Thermoadaptation-directed evolution of chloramphenicol acetyltransferase in an error-prone thermophile using improved procedures

Enhancing the thermostability of thermolabile enzymes extends their practical utility. We previously demonstrated that an error-prone thermophile derived from Geobacillus kaustophilus HTA426 can generate mutant genes encoding enzyme variants that are more thermostable than the parent enzyme. Here, w...

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Veröffentlicht in:	Applied microbiology and biotechnology 2015-07, Vol.99 (13), p.5563-5572
Hauptverfasser:	Kobayashi, Jyumpei, Furukawa, Megumi, Ohshiro, Takashi, Suzuki, Hirokazu
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetyltransferase Applied Genetics and Molecular Biotechnology Bacillus kaustophilus Biomedical and Life Sciences Biotechnology Catalytic activity Chloramphenicol chloramphenicol acetyltransferase Chloramphenicol O-acetyltransferase Chloramphenicol O-Acetyltransferase - chemistry Chloramphenicol O-Acetyltransferase - genetics Chloramphenicol O-Acetyltransferase - metabolism Chloromycetin Chromosomes Directed evolution Directed Molecular Evolution - methods Enzyme Stability Enzymes Evolution Gene mutation genes Genetic aspects Genetic markers Genetics, Microbial - methods Geobacillus Geobacillus - enzymology Geobacillus - genetics Geobacillus - metabolism Geobacillus - radiation effects Heat resistance High temperature Hydroxyl groups Life Sciences Microbial Genetics and Genomics Microbiology Mutant Proteins - chemistry Mutant Proteins - genetics Mutant Proteins - metabolism mutants Mutation Mutation, Missense Physiological aspects Properties Protein Stability Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Site-directed mutagenesis Staphylococcus aureus Staphylococcus aureus - enzymology Staphylococcus aureus - genetics Temperature Thermal stability thermophilic microorganisms Threonine Transferases
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