Trichoderma viride

Mould growth, 25 °C Trichoderma viride Waste paper Yes Yes... 

Vincken, J.-P., Beldman, G. and Voragen, A. G. J. (1994). The effect of xyioglucans on the degradation of cell-wall-embedded cellulose by the combined action of cellobiohydrolase and endoglucanases from Trichoderma viride. Plant Physion04, 99-107. 

Soils Trichoderma viride, extracts of soil humic fulvic acids stim d plant growth nodule mass dec d nodule no. 120... 

Rodriguez-Kabana, R., E.A. Curl, and H.H. Funderburk, Jr. 1968. Effect of atrazine on growth activity of Sclerotium rolfsii and Trichoderma viride in soil. Canad. Jour. Microbiol. 14 1283-1288. 

Trichoderma reesi, 12 479, 480 Trichoderma viride, 10 536 Trichothecene mycotoxins, 14 144, 146 Trichromatic sources, for white LEDs, 14 862... 

L-Pipecolic acid, a key component of many antibiotic and anticancer biomolecules, serves as an important chiral pharmaceutical intermediate. We have developed an enzyme-coupled system consisting of zl -piperidine-2-carboxylate reductase (Pip2C) from Pseudomonas putida, glucose dehydrogenase (GDH) from Bacillus subtilis, and L-lysine a-oxidase from Trichoderma viride, affording L-pipecolic acid from L-lysine in high yield with an excellent enantioselectivity (Figure 10.2). ... 

Under continuous flow conditions involving feeding, aeration, settling, and reflux, a mixture of jD-chloronitrobenzene and 2,4-dinitrochlorobenzene was reduced 61-70% after 8-13 d by Arthrobacter simplex, a microorganism isolated from industrial waste. A similar experiment was conducted using two aeration columns. One column contained A. simplex, the other a mixture of A. simplex and microorganisms isolated from soil Streptomyces coelicolor, Fusarium sp., probably aquaeductum and Trichoderma viride). After 10 d, 89.5-91% of the nitro compounds was reduced. p-Chloronitrobenzene was reduced to 4-chloroaniline and six unidentified compounds (Bielaszczyk et al., 1967). 

Matsumura and Bousch (1966) isolated carboxy lest erase (s) enzymes from the soil fungus Trichoderma viride und a bacterium Pseudomonas sp., obtained from Ohio soil samples, that were capable of degrading malathion. Compounds identified included diethyl maleate, desmethyl malathion, carboxylesterase products, other hydrolysis products, and unidentified metabolites. The authors found that these microbial populations did not have the capability to oxidize malathion due to the absence of malaoxon. However, the major degradative pathway appeared to be desmethylation and the formation of carboxylic acid derivatives. 

Matsumura, F. and Boush, G.M. Degradation of insecticides by a soil fungus, Trichoderma viride.J. Econ. EntomoL, 61 610-612, 1968. 

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... 

Piel, J., Atzorn, R., Gabler, R., Kuhnemann, F. and Boland, W. (1997). Cellulysin from the plant parasitic fungus Trichoderma viride elicits volatile biosynthesis in higher plants via the octadecanoid signalling cascade. Febs Letters 416 143-148. 

There are many sources of cellulolytic enzymes however, the fungus Trichoderma viride has proved to be the most effective source to date. The microbiology (25,32) and enzyme kinetics (24,30) studies on this organism have been pioneered by workers such as Reese and Mandels at... 

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. 

Enzymes. The mannanase was isolated from Aspergillus niger (11) fraction 4 b was used throughout the experiments (cf. Table 1 in (11)). The xylanase 2, the avicelase 1, and the avicelase 2 were isolated from Trichoderma viride (10). The properties of these enzymes have also been described in the papers cited above. The cellobiohydrolase C was kindly supplied by Dr. R. D. Brown, Jr., and Dr. E. K. Gum, Jr. (Virginia Polytechnic Institute, Blacksburg). The isolation (from Trichoderma viride) and the properties of the cellobiohydrolase C are described in their 1974 paper (12). 

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. 

The catalytic action of the two avicelases and the cellobiohydrolase C seems at least to be different from those of the xylanases isolated from Trichoderma viride i.e., the degradation products have a higher degree of polymerization even after prolonged incubation and, in the case of sprucewood holocellulose, no arabinose is liberated. 

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). 

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