You are not logged in.

Novel substrates for the measurement of endo-1,4-β-glucanase (endo-cellulase)

McCleary, Barry V., Mangan, David, Daly, Robin, Fort, Sebastien, Ivory, Ruth and McCormack, Niall 2014, Novel substrates for the measurement of endo-1,4-β-glucanase (endo-cellulase), Carbohydrate research, vol. 385, pp. 9-17, doi: 10.1016/j.carres.2013.12.001.

Attached Files
Name Description MIMEType Size Downloads

Title Novel substrates for the measurement of endo-1,4-β-glucanase (endo-cellulase)
Formatted title Novel substrates for the measurement of endo-1,4-β-glucanase (endo-cellulase)
Author(s) McCleary, Barry V.
Mangan, David
Daly, RobinORCID iD for Daly, Robin orcid.org/0000-0002-9897-1598
Fort, Sebastien
Ivory, Ruth
McCormack, Niall
Journal name Carbohydrate research
Volume number 385
Start page 9
End page 17
Total pages 9
Publisher Elsevier
Place of publication Amsterdam, The Netherlands
Publication date 2014-02-19
ISSN 0008-6215
1873-426X
Keyword(s) endo-1,4-β-glucanase
cellulase
assay procedure
2-chloro-4-nitrophenyl
colourimetric
oligosaccharides
Colorimetry
Nitrophenols
Trisaccharides
beta-Glucosidase
Summary A specific and sensitive substrate for the assay of endo-1,4-β-glucanase (cellulase) has been prepared. The substrate mixture comprises benzylidene end-blocked 2-chloro-4-nitrophenyl-β-cellotrioside (BzCNPG3) in the presence of thermostable β-glucosidase. Hydrolysis by exo-acting enzymes such as β-glucosidase and exo-β-glucanase is prevented by the presence of the benzylidene group on the non-reducing end ᴅ-glucosyl residue. On hydrolysis by cellulase, the 2-chloro-4-nitrophenyl-β-glycoside is immediately hydrolysed to 2-chloro-4-nitrophenol and free ᴅ-glucose by the β-glucosidase in the substrate mixture. The reaction is terminated and colour developed by the addition of a weak alkaline solution. The assay procedure is simple to use, specific, accurate, robust and readily adapted to automation. This procedure should find widespread applications in biomass enzymology and in the specific assay of endo-1,4-β-glucanase in general.
Language eng
DOI 10.1016/j.carres.2013.12.001
Field of Research 060199 Biochemistry and Cell Biology not elsewhere classified
0305 Organic Chemistry
0601 Biochemistry And Cell Biology
0304 Medicinal And Biomolecular Chemistry
Socio Economic Objective 970111 Expanding Knowledge in the Medical and Health Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2013, Elsevier
Persistent URL http://hdl.handle.net/10536/DRO/DU:30089227

Document type: Journal Article
Collections: Faculty of Health
School of Exercise and Nutrition Sciences
Connect to link resolver
 
Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved.

Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 0 times in TR Web of Science
Scopus Citation Count Cited 0 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 14 Abstract Views, 0 File Downloads  -  Detailed Statistics
Created: Thu, 24 Nov 2016, 13:57:57 EST

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.