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Please use this identifier to cite or link to this item: http://eprint.iitd.ac.in/handle/2074/436

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DC FieldValueLanguage
dc.contributor.authorSethi, Benu-
dc.contributor.authorMishra, Saroj-
dc.contributor.authorBisaria, Virendra S-
dc.date.accessioned2005-07-02T07:23:31Z-
dc.date.available2005-07-02T07:23:31Z-
dc.date.issued1997-
dc.identifier.citationJournal of fermentation and bioengineering, 86(2), 233-235en
dc.identifier.urihttp://eprint.iitd.ac.in/dspace/handle/2074/436-
dc.description.abstractThe adsorption parameter, A,, (maximum protein adsorbed/g substrate) and KA (adsorption equilibrium constant) of Trichoderma reesei C-5 cellulases were 58.8 mg protein/g cellulose and 11.6 x 104 Z/m01 respec-tively. The activation energies for the adsorption rate constants of cellobiobydrolases and endoglucanases of C-5 were 30% and 11% lower respectively than that in the parent T. reesei QM9414 enzymes indicating the greater binding ability of the former. This was also reflected in its increased saccharification efficiency.en
dc.format.extent404274 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoenen
dc.subjectcellulasesen
dc.subjectadsorptionen
dc.subjectcellulose hydrolysisen
dc.titleAdsorption characteristics of cellulases from a constitutive mutant of trichoderma reeseien
dc.typeArticleen
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