acidic proteins (pI < 3.5). Seven amylase isoforms (ACC 1-7) from the midgut of C. cerdo larvae were found in the ML midgut extract, six in the SL extract, and four in the ADL extract according to native PAGE zymogram. The ADL amylase had the highest activity. All crude midgut extracts of C. cerdo larvae were fractionated on a Superose 12 HR column. The molecular mass of the ACC was estimated to be 34 kDa. .

The pH along the midgut of M. funereus larvae had different values, being acidic in the anterior section and basic in the middle and posterior sections. Elastase- and chymotrypsin-like activities were highest in the middle, low in the anterior, and negligible in the posterior section of the midgut. Trypsin-like activities were detected along the whole midgut, with more than 90% of activity in the anterior section. The level of elastase- and chymotrypsin-like activity was very low compared to trypsin-like activity. In the anterior section of the midgut, two isoforms of trypsin-like enzymes were found, both being basic and almost completely inhibited by benzamidine.