Anatomie Generale by V. Delmas [FRENCH] PDF

By V. Delmas [FRENCH]

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By V. Delmas [FRENCH]

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1994]. Only one thermostable cellulase has been reported to be produced by this microorganism to date, and the gene cel8Y has been cloned and expressed in E. coli by Kim et al. [2000]. The gene product (Cel8Y) has been purified and characterized. 7 kDa and it was able to hydrolyze β-1,4 linkages in CMC but not in Avicel. 0 and 80°C, respectively. At 90 and 100°C, the activity of the recombinant Cel8Y decreased by 50% after 4 and 2 h, respectively. On the basis of sequence comparisons, the enzyme is very closely related to other cellulases of GH family 8.

0, and the temperature optimum was higher than 97°C. The endoglucanase from P. , 2002]. The features of thermophilicity and thermostability make this enzyme of potential use for industrial hydrolysis of cellulose at high temperatures, particularly in biopolishing of cotton products. In fact, the desizing, that is the step to remove starch from the fabrics, is performed at temperatures of 70°C or above as amylases active at these temperatures are already available. If a hyperthermostable cellulase will be introduced, it will be possible to combine desizing and biopolishing in a single step.

6. 6 after incubation for 1 h at 37°C. The optimal temperature was 65°C, but the total activity was lost after incubation at this temperature for 1 h. Purified CelA4 was protease-resistant and exhibited the highest enzymatic activity toward barley β-glucan. The high activity at low pH and protease resistance make CelA4 a good candidate as commercial cellulase able to improve nutrient use in the animal feed industry. In fact, barley β-glucan cannot be digested by monogastric animals and, furthermore, the pig gastrointestinal tract is highly acidic and contains a lot of proteolytic enzymes.

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Anatomie Generale by V. Delmas [FRENCH]

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