Thesis (M.S.)--Brigham Young University. Dept. of Microbiology and Molecular Biology, 2007. / Includes bibliographical references (p. 33-37).

No description available.

Thesis (Ph. D.), Oregon Graduate Institute of Science & Technology, 1992.

Thesis (Master)--İzmir Institute of Technology,İzmir, 2004 / Includes bibliographical references (leaves. 43-49).

Thesis (M.S. in chemical engineering)--Washington State University, May 2006. / Includes bibliographical references (p. 66-74).

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.

Thesis (Ph. D.)--Mississippi State University. Department of Chemistry. / Title from title screen. Includes bibliographical references.

Thesis (Ph. D.)--Oregon Graduate Institute of Science and Technology, 1996.

<p> This thesis describes the isolation and investigation of a DNA-dependent RNA polymerase from the extreme halophile Halobacterium cutirubrum.</p> <p> The enzyme system was analyzed under conditions of very high ionic strengths which are characteristic of the internal salt concentrations of extreme halophiles and at much lower ionic strengths found in conventional bacterial systems. The enzyme was found to have activity in a wide range of salt concentrations when attached to its DNA template in the form of a DNA-Membrane-Protein complex. The enzyme, however, lost the ability to function at high ionic strengths when freed from this complex.</p> <p> The properties of the isolated DNA-dependent RNA polymerase from the halophile were then compared to the properties of the same enzyme isolated from the non-halophilic bacterium, Eschericia coli. Both enzymes were found to have the same approximate molecular weights and to share the same substrate requirements. The enzymes differed, however, in their response to inhibitors specific for RNA synthesis. </p> / Thesis / Master of Science (MSc)

Thesis (M.S. in chemical engineering)--Washington State University, August 2005. / Includes bibliographical references.