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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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.
KASETTY. V. S. V. PRASAD M.Sc. BIOTECHNOLOGY
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Vendeur : BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, Allemagne
Taschenbuch. Etat : Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -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. 84 pp. Englisch. N° de réf. du vendeur 9783844317244
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Etat : New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: K V S V PRASADKASETTY. V. S. V. PRASAD M.Sc. BIOTECHNOLOGYAlkaline proteases have been sought to have applications in several industries like detergent, dairy, leather, pharmaceutical, waste treatment etc. Proteases serve as i. N° de réf. du vendeur 5472180
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Taschenbuch. Etat : Neu. This item is printed on demand - Print on Demand Titel. Neuware -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.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 84 pp. Englisch. N° de réf. du vendeur 9783844317244
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Taschenbuch. Etat : Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - 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. N° de réf. du vendeur 9783844317244
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Vendeur : preigu, Osnabrück, Allemagne
Taschenbuch. Etat : Neu. PURIFICATION AND CHARACTERIZATION OF DETERGENT STABLE ALKALINE PROTEASE | A Novel Approach | Prasad K V S V | Taschenbuch | 84 S. | Englisch | 2011 | LAP LAMBERT Academic Publishing | EAN 9783844317244 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu. N° de réf. du vendeur 107038646
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