title: Digestive enzymes of two brachyuran and two anomuran land crabs from Christmas Island, Indian Ocean.
abstract: The digestive ability of four sympatric land crabs species (the gecarcinids, Gecarcoidea natalis and Discoplax celeste and the anomurans, Birgus latro and Coenobita perlatus) was examined by determining the activity of their digestive enzymes. The gecarcinids are detritivores that consume mainly leaf litter; the robber crab, B. latro, is an omnivore that preferentially consumes items high in lipid, carbohydrate and/or protein; C. perlatus is also an omnivore/detritivore. All species possess protease, lipase and amylase activity for hydrolysing ubiquitous protein, lipid and storage polysaccharides (glycogen and starch). Similarly all species possess enzymes such as N-acetyl-β-D-glucosaminidase, the cellulases, endo-β-1,4-glucanase and β-glucohydrolase and hemicellulases, lichenase and laminarinase for the respective hydrolysis of structural substrates chitin, cellulose and hemicelluloses, lichenan and laminarin. Except for the enzyme activities of C. perlatus, enzyme activity could not be correlated to dietary preference. Perhaps others factors such as olfactory and locomotor ability and metabolic status may determine the observed dietary preferences. The digestive fluid of C. perlatus possessed higher endo-β-1,4-glucanase, lichenase and laminarinase activities compared to that of the other species. Thus, C. perlatus may be efficient at digestion of cellulose and hemicellulose within plant material. Zymography indicated that the majority of protease, lipase, phosphatase, amylase, endo-β-1,4-glucanase, β-glucohydrolase and N-acetyl-β-D-glucosaminidase isozymes were common to all species, and hence were inherited from a common aquatic ancestor. Differences were observed for the phosphatase, lipase and endo-β-1,4-glucanase isozymes. These differences are discussed in relation to phylogeny and possible evolution to cope with the adoption of a terrestrial diet.
authors.affiliation: School of Life and Environmental Sciences, Deakin University, Pigdons Road, Waurn Ponds, VIC, 3217, Australia, stuart.linton@deakin.edu.au.
authors.forename: Stuart M
authors.initials: SM
authors.lastname: Linton
authors.forename: Reinhard
authors.initials: R
authors.lastname: Saborowski
authors.forename: Alicia J
authors.initials: AJ
authors.lastname: Shirley
authors.forename: Jake A
authors.initials: JA
authors.lastname: Penny
mesh_terms: D000222:Adaptation, Physiological / Q000502:physiology; D000818:Animals; D033381:Anomura / Q000201:enzymology* / Q000502:physiology; D003386:Brachyura / Q000201:enzymology* / Q000502:physiology; D004063:Digestion / Q000502:physiology; D004798:Enzymes / Q000502:physiology*; D019156:Indian Ocean; D008297:Male; D010802:Phylogeny
chemical_list: D004798:Enzymes