Carbonic anhydrases catalyze a central reaction in life – the inter-conversion between carbon dioxide and water. Consequently, there is an increasing interest in research in using carbonic anhydrases for industrial applications such as biofuel production and carbon capture, since current approaches for CO2 capturing are expensive, harsh and energy demanding. The proof of principle for using carbonic anhydrase in these applications for carbon fixation has been validated. However, the current known and tested carbonic anhydrases are not tolerating the harsh industrial conditions. An ideal carbonic anhydrase should display thermo-, salt, and solvent stability and exhibit a decent reactivity. Herein we present the characterization and activity assessment of a halophilic γ-carbonic anhydrase from the Red Sea brine pool Discovery Deep. Protein X-ray structure exhibited the molecular structure and allowed the successful engineering of a small, active mutant library. Stopped-flow measurements gave insights into the activity and evaluated the engineering principles.
Identifer | oai:union.ndltd.org:kaust.edu.sa/oai:repository.kaust.edu.sa:10754/652899 |
Date | 04 1900 |
Creators | Vancea, Alexandra |
Contributors | Rueping, Magnus, Biological and Environmental Sciences and Engineering (BESE) Division, Arold, Stefan T., Al-Babili, Salim |
Source Sets | King Abdullah University of Science and Technology |
Language | English |
Detected Language | English |
Type | Thesis |
Rights | 2020-05-15, At the time of archiving, the student author of this thesis opted to temporarily restrict access to it. The full text of this thesis became available to the public after the expiration of the embargo on 2020-05-15. |
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