Single-step purification of a recombinant thermostable α-amylase after solubilization of the enzyme from insoluble aggregates |
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Authors: | Anni Linden Frank Niehaus Garabed Antranikian |
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Abstract: | The expression of the gene encoding a thermostable α-amylase (EC 3.2.1.1) (optimal activity at 100°C) from the hyperthermophilic archaeon Pyrococcus woesei in the mesophilic hosts Escherichia coli and Halomonas elongata resulted in the formation of insoluble aggregates. More than 85% of the recombinant enzyme was present within the cells as insoluble but catalytically active aggregates. The recombinant α-amylase was purified to homogeneity in a single step by hydrophobic interaction chromatography on a phenyl superose column after solubilization of the enzyme under nondenaturing conditions. The enzyme was purified 258-fold with a final yield of 54%. |
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Keywords: | Enzymes α -Amylase |
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