Bibliographic Details
| Title: |
Properties of two endoglucanases from a mutant strain Trichoderma sp. M7 with potential application in the paper industry. |
| Authors: |
Petrova, S.1 spetrova@biofac.uni-sofia.bg, Bakalova, N.1, Kolev, D.1 |
| Superior Title: |
Applied Biochemistry & Microbiology. Mar2009, Vol. 45 Issue 2, p150-155. 6p. 2 Charts, 3 Graphs. |
| Subject Terms: |
*TRICHODERMA, *PAPER industry, *HOMOGENEITY, *PLANT biomass, *HYDROGEN-ion concentration |
| Abstract: |
Two endoglucanases were purified to electrophoretic homogeneity from the culture filtrate of a mutant strain Trichoderma sp. M7. EG-III and EG-IV had Mr of 49.7 and 47.5 kDa, and estimated pi values of 3.7 and 6.35, respectively. The optimal pH and temperature values were determined to be pH 5.0 and 60°C for the first cellulase, whereas pH 5.2 and 50 °C were optimal for the other. Endoglucanases exhibited typical Michaelis-Menten kinetics with Km and V values of 2.9 mg ml−1 and 60498.5 μmol min−1 mg−1 for EG-III and 3.8 mg ml−1 and 22650.9 μmol min−1 mg−1 for EG-IV, respectively. Mn2+, Cu2+ and Pd2+ strongly inhibited the enzymes. EC-IV catalyzed the hydrolysis of Na-CMC and hydroxyethyl cellulose (HEC) only, whereas EG-III displayed high activity towards xylans, also. Different preferences towards cellulosic substrates and their regions define a different role of the investigated enzymes in the degradation of plant biomass. [ABSTRACT FROM AUTHOR] |
|
Copyright of Applied Biochemistry & Microbiology is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) |
| Database: |
Academic Search Premier |