Enzymes are naturally occurring catalysts with a broad spectrum of catalysed chemical reactions, and they therefore represent environmentally-friendly and economically costeffective tools in many industrial processes, bioremediation, biomedical and pharmacological applications. Among such biocatalysts belong haloalkane dehalogenases (HLDs), which catalyse the cleavage of the carbon-halogen bond of halogenated compounds, resulting in corresponding products – alcohols, halide ions and protons. Howe-ver, catalytic properties of naturally occurring HLDs very often do not fulfill reqirements of industrial applications which limits their practical potential. Methods of directed evolution and ratoional design are therefore often used to generate genetic diversity and cosntruct novel protein varaits with deired function. In this work, a protein engineering strategy was applied to improve catalytic parameters of haloalkane dehalogenase DhaA31 towards anthropogenic pollutant 1,2,3-trichloropropane.Formula clause:Please postpone publication of materials, methods, results and conclusions of this thesis for a period of 3 years. These results are part of a project that has not yet been published.
| Identifer | oai:union.ndltd.org:nusl.cz/oai:invenio.nusl.cz:426932 |
| Date | January 2018 |
| Creators | Kratochvíl, Jakub |
| Source Sets | Czech ETDs |
| Language | Czech |
| Detected Language | English |
| Type | info:eu-repo/semantics/masterThesis |
| Rights | info:eu-repo/semantics/restrictedAccess |
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