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dc.contributor.authorSethi, Benu
dc.contributor.authorMishra, Saroj
dc.contributor.authorBisaria, Virendra S
dc.date.accessioned2005-07-02T07:23:31Z
dc.date.accessioned2019-02-09T07:12:17Z
dc.date.available2005-07-02T07:23:31Z
dc.date.available2019-02-09T07:12:17Z
dc.date.issued1997
dc.identifier.citationJournal of fermentation and bioengineering, 86(2), 233-235en
dc.identifier.urihttp://localhost:8080/xmlui/handle/12345678/436
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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