Protease from Mucor subtilissimus UCP 1262: Evaluation of several specific protease activities and purification of a fibrinolytic enzyme
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چکیده
منابع مشابه
Isolation, Purification and Characterization of a Thermophilic Alkaline Protease from Bacillus subtilis BP-36
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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The protease produced by Mucor pusillus was recovered from a wheat bran medium by treatment with ammonium sulfate, ethyl alcohol, gel filtration and ion-exchange chromatography. The yield of the enzyme was 55%. The overall increase in the specific activity of the protease was 34-fold. The purified protease was most active at pH 3.8 and 5.6 against hemoglobin and casein, respectively. Optimal hy...
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Nomuraea rileyi (Farlow) Samson is an entomopathogenic fungus capable of producing a variety of enzymes including proteases and chitinases. Protease derived from microorganisms such as fungi, bacteria, and yeast has established wide spread applications in fields such as in the food, detergent and other industries. This study investigates the strategy for partial purification and characterizatio...
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A 36 kDa extracellular metalloprotease (designated to as vEP-MO6) was purified and characterized from Vibrio vulnificus sp. strain MO6 24/0. vEP-MO6 cleaved azocasein and a few other proteins such as prothrombin, plasminogen, fibrinogen and Factor Xa, which are associated with the blood coagulation pathway. The enzyme activity of vEP-MO6 was inhibited by EDTA, which was reversed by the addition...
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This research has focused on isolation and characterization of a strain of Bacillus <span style="font-variant: normal; font-style: normal; font-family: ArialMT...
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ژورنال
عنوان ژورنال: Anais da Academia Brasileira de Ciências
سال: 2020
ISSN: 1678-2690,0001-3765
DOI: 10.1590/0001-3765202020200882