Purification and properties of the cellulases from the thermophilic fungus Thermoascus aurantiacus
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چکیده
منابع مشابه
Substrate specificity and mode of action of the cellulases from the thermophilic fungus Thermoascus aurantiacus.
The substrate specificities of three cellulases and a beta-glucosidase purified from Thermoascus aurantiacus were examined. All three cellulases partially degraded native cellulose. Cellulase I, but not cellulase II and cellulase III, readily hydrolyzed the mixed beta-1,3; beta-1,6-polysaccharides such as carboxymethyl-pachyman, yeast glucan and laminarin. Both cellulase I and the beta-glucosid...
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An Endo-cellulase was purified to homogeneity using ammonium sulfate precipitation, ion exchange and size exclusion chromatography from newly isolated strain of Thermoascus aurantiacus RBB-1. The recovery and purification fold were 13.3% and 6.6, respectively, after size exclusion chromatography. The purified cellulase has a molecular mass (M) of 35 kDa. Optimum temperature for the enzyme was f...
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Polygalacturonases are enzymes involved in the degradation of pectic substances, being extensively used in food industries, textile processing, degumming of plant rough fibres, and treatment of pectic wastewaters. Polygalacturonase (PG) production by thermophilic fungus Thermoascus aurantiacus on solid-state fermentation was carried out in culture media containing sugar cane bagasse and orange ...
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Cellulose is the most plentiful renewable biopolymer in nature which could be utilized by cellulolytic enzymes. Cellulases are among the most important groups of industrial enzymes which are widely consumed in biofuel production, pulp and paper, textile, and detergent industries. These enzymes can support a cleaner environment through reducing chemical processes in mentioned industries and agro...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1980
ISSN: 0264-6021
DOI: 10.1042/bj1910083