Linked Life Data

11393354

Source:http://linkedlifedata.com/resource/pubmed/id/11393354

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-6-6
pubmed:abstractText
The interfacial behavior of Thermomonosporafusca E5 and Trichoderma reesei cellobiohydrolase I (CBHI) cellulases were studied at synthetic surfaces. For this purpose, colloidal silica and polystyrene particles were used to prepare cellulase-particle suspensions that could be analyzed by solution-phase techniques. Circular dichroism spectroscopy of each cellulase, alone as well as in suspension with silica, was used to determine whether structural changes occurred on adsorption. Changes in spectra were observed for CBHI, but not for E5. Gel-permeation chromatography of the cellulase-particle suspensions showed that neither cellulase binds to silica, suggesting that changes in spectra for CBHI were a result of solution-phase phenomena. Microfiltration of cellulase-polystyrene suspensions showed that both cellulases bind to polystyrene. However, circular dichroism experiments with polysterene proved unworkable, owing to excessive light absorption by the polystyrene. Adsorption kinetics of each cellulase were recorded, in situ, at hydrophilic and silanized, hydrophobic silica surfaces using ellipsometry. Ellipsometric data recorded for each cellulase at hydrophilic silica showed insignificant adsorption. Binding did occur between each cellulase and silanized silica, most likely mediated through hydrophobic associations. Adsorption in this case was irreversible to dilution.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0273-2289
pubmed:author
pubmed:issnType
Print
pubmed:volume
94
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
29-40
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Adsorption of Thermomonospora fusca E5 and Trichoderma reesei cellobiohydrolase I cellulases on synthetic surfaces.
pubmed:affiliation
Department of Bioengineering, Oregon State University, Corvallis 97331-3906, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't