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- Title
Accelerated CO2 Hydration with Thermostable Sulfurihydrogenibium azorense Carbonic Anhydrase-Chitin Binding Domain Fusion Protein Immobilised on Chitin Support.
- Authors
Hou, Juan; Li, Xingkang; Chen, Pengyu; Li, Kai; Jin, Peng; Liang, Yuanmei; Daroch, Maurycy; Kaczmarek, Michal B.
- Abstract
Carbonic anhydrases (CAs) represent a group of enzymes that catalyse important reactions of carbon dioxide hydration and dehydration, a reaction crucial to many biological processes and environmental biotechnology. In this study we successfully constructed a thermostable fusion enzyme composed of the Sulfurihydrogenibium azorense carbonic anhydrase (Saz_CA), the fastest CA discovered to date, and the chitin binding domain (ChBD) of chitinase from Bacillus circulans. Introduction of ChBD to the Saz_CA had no major impact on the effect of ions or inhibitors on the enzymatic activity. The fusion protein exhibited no negative effects up to 60 °C, whilst the fusion partner appears to protect the enzyme from negative effects of magnesium. The prepared biocatalyst appears to be thermally activated at 60 °C and could be partially purified with heat treatment. Immobilisation attempts on different kinds of chitin-based support results have shown that the fusion enzyme preferentially binds to a cheap, untreated chitin with a large crystallinity index over more processed forms of chitin. It suggests significant potential economic benefits for large-scale deployment of immobilised CA technologies such as CO2 utilisation or mineralisation.
- Subjects
CARBONIC anhydrase; CARBON dioxide; BIOTECHNOLOGY; CHITIN; MAGNESIUM
- Publication
International Journal of Molecular Sciences, 2019, Vol 20, Issue 6, p1494
- ISSN
1661-6596
- Publication type
Article
- DOI
10.3390/ijms20061494