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Characterization of Carboxylic Acid Reductase from Mycobacterium phlei Immobilized onto Seplite LX120
A multi-domain oxidoreductase, carboxylic acid reductase (CAR), can catalyze the one-step reduction of carboxylic acid to aldehyde. This study aimed to immobilize bacterial CAR from a moderate thermophile Mycobacterium phlei (MpCAR). It was the first work reported on immobilizing bacterial CAR onto...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9609965/ https://www.ncbi.nlm.nih.gov/pubmed/36297953 http://dx.doi.org/10.3390/polym14204375 |
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author | Basri, Rose Syuhada Rahman, Raja Noor Zaliha Raja Abd. Kamarudin, Nor Hafizah Ahmad Latip, Wahhida Ali, Mohd Shukuri Mohamad |
author_facet | Basri, Rose Syuhada Rahman, Raja Noor Zaliha Raja Abd. Kamarudin, Nor Hafizah Ahmad Latip, Wahhida Ali, Mohd Shukuri Mohamad |
author_sort | Basri, Rose Syuhada |
collection | PubMed |
description | A multi-domain oxidoreductase, carboxylic acid reductase (CAR), can catalyze the one-step reduction of carboxylic acid to aldehyde. This study aimed to immobilize bacterial CAR from a moderate thermophile Mycobacterium phlei (MpCAR). It was the first work reported on immobilizing bacterial CAR onto a polymeric support, Seplite LX120, via simple adsorption. Immobilization time and protein load were optimized for MpCAR immobilization. The immobilized MpCAR showed optimal activity at 60 °C and pH 9. It was stable over a wide range of temperatures (10 to 100 °C) and pHs (4–11), retaining more than 50% of its activity. The immobilized MpCAR also showed stability in polar solvents. The adsorption of MpCAR onto the support was confirmed by Scanning Electron Microscopy (SEM), Fourier-Transform Infrared (FTIR) spectroscopy, and Brunauer–Emmett–Teller (BET) analysis. The immobilized MpCAR could be stored for up to 6 weeks at 4 °C and 3 weeks at 25 °C. Immobilized MpCAR showed great operational stability, as 59.68% of its activity was preserved after 10 assay cycles. The immobilized MpCAR could also convert approximately 2.6 mM of benzoic acid to benzaldehyde at 60 °C. The successfully immobilized MpCAR on Seplite LX120 exhibited improved properties that benefit green industrial processes. |
format | Online Article Text |
id | pubmed-9609965 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-96099652022-10-28 Characterization of Carboxylic Acid Reductase from Mycobacterium phlei Immobilized onto Seplite LX120 Basri, Rose Syuhada Rahman, Raja Noor Zaliha Raja Abd. Kamarudin, Nor Hafizah Ahmad Latip, Wahhida Ali, Mohd Shukuri Mohamad Polymers (Basel) Article A multi-domain oxidoreductase, carboxylic acid reductase (CAR), can catalyze the one-step reduction of carboxylic acid to aldehyde. This study aimed to immobilize bacterial CAR from a moderate thermophile Mycobacterium phlei (MpCAR). It was the first work reported on immobilizing bacterial CAR onto a polymeric support, Seplite LX120, via simple adsorption. Immobilization time and protein load were optimized for MpCAR immobilization. The immobilized MpCAR showed optimal activity at 60 °C and pH 9. It was stable over a wide range of temperatures (10 to 100 °C) and pHs (4–11), retaining more than 50% of its activity. The immobilized MpCAR also showed stability in polar solvents. The adsorption of MpCAR onto the support was confirmed by Scanning Electron Microscopy (SEM), Fourier-Transform Infrared (FTIR) spectroscopy, and Brunauer–Emmett–Teller (BET) analysis. The immobilized MpCAR could be stored for up to 6 weeks at 4 °C and 3 weeks at 25 °C. Immobilized MpCAR showed great operational stability, as 59.68% of its activity was preserved after 10 assay cycles. The immobilized MpCAR could also convert approximately 2.6 mM of benzoic acid to benzaldehyde at 60 °C. The successfully immobilized MpCAR on Seplite LX120 exhibited improved properties that benefit green industrial processes. MDPI 2022-10-17 /pmc/articles/PMC9609965/ /pubmed/36297953 http://dx.doi.org/10.3390/polym14204375 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Basri, Rose Syuhada Rahman, Raja Noor Zaliha Raja Abd. Kamarudin, Nor Hafizah Ahmad Latip, Wahhida Ali, Mohd Shukuri Mohamad Characterization of Carboxylic Acid Reductase from Mycobacterium phlei Immobilized onto Seplite LX120 |
title | Characterization of Carboxylic Acid Reductase from Mycobacterium phlei Immobilized onto Seplite LX120 |
title_full | Characterization of Carboxylic Acid Reductase from Mycobacterium phlei Immobilized onto Seplite LX120 |
title_fullStr | Characterization of Carboxylic Acid Reductase from Mycobacterium phlei Immobilized onto Seplite LX120 |
title_full_unstemmed | Characterization of Carboxylic Acid Reductase from Mycobacterium phlei Immobilized onto Seplite LX120 |
title_short | Characterization of Carboxylic Acid Reductase from Mycobacterium phlei Immobilized onto Seplite LX120 |
title_sort | characterization of carboxylic acid reductase from mycobacterium phlei immobilized onto seplite lx120 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9609965/ https://www.ncbi.nlm.nih.gov/pubmed/36297953 http://dx.doi.org/10.3390/polym14204375 |
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