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

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.

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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
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

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Citation counts:	Cited 6 times in TR Web of Science Cited 6 times in Scopus
Access Statistics:	258 Abstract Views, 5 File Downloads - Detailed Statistics
Created:	Mon, 06 Dec 2010, 15:21:21 EST by Teresa Treffry

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

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