Cellulase is one of the most commercial and applicable enzymes which is produced chiefly by fungi, bacteria, protozoa and metazoa that catalyze cellulolysis, the decomposition of cellulose and of some related polysaccharides. Recently, the demand for this enzyme has been increased mostly for the various industrial purposes. It has been assumed that the milieu of earthworm’ s intestine is the final destination of digestive enzymes such as Cellulase. For the first time, this study is aimed to shed a light on the characteristics of Cellulase activity in the coelomic fluid and body extract of the earthworm Allolobophora chlorotica. Practically, following the preparation of homogenate and coelomic body in cold-ice and enzyme activities at different conditions were investigated and based on results, the optimum pH and temperature for Cellulase activity were pH 9 and 50 ° C, respectively for the two sources. Given the results, the earthworm contains a novel cellulolytic enzyme which is more stable at alkaline pH. A side from optimal pH and temperature, the addition of metal salts, including CaCl2, NaCl, MgCl2, KCl increase Cellulase activity, although, HgCl2 and EDTA have inhibitory effects on the enzyme. Due to common properties of Cellulase from coelomic and body extracts it can be concluded that coelomic Cellulase contents can be secreted from digestive tracts to facilitate the digestion of the food. Furthermore, based on results, the novel Cellulase is active at alkaline pH and moderately thermostable which can be used in biotechnological industries after purification.

The immobilization of Cellulase onto non-porous ultrafine silica particles was studied. Cellulase was extracted from a Trichoderma reesei culture after partial purification with ammonium sulfate (pH =5.0), which was then immobilizedonto non-porous ultra fine silica particles, with or without the use of glutaraldehyde as a cross linking agent. Cellulase was immobilized by adsorption onto ultrafine silica particles efficiently, as well as by covalent cross-linking with glutaraldehysde.Increasing the concentration of the free form of enzyme increased the amount of immobilized Cellulase. The maximum enzyme immobilization happened at the free enzyme concentration of 0.48 mg/ml. In general, the optimum pH for immobilization was found to be 5.0, which is close to the pi of the enzyme. The relative activity of the immobilized enzyme was also increased as t.he amount of immobilized enzyme was increased. However, immobilization of the enzyme on the ultrafine silica particles, with or without the use of glutaraldehyde, showed almost the same enzyme activities. The immobilized Cellulase showed a higher thermal stability, with respect to temperature, compared to the free cellulose.

Background and Objectives: Cellulose is a major component of plant biomass, which can be converted into biofuels and valuable chemicals. The key step in utilization of this organic material is its hydrolysis into soluble sugars. This study evaluated Cellulase production by Trichoderma harzianum under different pH values, temperatures and incubation periods with the aim to increase enzyme production and decrease its costs.Methods: The amount of protein production and the hydrolytic activity of Cellulase enzymes including exoglucanase, endoglucanase and b-glucosidase produced by T.harzianum were evaluated using various substrates such as avicel, carboxymethyl cellulose, cellobiose, Whatman grade 1 filter paper under different pH values (4, 4.8, 5.5 and 6.5), temperatures (25, 28 and 34 °C) and incubation times (48, 72, 96 and 120 h).Results: The optimum condition for Cellulase production by T. harzianum is 120 hours of incubation at 25 °C and pH of 6.5.Conclusion: T. harzianum can be used for the production of all three classes of Cellulase. This fungus is suitable for the efficient production of cellulolytic enzymes and reducing the cost of consumables.