Properties of two endoglucanases from a mutant strain Trichoderma sp. M₇ with potential application in the paper industry

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...

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Bibliographic Details
Published in:Applied biochemistry and microbiology 2009-03, Vol.45 (2), p.150-155
Main Authors: Petrova, S. D, Bakalova, N. G, Kolev, D. N
Format: Article
Language:English
Subjects:
Biochemistry
Biomedical and Life Sciences
Biotechnology
Cellulose
Enzymes
Filtrate
Flowers & plants
Life Sciences
Medical Microbiology
Microbiology
Mutation
Plant biomass
Pulp & paper industry
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Summary: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 K m 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.
ISSN:0003-6838
1608-3024
DOI:10.1134/S0003683809020069