The present work studied thermostable cellulase extracted from 12 marine strains of
Trichoderma. Among the strains, Hypocrea estonica showed the maximum activity. The …

Treatment of Trichoderma reesei C30 cellulase at pH 10.0 for 1 h at room temperature
increased its pH and thermal stability. Chemical modification of the free epsilon-amino …

Enzyme stability studies have been reinvestigated under the conditions used for cellulose
hydrolysis (pH 4.8, 50° C, 24 hr). The cellobiohydrolase (CBH) component as measured on …

Decrease of cellulosolytic activity Trichoderma viride cellulase under heating and
mechanical treatment in solution and in solid phase is investigated. A comparison between …

Denaturation of cellulosolytic enzymes produced by microorganisms Trichoderma viride in
the presence of water was studied. Effective kinetic constants characterizing denaturation …

Stability of enzymatic activities with respect to different temp.(44, 37, 30 and 20° C) in terms
of deactivation of constants were established for β-1, 4-endogluconase and filter paper …

Properties of cellulase from <Emphasis Type="Italic">Trichoderma viride </Emphasis> Page 1
Folia Microbiol. 24, 269--272 (1979) Properties of Cellulase from Trichoderma viride JK …

Cellulases are the enzymes that cleave linkages of cellulose, and carbohydrate that is main
part of plants cell walls. Presently, cellulase isolation and partial purification was executed …

Xylanase thermoinactivation followed first-order kinetics and the activation energy for the
decay was 311kJmol− 1. Xylanase showed at 60° C a half-life of 2.7 min in absence of …

The cellulase components of Trichoderma viride which had been purified so far were all
derived from Peak ll which was one of the groups of this cellulase system and it was eluted …