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Improving biocatalysts via semi-rational protein design : use of a multiple sequence alignment platform to reduce screening efforts and facilitate hit identification / vorgelegt von Alberto Nobili

Protein-Engineering, gerichtete Evolution, Esterasen, Transaminasen, 3DM

PPN (Catalogue-ID): 867159979
Personen: Nobili, Alberto [VerfasserIn]
Cooperations/Conferences: Ernst-Moritz-Arndt-Universität Greifswald [Grad-verleihende Institution]
Format: eBook eBook
Language: English
Published: Greifswald, 2016
Hochschule: Dissertation, Ernst-Moritz-Arndt-Universität Greifswald, 2016
Basisklassifikation: 35.74
35.76
35.17
Subjects:

Proteindesign / Gerichtete Evolution / Esterasen / Transaminasen / Biokatalyse

Formangabe: Hochschulschrift
Notes: Literaturverzeichnis: Seite 35-45
Physical Description: 1 Online-Ressource (PDF-Datei: 222 Seiten, 20954 Kilobyte), Illustrationen (teilweise farbig), Diagramme (teilweise farbig).

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520 |a The synthesis of valuable chemicals via traditional chemical methods can be often outperformed by the use of enzymes because of their excellent chemo-, regio- and stereoselectivity in aqueous solvents at ambient temperatures. On the other hand, enzymes often suffer from several limitations that hamper their industrial application. Protein engineering is commonly applied to overcome these limitations although the generation and the validation of mutants is often a laborious process that may not lead to the desired results within reasonable time frames. This thesis focuses on engineering the enantioselectivity and the substrate scope of industrially relevant enzymes, such as esterases and transaminases. Semi-rational protein engineering was employed to identify improved variants for the synthesis of valuable chemicals ensuring a reduced screening effort. Compared to previous works, 3DM’s applicability was extended to the study of correlated mutations and proved effective in the acceleration of the comprehension and in the mutation of these enzymatic scaffolds. Semi-rational approaches require an extensive amount of information such as protein structures, reaction mechanisms, previous mutational experiments reported in literature and a considerable amount of amino acid sequences from similar proteins to analyze amino acid distributions and correlated mutations. Here, we have exploited 3DM as a tool that can combine all this wealth of information: 3DM is a convenient solution ... 
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