Properties and compartmentalization of digestive carbohydrases and proteases in Scaptotrigona bipunctata (Apidae: Meliponinae) larvaeT.T.S. Schumaker, P.T. Cristofoletti and W.R. Terra
Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, CP 20780, 01498 São Paulo, Brazil
Abstract - Aminopeptidase (pH optimum, pHo, 7.5; enzyme relative molecular weights, Mr values: 1, 110 000; 2, 190 000; 3, 300 000), amylase (pHo 5.5, Mr values: 1, 21 000; 2, 68 000); cellobiase (pHo 5.5) and maltase (pHo 5.0, Mr values: 1, 75 000; 2, 110 000; 3, 200 000) are found in the anterior (60-80%) and posterior (20-35%) midgut contents, with minor amounts occurring in midgut cells (2-5%). Trypsin (pHo 7.0, Mr 38 000) occurs mainly in the posterior (62%) rather than in the anterior (37%) midgut contents. Maltase 1 is more active on sucrose than on maltose, the reverse being true for the other maltases. A cysteine-proteinase (pHo 5.6, Mr 79 000) was found in major amounts in the pollen grains ingested by the larvae. The results suggest that, except for a cysteine-proteinase derived from ingested pollen, all digestive enzymes originate in the midgut tissue and are most active in the luminal contents. Evidence is presented supporting the hypothesis that enzymes and nutrients diffusing through the peritrophic membrane are translocated forward by a countercurrent flux. The absence of a midgut differentiation of midgut luminal pH in S bipunctata larvae is though to be derived from putative Hymenopteran ancestors.
Key words: Scaptotrigona bipunctata / digestion / enzyme activity / Meliponinae