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Analysis of Molecular Size Distributions of Cellulose Molecules during Hydrolysis of Cellulose by Recombinant Cellulomonas fimi -1,4-Glucanases

Stålbrand, Henrik LU ; Mansfield, Shawn D; Saddler, John N; Kilburn, Douglas G; J Warren, R Antony and Gilkes, Neil R (1998) In Applied and Environmental Microbiology 64(7). p.2374-2379
Abstract
Four -1,4-glucanases (cellulases) of the cellulolytic bacterium Cellulomonas fimi were purified from Escherichia coli cells transformed with recombinant plasmids. Previous analyses using soluble substrates had suggested that CenA and CenC were endoglucanases while CbhA and CbhB resembled the exo-acting cellobiohydrolases produced by cellulolytic fungi. Analysis of molecular size distributions during cellulose hydrolysis by the individual enzymes confirmed these preliminary findings and provided further evidence that endoglucanase CenC has a more processive hydrolytic activity than CenA. The significant differences between the size distributions obtained during hydrolysis of bacterial microcrystalline cellulose and acid-swollen cellulose... (More)
Four -1,4-glucanases (cellulases) of the cellulolytic bacterium Cellulomonas fimi were purified from Escherichia coli cells transformed with recombinant plasmids. Previous analyses using soluble substrates had suggested that CenA and CenC were endoglucanases while CbhA and CbhB resembled the exo-acting cellobiohydrolases produced by cellulolytic fungi. Analysis of molecular size distributions during cellulose hydrolysis by the individual enzymes confirmed these preliminary findings and provided further evidence that endoglucanase CenC has a more processive hydrolytic activity than CenA. The significant differences between the size distributions obtained during hydrolysis of bacterial microcrystalline cellulose and acid-swollen cellulose can be explained in terms of the accessibility of -1,4-glucan chains to enzyme attack. Endoglucanases and cellobiohydrolases were much more easily distinguished when the acid-swollen substrate was used. (Less)
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organization
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type
Contribution to journal
publication status
published
subject
in
Applied and Environmental Microbiology
volume
64
issue
7
pages
2374 - 2379
publisher
American Society for Microbiology
ISSN
0099-2240
language
English
LU publication?
yes
id
fadb4cbb-41ec-4df2-8f71-a886ff8cecc0 (old id 125611)
alternative location
http://aem.asm.org/cgi/content/full/64/7/2374
date added to LUP
2007-07-06 15:51:59
date last changed
2016-04-15 19:05:18
@article{fadb4cbb-41ec-4df2-8f71-a886ff8cecc0,
  abstract     = {Four -1,4-glucanases (cellulases) of the cellulolytic bacterium Cellulomonas fimi were purified from Escherichia coli cells transformed with recombinant plasmids. Previous analyses using soluble substrates had suggested that CenA and CenC were endoglucanases while CbhA and CbhB resembled the exo-acting cellobiohydrolases produced by cellulolytic fungi. Analysis of molecular size distributions during cellulose hydrolysis by the individual enzymes confirmed these preliminary findings and provided further evidence that endoglucanase CenC has a more processive hydrolytic activity than CenA. The significant differences between the size distributions obtained during hydrolysis of bacterial microcrystalline cellulose and acid-swollen cellulose can be explained in terms of the accessibility of -1,4-glucan chains to enzyme attack. Endoglucanases and cellobiohydrolases were much more easily distinguished when the acid-swollen substrate was used.},
  author       = {Stålbrand, Henrik and Mansfield, Shawn D and Saddler, John N and Kilburn, Douglas G and J Warren, R Antony and Gilkes, Neil R},
  issn         = {0099-2240},
  language     = {eng},
  number       = {7},
  pages        = {2374--2379},
  publisher    = {American Society for Microbiology},
  series       = {Applied and Environmental Microbiology},
  title        = {Analysis of Molecular Size Distributions of Cellulose Molecules during Hydrolysis of Cellulose by Recombinant Cellulomonas fimi -1,4-Glucanases},
  volume       = {64},
  year         = {1998},
}