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Digestive enzyme activity of two stonefly species (Insecta, Plecoptera) and their feeding habits.
- Source :
-
Comparative biochemistry and physiology. Part A, Molecular & integrative physiology [Comp Biochem Physiol A Mol Integr Physiol] 2011 Nov; Vol. 160 (3), pp. 426-30. Date of Electronic Publication: 2011 Jul 26. - Publication Year :
- 2011
-
Abstract
- The digestive enzymes of two stoneflies species, Hemimelaena flaviventris and Isoperla morenica, were studied for the first time. These species are temporary water inhabitants and exhibit great feeding plasticity. Although they are traditionally referred to as predators, a previous study revealed that H. flaviventris incorporates some diatoms into its diet in addition to feeding usually on several prey, and I. morenica (in that study under the name of I. curtata) only feeds on animals occasionally. The enzymatic activities of digestive amylase, lipase, protease, trypsin and chymotrypsin were determined for each species at the same developmental stage. The results show that H. flaviventris has a greater digestive enzymatic pool and higher relative and absolute protease, lipase and trypsin activities than I. morenica. The latter has a relative higher amylase activity. As higher amylase activity is typical of phytophagous species and higher protease activity typical of carnivorous species; these results reveal that H. flaviventris is a more efficient zoophagous species than I. morenica. The ecological implications of these findings, including the higher secondary production of H. flaviventris in its habitat, are discussed.<br /> (Copyright © 2011 Elsevier Inc. All rights reserved.)
- Subjects :
- Amylases physiology
Animals
Chymotrypsin metabolism
Chymotrypsin physiology
Endopeptidases metabolism
Endopeptidases physiology
Feeding Behavior physiology
Lipase physiology
Motor Activity
Peptide Hydrolases physiology
Trypsin metabolism
Trypsin physiology
Amylases metabolism
Digestive System enzymology
Insecta enzymology
Lipase metabolism
Peptide Hydrolases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1531-4332
- Volume :
- 160
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Comparative biochemistry and physiology. Part A, Molecular & integrative physiology
- Publication Type :
- Academic Journal
- Accession number :
- 21820525
- Full Text :
- https://doi.org/10.1016/j.cbpa.2011.07.014