Purification and characterization of alkaline chitinase from Paenibacillus pasadenensis CS0611
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منابع مشابه
Purification and Characterization of Alkaline Xylanase Secreted from Paenibacillus macquariensis
An alkaline xylanase secreted by Paenibacillus macquariensis RC 1819 has been purified using ammonium sulfate fractionation, ion exchange chromatography using DEAE-cellulose and gel filtration chromatography over Sephadex G-200 and Sephadex G-100. The purified enzyme had the specific activity, 25.2 units/mg protein with birchwood xylan as a substrate. The purified enzyme showed a single protein...
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Two novel spore-forming, Gram-positive, mesophilic, heterotrophic bacteria representing two novel species were isolated from the Jet Propulsion Laboratory Spacecraft Assembly Facility (JPL-SAF) at Pasadena, CA, USA. The incidence of similar strains was examined by screening the growing collection of isolates ( approximately 400 strains) obtained from the JPL-SAF using species-specific PCR prime...
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The goal of this research was to isolate and identify the thermostable alkaline protease producing bacteria among several native Iranian microorganisms. At the end of screening program, a Bacillus subtilis BP-36 strain producing thermophilic alkaline protease was isolated from a hot spring in Ardebil province. The target enzyme was purified using a one-step Aqueous two-phase systems (ATPS) prot...
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Chitinase (EC 3.2.1.14) was isolated from the culture filtrate of Streptomyces sp. M-20 and purified by ammonium sulfate precipitation, DEAE-cellulose ion-exchange chromatography, and Sephadex G-100 gel filtration. No exochitinase activity was found in the culture filtrate. The molecular mass of the purified chitinase was 20 kDa, estimated by a sodium dodecyl sulfate-polyacrylamide gel electrop...
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ژورنال
عنوان ژورنال: Chinese Journal of Catalysis
سال: 2017
ISSN: 1872-2067
DOI: 10.1016/s1872-2067(17)62787-6