The enzymatic solubilization of crystalline cellulose

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.

Name thesis:degree_name

Ph. D.

Level thesis:degree_level

doctoral

Discipline thesis:degree_discipline

Biochemistry

Department dc:contributor.department

Biochemistry

Grantor dc:publisher

Virginia Tech

Year dc:date.issued

1964

Author dc:creator

• Flora, Robert Montgomery

Chair dc:contributor.committeechair

• King, Kendall W.

Committee member dc:contributor.committeemember

• Engel, R. W.

Statement dc:rights

• In Copyright

Licence dc:rights.uri

• http://rightsstatements.org/vocab/InC/1.0/

Language dc:language.iso

en

Dc Identifier Other

etd-12232009-020727

OAI identifier oai:identifier

oai:vtechworks.lib.vt.edu:10919/40481