PURIFICATION AND CHARACTERIZATION OF DETERGENT STABLE ALKALINE PROTEASE
A Novel Approach
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Alkaline proteases have been sought to have applications in several industries like detergent, dairy, leather, pharmaceutical, waste treatment etc. Proteases serve as important tools in determination of structures of proteins and polypeptides. The biotechnological promise of proteases makes them an ideal candidate for structure-function relationship studies and are also wide spread in nature. Microbes serve as preferred source of these enzymes because of their rapid growth, the limited space required for their cultivation and the facility with which they can be genetically manipulated to gener...
Alkaline proteases have been sought to have applications in several industries like detergent, dairy, leather, pharmaceutical, waste treatment etc. Proteases serve as important tools in determination of structures of proteins and polypeptides. The biotechnological promise of proteases makes them an ideal candidate for structure-function relationship studies and are also wide spread in nature. Microbes serve as preferred source of these enzymes because of their rapid growth, the limited space required for their cultivation and the facility with which they can be genetically manipulated to generate new enzymes with altered properties that are desirable for various applications. In order to withstand the market, enzymes from sources that are stable, active and more reliable have been identified and pure culture was obtained. The present study here in discloses the purification of an alkaline protease from a novel strain of Exiguobacterium sps.
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