Trichoderma viride cellulase

A typical polymerization example is shown. The monomer -CF and cellulase Trichoderma viride 5 wt % for y6-CF) in a 5 1 mixture of acetonitrile and 0.05 M acetate buffer (pH 5) solution were stirred at 30 °C. The initially homogeneous solution became heterogeneous with a white precipitation of the product. After 12 h, the resulting suspension was heated at 100 °C to inactivate the enzyme and poured into an excess amount of methanol/water... 

Cellulase solution - dissolve 6.25 g cellulase from Trichoderma viride (Merck Ltd) in 1 I citrate-phosphate buffer, pH 4.6, immediately before use. 

Enz5mies Proteases Amylases Cellulases Various Bacilli, e.g. Bacillus licheniformis Bacillus subtilis, Aspergillus oryzae Trichoderma viride, Penicillium pinophilum... 

The Km of the Trichoderma viride cellulase is strongly dependent on the degree of substrate substitution (DS), and an extrapolation to DS = 0 gave a Km value of 3 mg/L for cellulose in a hypothetical solution. 

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. 

Sprucewood holocellulose was treated with an endo-p-1,4-mannanase isolated from Aspergillus niger and an endo-/3-1,4-xylanase, two avicelases, and a cellobiohydrolase C isolated from Trichoderma viride. The mannanase hydrolyzed about a quarter of the mannan in 2-3 days without xylan or cellulose degradation. The xylanase hydrolyzed about half the xylan with 10% mannan solubilization. The three cellulases hydrolyzed up to 45% of the cellulose and 20% of the xylan, accompanied by 40-70% solubilization of the mannan. Combined xylanase-mannanase treatment hydrolyzed about half the xylan and mannan. Addition of mannanase to to cellulose-treated samples increased the degradation of the cellulose and mannan. Micromorphological studies of the variously treated specimens revealed a loss of substances in P/Slf T, and adjacent zones of S2 of the tracheid wall. 

The three cellulases decomposed about 25-45% of the cellulose accompanied by solubilization of about 40-70% of the mannan and, by partial hydrolysis, of about 20% of the xylan present in the untreated sprucewood holocellulose. Based on the degradation products (cf. Table III, Columns 13-15, and Table II), the catalytic actions of the three cellulases—all isolated from Trichoderma viride—are similar or identical. The lower absolute degradation values obtained with cellobiohydrolase C might merely be a result of enzyme concentration. 

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). 

Howell, J. A. and J. D. Stuck, "Kinetics of Solka Floe Cellulose Hydrolysis by Trichoderma viride Cellulase," Biotechnol. Bioeng. 17 (1975) 873-893. 

Capitalizing on this metabolic difference between higher forms of life and micro-organisms is the basis for this research approach to wood protection. Compounds are available which inhibit the cellulase enzyme systems however, their specificity has not been determined. Mandels and Reese (21,22) found that the extracts from the immature fruit of persimmon or the extract from leaves of bayberry were very effective inhibitors of the cellulase system. At concentration levels of. 00005 and. 00018%, respectively, these two extracts inhibited the cellulase enzymes isolated from Trichoderma viride. It is not known what the active component(s) are in these two extracts. 

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. 

Trichoderma viride preparations cellulase pectinase hemicellulase... 

With the example provided by the characterization of these chemically and enzymologically pure cellulases, we decided to purify and describe the enzyme components of a cellulolytic organism, Trichoderma viride. Brief descriptions of the properties of partially purified exo-fi (1 4)glucanase (20), Ci or hydrocellulase (48), and endo-fi-(l 4)-... 

In 1968 Nisizawas laboratory (55) purified three cellulase components from Meicelase, which is a commercial cellulase from Trichoderma viride. These three components—Cellulases II, III, and IV—contained 16.8, 15.6, and 10.4% carbohydrate, respectively, and were active in hydrolyzing cellooligosaccharides, CM-cellulose, and cotton. They were inactive toward cellobiose and p-nitrophenyl-yS-D-glucoside. 

Table VIII. Hydrolysis of Cellulose Materials by Trichoderma viride Cellulase ...

Enzymatic synthesis of cellulose has been achieved by cel-lulase. For example, incubation of fS-cellobiosyl fluoride with a cellulase from Trichoderma viride can produce cellulose in 54% yield with DP around 22 after 12h. In addition, change of the reaction conditions (substrate concentration or organic solvent concentration) enabled the selective synthesis of the water-soluble celloohgosaccharides (118). 

The stilbene pinosylvin and its derivatives showed inhibitory activity on the fungal shoot blight and canker pathogen of conifers Sphaeropsis sapinea (P<0.001) [453]. Isorhapontin could inhibit the growth of the wood-staining fungus Trichoderma viride by inhibiting Trichoderma cellulases activity [454 and references therein]. 

The D-xylanase system of Stereum sanguinolentum,199 the only D-xylanase for which an amino acid composition has as yet been published, was found to contain a high proportion of acidic and aromatic amino acid residues. The M.W., as determined from the amino acid composition, is 23,900, compared with 21,600 as calculated from ultracentrifugation data. Other physical parameters that have been determined199 for this D-xylanase include the sedimentation coefficient [2.8S, which is similar to that reported for a D-xylanase isolated from Trichoderma viride,203 namely, 2.IS], the partial specific volume (0.71 cm3.g 1), and the molar extinction coefficient (6.25 X 104). Activation energies have been reported for D-xylanases from Schizophyllum commune233 (EA 28.6 kj.mol-1) and from a commercial cellulase preparation229 (EA 34.0 kj.mol-1). 

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... 

Cellulase Origin Trichoderma viride Jlilich Enzyme Products... 

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