Partial Purification and Characterization of a Thermostable β-Mannanase from Aspergillus foetidus
نویسندگان
چکیده
منابع مشابه
PARTIAL PURIFICATION AND CHARACTERIZATION OF B-GALACTOSIDASE FROM ASPERGILLUS NIGER UV-5
The enzyme pgalactosidase from a mutant strain of A. niger UV-5 was partially purified using ammonium sulfate and acetone. The saturation range of 60-80% ammonium sulfate was found to yield 60.5% enzyme recovery with 2.4 fold purification. Acetone precipitation at enzyme: acetone ratio of 1 : 1.5 brought about a higher yield i.e. 68% and three-fold purification. The combined procedures of ...
متن کاملPurification and Characterization of a Thermostable β-Mannanase from Bacillus subtilis BE-91: Potential Application in Inflammatory Diseases
β-mannanase has shown compelling biological functions because of its regulatory roles in metabolism, inflammation, and oxidation. This study separated and purified the β-mannanase from Bacillus subtilis BE-91, which is a powerful hemicellulose-degrading bacterium using a "two-step" method comprising ultrafiltration and gel chromatography. The purified β-mannanase (about 28.2 kDa) showed high sp...
متن کاملPurification and Characterization of a Thermostable Neutrophilic Metalloprotease from Pseudomonas sp. DR89
A novel neutrophilic metalloprotease was isolated from Pseudomonas sp. DR89 isolate which was identified ina mineral spring in Iran. The enzyme was purified from the isolate to 21-folds in a three-step procedure involving ammonium sulfate precipitation, Q-Sepharose ionic exchange and Sephadex G-100 gel filtrationchromatography. Resuts showed that the enzyme was active at high temper...
متن کاملCloning, Purification, and Characterization of a Thermostable β-Glucosidase from Thermotoga thermarum DSM 5069
A 56-kDa β-glucosidase (TthBgl) derived from Thermotoga thermarum DSM 5069 was expressed and purified from Escherichia coli BL21 (DE3). The purified enzyme showed hydrolytic activity towards only pnitrophenyl-β-D-glucopyranoside among the synthetic glycosides tested. The pH maximum was 5.0, and under the conditions tested, maximal activity was at 85 oC, and pH stability occurred from 5.0 to 6.0...
متن کاملPartial purification and characterization of arginine decarboxylase from avocado fruit, a thermostable enzyme.
A partially purified preparation of arginine decarboxylase (EC 4.1.1.19), a key enzyme in polyamine metabolism in plants, was isolated from avocado (Persea americana Mill. cv Fuerte) fruit. The preparation obtained from the crude extract after ammonium sulfate precipitation, dialysis, and heat treatment, had maximal activity between pH 8.0 and 9.0 at 60 degrees C, in the presence of 1.2 millimo...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Applied Sciences
سال: 2015
ISSN: 2076-3417
DOI: 10.3390/app5040881