Xylose induces cellulase production in Thermoascus aurantiacus
نویسندگان
چکیده
منابع مشابه
Xylose induces cellulase production in Thermoascus aurantiacus
Background Lignocellulosic biomass is an important resource for renewable production of biofuels and bioproducts. Enzymes that deconstruct this biomass are critical for the viability of biomass-based biofuel production processes. Current commercial enzyme mixtures have limited thermotolerance. Thermophilic fungi may provide enzyme mixtures with greater thermal stability leading to more robust p...
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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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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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The present study compared the production and the catalytic properties of amylolytic enzymes obtained from the fungi Lichtheimia ramosa (mesophilic) and Thermoascus aurantiacus (thermophilic). The highest amylase production in both fungi was observed in wheat bran supplemented with nutrient solution (pH 4.0) after 96 hours of cultivation, reaching 417.2 U/g of dry substrate (or 41.72 U/mL) and ...
متن کاملBiochemical characterization and mechanism of action of a thermostable beta-glucosidase purified from Thermoascus aurantiacus.
An extracellular beta-glucosidase from Thermoascus aurantiacus was purified to homogeneity by DEAE-Sepharose, Ultrogel AcA 44 and Mono-P column chromatography. The enzyme was a homotrimer, with a monomer molecular mass of 120 kDa; only the trimer was optimally active at 80 degrees C and at pH 4.5. At 90 degrees C, the enzyme showed 70% of its optimal activity. It was stable at pH 5.2 and at tem...
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ژورنال
عنوان ژورنال: Biotechnology for Biofuels
سال: 2017
ISSN: 1754-6834
DOI: 10.1186/s13068-017-0965-z