Openly accessible

The last piece in the cellulase puzzle : the characterisation of β-glucosidase from the herbivorous gecarcinid land crab Gecarcoidea natalis

Allardyce, Benjamin J., Linton, Stuart M. and Saborowski, Reinhard 2010, The last piece in the cellulase puzzle : the characterisation of β-glucosidase from the herbivorous gecarcinid land crab Gecarcoidea natalis, Journal of experimental biology, vol. 213, no. 17, pp. 2950-2957.

Attached Files
Name Description MIMEType Size Downloads
linton-lastpiece-2010.pdf Published version application/pdf 687.74KB 18

Title The last piece in the cellulase puzzle : the characterisation of β-glucosidase from the herbivorous gecarcinid land crab Gecarcoidea natalis
Formatted title The last piece in the cellulase puzzle: the characterisation of β-glucosidase from the herbivorous gecarcinid land crab Gecarcoidea natalis
Author(s) Allardyce, Benjamin J.
Linton, Stuart M.
Saborowski, Reinhard
Journal name Journal of experimental biology
Volume number 213
Issue number 17
Start page 2950
End page 2957
Total pages 8
Publisher Company of Biologists Ltd.
Place of publication Cambridge, England
Publication date 2010-09
ISSN 0022-0949
1477-9145
Keyword(s) crustacea
Gecarcoidea natalis
digestion
cellulose
glucohydrolase
Summary A 160 kDa enzyme with β-glucosidase activity was purified from the midgut Gland of the land crab Gecarcoidea natalis. The enzyme was capable of releasing glucose progressively from cellobiose, cellotriose or cellotetraose. Although β-glucosidases (EC 3.2.1.21) have some activity towards substrates longer than cellobiose, the enzyme was classified as a glucohydrolase (EC 3.2.1.74) as it had a preference for larger substrates (cellobiose<cellotriose=cellotetraose). It was able to synthesise some cellotetraose by the transglycosylation of smaller substrates – another common feature of glucohydrolases. The interaction between the glucohydrolase described here and the endo-β-1,4-glucanases described previously for G. natalis provides a complete model for cellulose hydrolysis in crustaceans and possibly in other invertebrates. After mechanical fragmentation by the gastric mill, multiple endo-β-1,4-glucanases would initially cleave β-1,4-glycosidic bonds within native cellulose, releasing small oligomers, including cellobiose, cellotriose and cellotetraose. The glucohydrolase would then attach to these oligomers, progressively releasing glucose. The glucohydrolase might also attach directly to crystalline cellulose to release glucose from free chain ends. This two-enzyme system differs from the traditional model, which suggests that total cellulose hydrolysis requires the presence an endo-β-1,4-glucanse, a cellobiohydrolase and a β-glucosidase
Language eng
Field of Research 060107 Enzymes
Socio Economic Objective 970106 Expanding Knowledge in the Biological Sciences
HERDC Research category C1 Refereed article in a scholarly journal
HERDC collection year 2010
Copyright notice ©2010, Company of Biologists
Persistent URL http://hdl.handle.net/10536/DRO/DU:30031463

Document type: Journal Article
Collections: School of Life and Environmental Sciences
Open Access Collection
Connect to link resolver
 
Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved.

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.

Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 9 times in TR Web of Science
Scopus Citation Count Cited 8 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 289 Abstract Views, 19 File Downloads  -  Detailed Statistics
Created: Mon, 06 Dec 2010, 15:21:21 EST by Teresa Treffry

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.