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Entrapment of the Fastest Known Carbonic Anhydrase with Biomimetic Silica and Its Application for CO(2) Sequestration

Capturing and storing CO(2) is of prime importance. The rate of CO(2) sequestration is often limited by the hydration of CO(2), which can be greatly accelerated by using carbonic anhydrase (CA, EC 4.2.1.1) as a catalyst. In order to improve the stability and reusability of CA, a silica-condensing pe...

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Detalles Bibliográficos
Autores principales: Hsieh, Chia-Jung, Cheng, Ju-Chuan, Hu, Chia-Jung, Yu, Chi-Yang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8347136/
https://www.ncbi.nlm.nih.gov/pubmed/34372054
http://dx.doi.org/10.3390/polym13152452
Descripción
Sumario:Capturing and storing CO(2) is of prime importance. The rate of CO(2) sequestration is often limited by the hydration of CO(2), which can be greatly accelerated by using carbonic anhydrase (CA, EC 4.2.1.1) as a catalyst. In order to improve the stability and reusability of CA, a silica-condensing peptide (R5) was fused with the fastest known CA from Sulfurihydrogenibium azorense (SazCA) to form R5-SazCA; the fusion protein successfully performed in vitro silicification. The entrapment efficiency reached 100% and the silicified form (R5-SazCA-SP) showed a high activity recovery of 91%. The residual activity of R5-SazCA-SP was two-fold higher than that of the free form when stored at 25 °C for 35 days; R5-SazCA-SP still retained 86% of its activity after 10 cycles of reuse. Comparing with an uncatalyzed reaction, the time required for the onset of CaCO(3) formation was shortened by 43% and 33% with the addition of R5-SazCA and R5-SazCA-SP, respectively. R5-SazCA-SP shows great potential as a robust and efficient biocatalyst for CO(2) sequestration because of its high activity, high stability, and reusability.