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Presence and properties of cellulase and hemicellulase enzymes of the gecarcinid land crabs Gecarcoidea natalis and Discoplax hirtipes.

Linton, Stuart and Greenaway, Peter 2004, Presence and properties of cellulase and hemicellulase enzymes of the gecarcinid land crabs Gecarcoidea natalis and Discoplax hirtipes., Journal of experimental biology, vol. 207, no. 23, pp. 4095-4104.

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Title Presence and properties of cellulase and hemicellulase enzymes of the gecarcinid land crabs Gecarcoidea natalis and Discoplax hirtipes.
Formatted title Presence and properties of cellulase and hemicellulase enzymes of the gecarcinid land crabs Gecarcoidea natalis and Discoplax hirtipes.
Author(s) Linton, StuartORCID iD for Linton, Stuart orcid.org/0000-0002-8292-7816
Greenaway, Peter
Journal name Journal of experimental biology
Volume number 207
Issue number 23
Start page 4095
End page 4104
Publisher Cambridge University Press
Place of publication Cambridge, England
Publication date 2004-11
ISSN 0022-0949
1477-9145
Keyword(s) land crab
Gecarcoidea natalis
Discoplax hirtipes
cellulase
endo-ß-1
4-glucanase
cellobiohydrolase
ß-1
4-glucosidase
laminarinase
xylanase
licheninase
fibre digestion
Summary Digestive juice from the herbivorous gecarcinid land crabs Gecarcoidea natalis and Discoplax hirtipes exhibited total cellulase activity and activities of two cellulase enzymes; endo-ß-1,4-glucanase and ß-1,4-glucosidase. These enzymes hydrolysed native cellulose to glucose. The digestive juice of both species also contained laminarinase, licheninase and xylanase, which hydrolysed laminarin, lichenin and xylan, respectively, to component sugars. The pH optima of ß-1,4-glucosidase, endo-ß-1,4-glucanase and total cellulase from G. natalis were 4–5.5, 5.5 and 5.5–7, respectively. In the digestive juice from D. hirtipes, the corresponding values were 4–7, 5.5–7 and 4–9, respectively. The pH of the digestive juice was 6.69±0.03 for G. natalis and 6.03±0.04 for D. hirtipes and it is likely that the cellulases operate near maximally in vivo. In G. natalis, total cellulase activity and endo-ß-1,4-glucanase activity were higher than in D. hirtipes, and the former species can thus hydrolyse cellulose more rapidly. ß-1,4-glucosidase from G. natalis was inhibited less by glucono-D-lactone (Ki=11.12 mmol l-1) than was the ß-1,4-glucosidase from D. hirtipes (Ki=4.53 mmol l-1). The greater resistance to inhibition by the ß-1,4-glucosidase from G. natalis may contribute to the efficiency of the cellulase system in vivo by counteracting the effects of product inhibition and possibly dietary tannins. The activity of ß-1,4-glucosidase in the digestive juice of D. hirtipes was higher than that of G. natalis.
Language eng
Field of Research 060604 Comparative Physiology
Socio Economic Objective 970106 Expanding Knowledge in the Biological Sciences
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2004, Cambridge University Press
Free to Read? Yes
Persistent URL http://hdl.handle.net/10536/DRO/DU:30002852

Document type: Journal Article
Collections: School of Biological and Chemical Sciences
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Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.