title: Morphology and preliminary enzyme characterization of the salivary glands from the predatory bug Podisus nigrispinus (Heteroptera: Pentatomidae).
abstract: Podisus nigrispinus (Dallas) is a common predator in agricultural and natural systems in Neotropical America. Its feeding strategy involves extra-oral digestion and to better understand this process its salivary glands were extracted and subjected to morphological and preliminary enzyme characterization. The salivary glands of P. nigrispinus are formed by a pair of main and accessory gland complexes. The main salivary glands are further divided into an anterior and a posterior lobe. The compartmentalization of the salivary gland complex is likely to be important for the production, activation and release of the digestive enzymes used in the extra-oral digestion of prey items. Proteases and lipase, important digestive enzymes involved in zoophagy, were detected in the salivary glands of P. nigrispinus. The prevailing trypsin-like protease activity was characterized by using the serine-protease substrate N-alpha-benzoyl-L-Arg-p-nitroanilidine (L-BApNA) and the trypsin inhibitors tosyl-L-lysine chloromethyl ketone (TLCK) and benzamidine. The KM value obtained for trypsin-like activity was 1.57 mm and the different peaks of optimum pH and temperature activity suggest the presence of multiple forms of this enzyme in P. nigrispinus. Detection of amylase activity in the salivary glands of this predator suggests its ability to digest starch and obtain nutrients from plants, which may have adaptative value under prey scarcity.
authors.affiliation: Departamento de Biologia Animal, Universidade Federal de Viçosa, Viçosa, MG 36571-000, Brazil.
authors.forename: J A
authors.initials: JA
authors.lastname: Oliveira
authors.forename: M G A
authors.initials: MG
authors.lastname: Oliveira
authors.forename: R N C
authors.initials: RN
authors.lastname: Guedes
authors.forename: M J
authors.initials: MJ
authors.lastname: Soares
mesh_terms: D000681:Amylases / Q000032:analysis / Q000378:metabolism; D000818:Animals; D001550:Benzamidines / Q000494:pharmacology; D001586:Benzoylarginine Nitroanilide / Q000378:metabolism; D004063:Digestion / Q000502:physiology; D005260:Female; D020062:Heteroptera / Q000201:enzymology* / Q000502:physiology / Q000648:ultrastructure*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008049:Lipase / Q000032:analysis / Q000378:metabolism; D008297:Male; D008855:Microscopy, Electron, Scanning / Q000662:veterinary; D012469:Salivary Glands / Q000201:enzymology / Q000648:ultrastructure; D012697:Serine Endopeptidases / Q000032:analysis / Q000187:drug effects / Q000378:metabolism; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology; D013696:Temperature; D014107:Tosyllysine Chloromethyl Ketone / Q000494:pharmacology
chemical_list: D001550:Benzamidines; D015842:Serine Proteinase Inhibitors; D014107:Tosyllysine Chloromethyl Ketone; D001586:Benzoylarginine Nitroanilide; D008049:Lipase; D000681:Amylases; D012697:Serine Endopeptidases; C032157:benzamidine