Digestion in adult females of the leaf-footed bug Leptoglossus zonatus (Hemiptera: Coreidae) with emphasis on the glycoside hydrolases α-amylase, α-galactosidase, and α-glucosidase.
The leaffooted bug, Leptoglossus zonatus (Hemiptera: Coreidae) is an emerging pest of several crops around the World and up to now very little is known of its digestive system. In this article, glycoside hydrolase (carbohydrase) activities in the adult midgut cells and in the luminal contents of L. zonatus adult females were studied. The results showed the distribution of digestive carbohydrases in adults of this heteropteran species in the different intestinal compartments. Determination of the spatial distribution of α-glucosidase activity in L. zonatus midgut showed only one major molecular form, which was not equally distributed between soluble and membrane-bound isoforms, being more abundant as a membrane-bound enzyme. The majority of digestive carbohydrases were found in the soluble fractions. Activities against starch, maltose and the synthetic substrate NPαGlu were found to show the highest levels of activity, followed by enzymes active against galactosyl oligosaccharides. Based on ion-exchange chromatography elution profiles and banding patterns in mildly denaturing electrophoresis, both midgut α-amylases and α-galactosidases showed at least two isoforms. The data suggested that the majority of carbohydrases involved in initial digestion were present in the midgut lumen, whereas final digestion of starch and of galactosyl oligosaccharides takes place partially within the lumen and partially at the cell surface. The complex of carbohydrases here described was qualitatively appropriate for the digestion of free oligosaccharides and oligomaltodextrins released by α-amylases acting on maize seed starch granules.
Departamento de Microbiologia e Parasitologia, Centro de Ciências Biológicas, Universidade Federal de Santa Catarina, Florianópolis, Santa Catarina, Brazil.
Ariane A
AA
Rocha
Carlos J C
CJ
Pinto
Richard I
RI
Samuels
Daniel
D
Alexandre
Carlos P
CP
Silva
D000824:Animal Nutritional Physiological Phenomena; D000818:Animals; D002852:Chromatography, Ion Exchange; D004063:Digestion / Q000502:physiology*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D041981:Gastrointestinal Tract / Q000502:physiology; D005786:Gene Expression Regulation; D006026:Glycoside Hydrolases / Q000235:genetics / Q000378:metabolism*; D020062:Heteroptera / Q000201:enzymology / Q000235:genetics / Q000502:physiology*; D019476:Insect Proteins / Q000235:genetics* / Q000378:metabolism; D013213:Starch / Q000378:metabolism*; D000516:alpha-Amylases / Q000235:genetics / Q000378:metabolism; D000519:alpha-Galactosidase / Q000235:genetics / Q000378:metabolism; D000520:alpha-Glucosidases / Q000235:genetics / Q000378:metabolism
D019476:Insect Proteins; D013213:Starch; D006026:Glycoside Hydrolases; D000516:alpha-Amylases; D000520:alpha-Glucosidases; D000519:alpha-Galactosidase
Plant-insect interaction; digestive enzymes; insect digestion; α-amylase; α-galactosidase; α-glucosidase