4.5 Article

Galactolipase, phospholipase and triacylglycerol lipase activities in the midgut of six species of lepidopteran larvae feeding on different lipid diets

Journal

JOURNAL OF INSECT PHYSIOLOGY
Volume 57, Issue 9, Pages 1232-1239

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jinsphys.2011.05.012

Keywords

Galactolipid; Phospholipid; Folivore; Granivore; Carnivore; Keratinophage; Phytophagy

Funding

  1. FRST [C06X0804]
  2. Agence Nationale de la Recherche (France) [ANR-09-CP2D-06-01]
  3. ISAT (Royal Society of New Zealand)
  4. CNRS
  5. New Zealand Ministry of Business, Innovation & Employment (MBIE) [C06X0804] Funding Source: New Zealand Ministry of Business, Innovation & Employment (MBIE)

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Galactolipase, phospholipase and triacylglycerol lipase activities were measured from the midgut of six species of lepidopteran larvae, two folivores, Epiphyas postvittana (Tortricidae) and Helicoverpa armigera (Noctuidae); two granivores. Plodia interpunctella (Pyralidae) and Ephestia kuehniella (Pyrallidae); a presumptive carnivore, Galleria mellonella (Pyralidae); and a keratinophage, Tineola bisselliella (Tineidae). Galactolipase has not been previously reported in insects. Galactolipase and phospholipase activities were high in the folivores and triacylglycerol lipase activity was low, matching the high galactolipid content of leaves. Conversely, galactolipase and phospholipase activities were low, but not absent, and triacylglycerol lipase activity high in the four other non-folivorous species, matching the high acylglycerol content of their diets. These data suggest the utility of reclassification, for evolutionary studies, of phytophagous lepidoptera into two feeding classes; folivore and granivore, the latter having similarity to the fungivore line of feeders in terms of its lipase activities and ability to retrieve essential polyunsaturated long chain fatty acids from their diets. All the digestive lipases have alkaline pH optima for activity, matching the pH of the lepidopteran midgut and their amino acid content show modifications likely to stabilize the proteins in that environment. (C) 2011 Elsevier Ltd. All rights reserved.

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