Purification and Characterization of Chitosanase Enzyme from Streptomyces cyaneogriseus
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چکیده
منابع مشابه
Characterization of proteolytic enzyme secreted by Streptomyces cinereoruber ssp. cinereoruber isolated from human pleural fluid
Actinomycetes are an uncommon agent of human infections and its pathogenic factors are not known. The present study reports a rare case isolation of an actinomycete from a woman pleural fluid; the strain was identified by 16S rRNA gene sequence analysis. This strain was tested to produce an extracellular protease that hydrolysis gelatin, casein and hemoglobin on agar mediums. The purification o...
متن کاملThermostable Chitosanase from BacMus Characterization
chitin or other P-linked polymers. The enzyme activity was increased about 2.5-fold by the addition of 10 mM Co2+ and 1.4-fold by Mn2+. However, Cu2+ ion strongly inhibited the enzyme. Optimum temperature and pH were 60eC and 6.5, respectively. The enzyme was stable after heat treatment at 800C for 30 min or 70eC for 60 min and fairly stable in protein denaturants as well. Chitosan was hydrolyz...
متن کاملCharacterization of proteolytic enzyme secreted by Streptomyces cinereoruber ssp. cinereoruber isolated from human pleural fluid
Actinomycetes are an uncommon agent of human infections and its pathogenic factors are not known. The present study reports a rare case isolation of an actinomycete from a woman pleural fluid; the strain was identified by 16S rRNA gene sequence analysis. This strain was tested to produce an extracellular protease that hydrolysis gelatin, casein and hemoglobin on agar mediums. The purification o...
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L-asparaginase is an anti-neoplastic agent used in the lymphoblastic leukaemia chemotherapy. In the present study a novel strain, Streptomyces gulbargensis was explored for the production of extra-cellular L-asparaginase using groundnut cake extract. The optimum pH, temperature, inoculum size and agitation speed for enzyme production were pH 8.5, 40°C, 1x10(8)spores/ml and 200 rev/min respectiv...
متن کاملPurification and characterization of chitinase from Streptomyces sp. M-20.
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: Asian Journal of Biological Sciences
سال: 2010
ISSN: 1996-3351
DOI: 10.3923/ajbs.2011.15.24