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Regional distribution and substrate specificity of digestive enzymes involved in terminal digestion in Musca domestica hind‐midguts
Author(s) -
Jordāo Beatriz P.,
Terra Walter R.
Publication year - 1991
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.940170209
Subject(s) - midgut , maltotriose , maltose , biology , biochemistry , dipeptidase , musca , digestion (alchemy) , amylase , starch , enzyme , muscidae , centrifugation , aminopeptidase , chromatography , chemistry , larva , amino acid , leucine , botany , ecology
One membrane‐bound α‐glucosidase and two soluble α‐glucosidases were isolated from homogenates of the hind‐midgut, the main digestive region in Musca domestica larvae. The membrane‐bound α‐glucosidase and the low‐Mr soluble α‐glucosidase hydrolyze maltopentaose better than maltose, maltotriose, and maltotetraose, the reverse being true for the high‐Mr soluble α‐glucosidase. A membrane‐bound glucoamylase previously described in Musca domestica midgut was shown by gradient centrifugation and dialysis against EDTA to result from the combined action of an amylase and an α‐glucosidase. The determination of amylase, α‐glucosidases, soluble and membrane‐bound carboxypeptidase A, membrane‐bound aminopeptidase and dipeptidase along the tissue and luminal contents of the hind‐midgut is described. The data support a proposal concerned with how starch and protein are digested in Musca domestica larval hind‐midguts and where and how midgut glycosidases and peptidases are secreted.