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dc.contributor.authorFlora, Robert Montgomeryen_US
dc.date.accessioned2014-03-14T21:23:42Z
dc.date.available2014-03-14T21:23:42Z
dc.date.issued1964-07-05en_US
dc.identifier.otheretd-12232009-020727en_US
dc.identifier.urihttp://hdl.handle.net/10919/40481
dc.description.abstract

A crude cellulolytic enzyme prepq.ration derived from Trichoderma viride was capable of solubilizing native crystalline forms of cellulose. Enzyme activity ("hydrocellulase") was determined by measuring the decrease in turbidity of the assay reaction mixture which contained a suspended hydrocellulose substrate.

Preliminary studies of "hydrocellulase" showed that under assay conditions maximum activity was obtained at pH 4.7 to 4.8 and at 40° for 3 hours. The activity was relatively stable for a three hour period between pH 4.0 and 7.0 and at temperatures up to 40°. Cellobiose was several times more inhibitory than glucose. Methylcellulose was very inhibitory. Sulfhydryl compounds stimulated activity of the crude preparation. EDTA was without effect.

en_US
dc.format.mediumBTDen_US
dc.publisherVirginia Techen_US
dc.relation.haspartLD5655.V856_1964.F566.pdfen_US
dc.subjectEnzymesen_US
dc.subject.lccLD5655.V856 1964.F566en_US
dc.titleThe enzymatic solubilization of crystalline celluloseen_US
dc.typeDissertationen_US
dc.contributor.departmentBiochemistryen_US
dc.description.degreePh. D.en_US
thesis.degree.namePh. D.en_US
thesis.degree.leveldoctoralen_US
thesis.degree.grantorVirginia Polytechnic Instituteen_US
thesis.degree.disciplineBiochemistryen_US
dc.contributor.committeechairKing, Kendall W.en_US
dc.contributor.committeememberEngel, R. W.en_US
dc.identifier.sourceurlhttp://scholar.lib.vt.edu/theses/available/etd-12232009-020727/en_US
dc.date.sdate2009-12-23en_US
dc.date.rdate2009-12-23
dc.date.adate2009-12-23en_US


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