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Thermostability is a desirable characteristic in catalysts for biotechnology purposes. This is especially applicable for carbon sequestration at industrial sites, where there is mass production of industrial flue gas at high temperatures, containing large concentrations of CO2. Accordingly, the main focus of this study was to assess selected γ-CA proteins in silico for thermostability properties. The γ-CAs were from three organisms, Persephonella hydrogeniphila [29], Persephonella marina [30] and Thermosulfidibacter takaii [31], which were isolated from hydrothermal vent systems. A fourth γ-CA protein, from a hot spring thermophile Thermus thermophilus HB8 (γ-TtCA), was included in this study, based on its alleged thermostability properties, for comparison purposes [28].
An in silico approach was motivated by a similar study of the α-CAs including those from P. hydrogeniphila and P. marina, revealing important functional characteristics of the CAs as well as identifying possible thermostable sequestration agents [32]. Computational studies of the well-studied α-CA from Thermovibrio ammonificans have also been performed, where possible residue mutations for enhanced thermostability were identified [33]. The variants expressed after mutation studies indeed produced a more stable CA with an increased tolerance for high temperatures [34]. The prospects for in silico studies are therefore considered monumental and worth exploring. 153554b96e
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