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Novel bovine carbonic anhydrase encapsulated in a metal–organic framework: a new platform for biomimetic sequestration of CO(2)
In this work, maximizing the utilization of CO(2) and its precipitation as CaCO(3) by using immobilized bovine carbonic anhydrase (BCA) was evaluated. In this way, selection of suitable carriers which have a gas adsorption function would enhance the CO(2) sequestration efficiency of the carbonic anh...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9071054/ https://www.ncbi.nlm.nih.gov/pubmed/35529640 http://dx.doi.org/10.1039/c9ra04603h |
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author | Asadi, Vahideh Kardanpour, Reihaneh Tangestaninejad, Shahram Moghadam, Majid Mirkhani, Valiollah Mohammadpoor-Baltork, Iraj |
author_facet | Asadi, Vahideh Kardanpour, Reihaneh Tangestaninejad, Shahram Moghadam, Majid Mirkhani, Valiollah Mohammadpoor-Baltork, Iraj |
author_sort | Asadi, Vahideh |
collection | PubMed |
description | In this work, maximizing the utilization of CO(2) and its precipitation as CaCO(3) by using immobilized bovine carbonic anhydrase (BCA) was evaluated. In this way, selection of suitable carriers which have a gas adsorption function would enhance the CO(2) sequestration efficiency of the carbonic anhydrase (CA). So a metal–organic framework (MOF), an excellent material for gas adsorption and enzyme immobilization was used. In this manner, BCA was encapsulated into the microporous zeolite imidazolate framework, ZIF-8, for the first time, using a bottle-around-a-ship method. Systematic characterization including powder X-ray diffraction (PXRD), UV-vis, and Fourier transform infrared (FT-IR) spectroscopies, BET, field emission scanning electron microscopy (FE-SEM) and energy dispersive X-ray (EDX) confirmed that the entrapment of BCA molecules was successfully achieved during the crystal growth of ZIF-8 with an enzyme loading of ca. 100 ± 1.2 mg g(−1) of BCA–ZIF-8. Optimization of the matrix for increasing the stability of the enzyme in an encapsulated form is the main aim of the present study. The de novo approach was proposed because this method provides better enzyme protection from degradation, minimizes enzyme leaching and enables multiple reuse. Then, the influence of different parameters, including pH, temperature, storage and reusability, was evaluated for enzyme@MOF composites versus free enzymes. The prepared biocatalyst exhibited outstanding activity in a wide pH and temperature range and demonstrates high storage stability up to 37 days. This efficient and simple association procedure seems well-adapted to produce an enzymatic bio-catalyst for biocatalytic hydration of CO(2). The FT-IR analysis revealed that the structure of BCA was well maintained during the encapsulation process. The thermal stability and reusability of the BCA–ZIF-8 increased noticeably due to the structural rigidity and confinement of the ZIF-8 scaffolds. These two parameters are very important for practical applications. |
format | Online Article Text |
id | pubmed-9071054 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | The Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-90710542022-05-06 Novel bovine carbonic anhydrase encapsulated in a metal–organic framework: a new platform for biomimetic sequestration of CO(2) Asadi, Vahideh Kardanpour, Reihaneh Tangestaninejad, Shahram Moghadam, Majid Mirkhani, Valiollah Mohammadpoor-Baltork, Iraj RSC Adv Chemistry In this work, maximizing the utilization of CO(2) and its precipitation as CaCO(3) by using immobilized bovine carbonic anhydrase (BCA) was evaluated. In this way, selection of suitable carriers which have a gas adsorption function would enhance the CO(2) sequestration efficiency of the carbonic anhydrase (CA). So a metal–organic framework (MOF), an excellent material for gas adsorption and enzyme immobilization was used. In this manner, BCA was encapsulated into the microporous zeolite imidazolate framework, ZIF-8, for the first time, using a bottle-around-a-ship method. Systematic characterization including powder X-ray diffraction (PXRD), UV-vis, and Fourier transform infrared (FT-IR) spectroscopies, BET, field emission scanning electron microscopy (FE-SEM) and energy dispersive X-ray (EDX) confirmed that the entrapment of BCA molecules was successfully achieved during the crystal growth of ZIF-8 with an enzyme loading of ca. 100 ± 1.2 mg g(−1) of BCA–ZIF-8. Optimization of the matrix for increasing the stability of the enzyme in an encapsulated form is the main aim of the present study. The de novo approach was proposed because this method provides better enzyme protection from degradation, minimizes enzyme leaching and enables multiple reuse. Then, the influence of different parameters, including pH, temperature, storage and reusability, was evaluated for enzyme@MOF composites versus free enzymes. The prepared biocatalyst exhibited outstanding activity in a wide pH and temperature range and demonstrates high storage stability up to 37 days. This efficient and simple association procedure seems well-adapted to produce an enzymatic bio-catalyst for biocatalytic hydration of CO(2). The FT-IR analysis revealed that the structure of BCA was well maintained during the encapsulation process. The thermal stability and reusability of the BCA–ZIF-8 increased noticeably due to the structural rigidity and confinement of the ZIF-8 scaffolds. These two parameters are very important for practical applications. The Royal Society of Chemistry 2019-09-10 /pmc/articles/PMC9071054/ /pubmed/35529640 http://dx.doi.org/10.1039/c9ra04603h Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/ |
spellingShingle | Chemistry Asadi, Vahideh Kardanpour, Reihaneh Tangestaninejad, Shahram Moghadam, Majid Mirkhani, Valiollah Mohammadpoor-Baltork, Iraj Novel bovine carbonic anhydrase encapsulated in a metal–organic framework: a new platform for biomimetic sequestration of CO(2) |
title | Novel bovine carbonic anhydrase encapsulated in a metal–organic framework: a new platform for biomimetic sequestration of CO(2) |
title_full | Novel bovine carbonic anhydrase encapsulated in a metal–organic framework: a new platform for biomimetic sequestration of CO(2) |
title_fullStr | Novel bovine carbonic anhydrase encapsulated in a metal–organic framework: a new platform for biomimetic sequestration of CO(2) |
title_full_unstemmed | Novel bovine carbonic anhydrase encapsulated in a metal–organic framework: a new platform for biomimetic sequestration of CO(2) |
title_short | Novel bovine carbonic anhydrase encapsulated in a metal–organic framework: a new platform for biomimetic sequestration of CO(2) |
title_sort | novel bovine carbonic anhydrase encapsulated in a metal–organic framework: a new platform for biomimetic sequestration of co(2) |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9071054/ https://www.ncbi.nlm.nih.gov/pubmed/35529640 http://dx.doi.org/10.1039/c9ra04603h |
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