Cellulase of Trichoderma

Biosynthesis, Purification, and Mode of Action of Cellulases of Trichoderma reesei... 

Reese, E. T. and M. Mandels, "Stability of the Cellulase of Trichoderma reesei under Use Conditions," Biotech. Bioeng. 22 (1980) 323-335. 

Bailey, M., Siika-aho, M., Valkeajarvi, A., and Penttila, M. 1993. Hidrolytic properties of two cellulases of Trichoderma reesei expressed in yeast. Biotechnol. Appl. Biochem., 17,75-76. 

Sheir-Neiss, G. and Montenecourt, B. S., Characterization of the secreted cellulases of Trichoderma reesei wild type and mutants during controlled fermentations. Appl. Microbiol. Biotechnol. 1984, 20, 46-53. 

Beldman, G., Searle-Van Leeuwen, M., Rombouts, F., and Voragen, F., The cellulase of Trichoderma viride Purification, characterization and comparison of all detectable endoglucanases, exoglucanases and B-glucosi-dases. EurJ. Biochem 1985, 146, 301-8. 

Gong C-S, Ladisch MR, Tsao GT (1977) Cellobiase from Trichoderma viride-. purification, properties,kinetics, and mechanism. Biotechnology and Bioengineering 19 959-981 Gong C-S, Ladisch MR, Tsao GT (1979) Biosynthesis, purification and mode of action of cellulase of Trichoderma reesei-. hydrolysis of cellulose mechanisms of enzymatic and acid catalysis. Advances in Chemistry Series vol. 181, American Chemical Society, Washington, DC, pp 261-287... 

This appHcation is carried out with the crude cellulases of Trichoderma, Aspergillus, and Penicillium. The digestive process and action of cellulase in the... 

The conversion of cellulase component B into A may be a result of some enzymatic modification of the enzyme molecule. Similar type of in vitro conversion has also been reported, for example, for the extracellular cellulase of Trichoderma viride (38) and the cell-bound invertase of bakers yeast (15). The occurrence of another type of conversion where the reversible association and dissociation of active subunits are operative, has been proven on the intrawall and extracellular invertases of Neurospora crassa (25). 

A number of commercial cellulases, samples from other workers, and acetone precipitated powders were compared (Table II). All of these demonstrated good activity on carboxymethylcellulose. In fact a number of these, notably the enzyme from Poria, were more active on CMC than the T. viride enzyme. About half of the enzymes showed good activity on filter paper. But T. viride enzymes show the highest activity on cotton, the most resistant substrate. In case inactivation at 50 °C. affected the activity on cotton and filter paper, these enzymes were also tested for hydrolysis at 25°C. (data not shown). The relative activities were the same as those found at 50°C. Selby (31) made a similar study of a number of cellulase preparations. He also found that the cellulase of Trichoderma viride had the highest activity on cotton. 

Production of Trichoderma reesei Cellulase System with High Hydrofytic Potential by Solid-State Fermentation... 

Wheat straw. Wheat straw ground to 20 mesh was treated with 2% NaOH solution (wt/vol) in 1 2 (solidiliquid) ratio at 121 C for 0.5 h (i.e., 4 g NaOH/100 g wheat straw). Trichoderma reesei QMY-1 was grown on pretreated wheat straw in SSF as well as in LSF under otherwise identical culture conditions. The SSF was carried out with full nutrient concentrations in one set and with one-half nutrient concentrations in the other set to evaluate the possible deleterious effects of elevated osmotic pressure. T reesei QMY-1 produced FP cellulase of 8.6 lU/ml (430 lU/g cellulose or 172 lU/g substrate) in 22 days. This showed that the organism was able to tolerate the high salt concentrations required in the SSF. In contrast, when the nutrients were supplied in one-half concentration, FP cellulase activity dropped to 6.7 lU/ml (335 lU/g cellulose or 134 lU/g substrate). However, the maximum enzyme activity was obtained one week earlier (14 days) than that obtained with full salt concentrations (Table I). 

Similarity of C. fimi Cellulases to Trichoderma reesei Cellulases... 

Targonski, Z. and Pielecki, J., Continuous semi-solid cultivation for the production of cellulase by Trichoderma reesei mutants using a polyurethane foam carrier and a liquid medium, Acta-Biotechnol. 1995 vol. 15, no. 3, pp. 289-296. 

Tuerker. M. and Mavituna, E, Production of cellulase by freely suspended and immobilized cells of Trichoderma reesei, Enzyme-Microb.-Technol. 1987. vol. 9, no. 

Targonski and Pielecki investigated the production of cellulase using immobilized mycelium of Trichoderma reesei mutants on polyurethane foam impregnated... 

For enzymatic degradation, culture filtrates of selected strains of Trichoderma viride ( Cellulase T ) and Gliocladium spec. ( Cellulase G ) were used, strains being selected by screening with respect to Ci activity. Generally, 1-g samples of substrate were incubated at 40°C with a mixture of 80 ml of culture filtrate and 20 ml of acetate buffer (pH = 5.0) for 12 to 170 hours. 

All naturally occurring fungal strains of Trichoderma require an inducer for cellulase synthesis. In the absence of an inducer such as cellulose, cellobiose (21,22), or sophorose (12,13,14,23), Trichoderma does not make any detectable cellulase complex enzymes. The true physiological inducer of cellulase is currently unknown. Insoluble cellulose is presumably not such an inducer since there is no way for the internal cell machinery to sense the presence of this insoluble material. However, a small transglycosylation product such as sophorose, 2-0-/ -glucopyranosyl-D-glucose, may well be the natural inducer. 

Several microorganisms have been studied with respect to the production of a cellulolytic enzyme system for the saccharification of cellu-losic materials, the most thoroughly investigated organism and best producer of cellulase being Trichoderma viride (I). Recently, good saccharification data have been reported using a strain of Penicillium (2). 

Dynamics of Cellulase Production by Glucose Grown Cultures of Trichoderma reesei Rut-C30 as a Response to Addition of Cellulose... 

Baker, J. O., Tatsumoto, K., Grohmann, K., Woodward, I, Wichert, J. M., Shoemaker, S. R, and Himmel, M. E. 1992. Thermal denaturation of Trichoderma reesei Cellulases Studied by Differential Scanning Calorimetry and Tryptophan Fluorescence. Appl. Biochem. Biotechnol., 34/35, 217-231. 

Cavaco-Paulo, A., Almeida, L., and Bishop, D. 1998. Hydrolysis of Cotton Cellulose by Engineered Cellulases from Trichoderma Reesei. Textile Res. J., 68(4), 273-280. 

Kleman-Leyer, K. M., Siika-Aho, M., Teeri, T. T., and Kirk, T. K. 1996. The Cellulases Endoglucanase I and Cellobiohydrolase II of Trichoderma Reesei act synergistically to solubilize native cotton cellulose but not to decrease its moleculare size. Appl. Environ. Microbiol., 62,2883-2887. 

Nidetzky, B., Hayn, M., Macarron, R., and Steiner, W. 1993. Synergism of Trichoderma-Reesei Cellulases While Degrading Different Celluloses. Biotechnoi. Lett., 15, 71-76. 

Nidetzky, B., Steiner, W., and Claeyssens, M. 1995. Synergistic interaction of cellulases from Trichoderma reesei during cellulose degradation. Enzymatic Degradation of Insoluble Carbohydrates. ACS Symposium Series, 618, 90-112. 

Otter, D. E. Munro, P. A., Scott, G. K., and Geddes, R. 1984. Elution of Trichoderma reesei cellulases from cellulose by pH adjustment with sodium hydroxide. Biotechnol. Lett., 6, 369. 

---