Isolation procedures for thermostable neutral proteinases produced by Bacillus stearothermophilus |
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Authors: | W. Sidler H. Zuber |
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Affiliation: | (1) Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule, Hönggerberg, CH-8903 Zürich, Switzerland |
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Abstract: | Summary Purification procedures for extracting and concentrating thermostable neutral proteinases using vacuum evaporation and ammonium sulfate precipitation, or adsorption chromatography on amberlite XAD-7 resin were compared. Adsorption chromatography proved to be the most effective method to concentrate, extract and partially purify the thermostable neutral proteases produced by Bacillus stearothermophilus NCIB 8924 and NRRL B-3880. Proteases can also be extracted from large volumes of culture media containing only weak proteolytic activity and a low protein concentration. Final purification of the thermostable neutral proteases was performed with an established affinity chromatography method. The method seems to be suitable for scaling up. |
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