(Hyper)thermophilic enzymes : Production and purification
Autor: | Pierpaolo Falcicchio, Sotirios Koutsopoulos, Servé W. M. Kengen, John van der Oost, Mark Levisson |
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Jazyk: | angličtina |
Rok vydání: | 2020 |
Předmět: |
Laboratorium voor Fysische chemie en Kolloïdkunde
Biology Microbiology Microbiologie Protein purification Laboratorium voor Plantenfysiologie Temperature limit Overproduction Physical Chemistry and Colloid Science Heterologous production VLAG chemistry.chemical_classification Thermophile Size exclusion chromatography (SEC) Heat stability BacGen Thermal stability Thermozymes Immobilized metal affinity chromatography (IMAC) Enzyme Biochemistry chemistry Biocatalysis His-tag Laboratory of Plant Physiology |
Zdroj: | Protein Downstream Processing Methods in Molecular Biology ISBN: 9781071607749 Protein Downstream Processing. Totowa: Humana Press Methods in Molecular Biology ISBN: 9781627039765 Protein Downstream Processing. Humana Press Inc. |
Popis: | The discovery of thermophilic and hyperthermophilic microorganisms, thriving at environmental temperatures near or above 100 °C, has revolutionized our ideas about the upper temperature limit at which life can exist. The characterization of (hyper)thermostable proteins has broadened our understanding and presented new opportunities for solving one of the most challenging problems in biophysics: how are structural stability and biological function maintained at high temperatures where “normal” proteins undergo dramatic structural changes? In our laboratory, we have purified and studied many thermostable and hyperthermostable proteins in an attempt to determine the molecular basis of heat stability. Here, we present methods to express such proteins and enzymes in E. coli and provide a general protocol for overproduction and purification. The ability to produce enzymes that retain their stability and activity at elevated temperatures creates exciting opportunities for a wide range of biocatalytic applications. |
Databáze: | OpenAIRE |
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