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In the present study we selected Trichoderma sp. Enzyme production of 4.34 IU/ml (CMCase activity)
was obtained using 1% cellulose as substrate at 30 °C and 200 rpm after 6 days of incubation. The
enzyme was functional in a pH range of 4.0 to 6.5 with optimum activity at pH 5.0 for crude and 5.0 for
partially purified enzyme. Both crude and partially purified cellulase were functional in the range of 30-
70°C with the optimum enzyme activity at 60°C. The partially purified cellulase from Trichoderma sp.
was stable at pH 5.0 for 24 h retaining. No effect of b-mercaptoethanol, dithiothreitol and urea was found
on cellulase activity of Trichoderma sp. Glucose concentrations with 0.025% and above were inhibitory
for cellulase activity from Trichoderma sp. Xylose at lower concentrations were found to support
cellulase activity. The purified cellulase from Trichoderma sp. showed km and Vmax of 7 mg/ml and 0.45
μmol/ml/min. Modification of tryptophan residues present in the catalytic domain (SBD) using oxidation
by N- Bromosuccinimide revealed 2.5 mM was highly inhibitory for cellulase from Trichoderma sp. This
clearly suggests that tryptophan is important for the catalytic activity of cellulase. Effect of NAcetylimidazole,
a tyrosine modifiying agent showed that 60% of the native enzyme activity was retained.
This result indicates that acetylation of tyrosyl groups changes the enzymatic activity of cellulase. The
cellulase from Trichoderma sp. showed a good hydrolytic potential with maximum hydrolysis of 22.76%
and 22.14% from Agrowaste1 and Agrowaste2, which was slightly higher as compared to commercial
cellulase, thus proving the hydrolytic potential of the selected cellulase.
Keywords: Cellulose, Trichoderma, Microorganism.