Linked Life Data

16346849

Source:http://linkedlifedata.com/resource/pubmed/id/16346849

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2010-6-25
pubmed:abstractText
Acetivibrio cellulolyticus extracellular cellulase extensively hydrolyzed crystalline celluloses such as Avicel (FMC Corp., Food and Pharmaceutical Products Div., Philadelphia, Pa.) but only if it was desalted and supplemented with Ca. The Ca effect was one of increased enzyme stability in the presence of the ion. Although preincubation of the cellulase complex at 40 degrees C for 5 h without added Ca had a negligible effect on endoglucanase activity or on the subseqent hydrolysis of amorphous cellulose, the capacity of the enzyme to hydrolyze crystalline cellulose was almost completely lost. Adsorption studies showed that 90% of the Avicel-solubilizing component of the total enzyme preparation bound to 2% Avicel at 40 degrees C. Under these conditions, only 15% of the endoglucanase and 25% of the protein present in the enzyme preparation adsorbed to the substrate. The protein profile of the bound enzyme, as analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, was complex and distinctly different from the profile observed for total cellulase preparations. The specific activity of A. cellulolyticus cellulase with respect to Avicel hydrolysis was compared with that of commercially available Trichoderma reesei cellulase.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Aug
pubmed:issn
0099-2240
pubmed:author
pubmed:issnType
Print
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
243-8
pubmed:dateRevised
2010-9-20
pubmed:year
1985
pubmed:articleTitle
Studies on Cellulose Hydrolysis by Acetivibrio cellulolyticus.
pubmed:affiliation
Division of Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada K1A 0R6.
pubmed:publicationType
Journal Article