Purification a d Some Properties of a from an Alkaliphilic Nocardiopsis sp . Keratinolytic TOA - 1 Enzyme JSsw
نویسنده
چکیده
Although the tile-joints of bathrooms are highly alkaline, it is well known that many microorganisms, especially certain fungi, can grow preferentially in such environments.i) Thus, attempts to prevent microbial growth in bathrooms have been continuously conducted. In a series of these studies, we have isolated a number of alkaliphilic bacterial strains from the tile-joints. The isolation of alkaliphilic microorganisms was done out using an alkaline medium containing 10g of glucose, 5 g of peptone, 1 g of K2HP04, O.5 g of MgS04・7H20, 15gof agar, and 10gof Na2C03 (per liter). Among a number of alkaliphilic strains isolated in this study, an alkaliphilic actinornycetes strain, TOA-1, was chosen as a protease producer. The substrate mycelium of this strain was colorless. The spores were in straight chains between 10 and 50 in number, and the surface was smooth and white, Strain TOA-1 grew at pH 7.5-13.0 between 1S-40eC. The optimal pH and temperature for growth were 10.0 and 300C, respectively. Diaminopimeric acid was the meso type and diagnostic sugars were not de-
منابع مشابه
Purification and some properties of a keratinolytic enzyme from an alkaliphilic Nocardiopsis sp. TOA-1.
A novel alkaliphilic Nocardiopsis sp., strain TOA-1, was isolated from a tile-joint of a bathroom. Strain TOA-1 produced a variety of alkaline hydrolytic enzymes. An alkaline protease, designated NAPase, was purified and characterized. NAPase had a very high keratinolytic activity and high stability under acidic conditions.
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تاریخ انتشار 2018