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Chitosan‐Based metal-organic framework for Stabilization of β-glucosidase: Reusability and storage stability()
Enzyme immobilization is a powerful tool for protecting enzymes from harsh reaction conditions and improving enzyme activity, stability, and reusability. In this study, metal organic frameworks (MIL-Fe composites) were synthesized via solvothermal reactions and then modified with chitosan (CS). β-Gl...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10618774/ https://www.ncbi.nlm.nih.gov/pubmed/37920506 http://dx.doi.org/10.1016/j.heliyon.2023.e21169 |
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author | Zeyadi, Mustafa Almulaiky, Yaaser Q. |
author_facet | Zeyadi, Mustafa Almulaiky, Yaaser Q. |
author_sort | Zeyadi, Mustafa |
collection | PubMed |
description | Enzyme immobilization is a powerful tool for protecting enzymes from harsh reaction conditions and improving enzyme activity, stability, and reusability. In this study, metal organic frameworks (MIL-Fe composites) were synthesized via solvothermal reactions and then modified with chitosan (CS). β-Glucosidase was immobilized on the chitosan-metal organic framework (CS-MIL-Fe), and the resulting composites were characterized with various analytical techniques. The β-glucosidase immobilized on a CS-MIL-Fe composite had an immobilization yield of 85 % and a recovered activity of 74 %. The immobilized enzyme retained 81 % of its initial activity after ten successive cycles and preserved 69 % of its original activity after 30 days of storage at 4 °C. In contrast, the free enzyme had only preserved 32 % of its original activity after 30 days. Under various temperature and pH conditions, the immobilized enzyme showed greater stability than the free enzyme, and the optimal temperature and pH were 60 °C and 6.0 for the immobilized enzyme and 50 °C and 5.0 for the free enzyme. The kinetic parameters were also determined, with the Km values of 13.4 and 6.98 mM for the immobilized and free β-glucosidase, respectively, and Vmax values of 3.96 and 1.72 U/mL, respectively. Overall, these results demonstrate that the CS-MIL-Fe@β-glucosidase is a promising matrix showing high catalytic efficiency and enhanced stability. |
format | Online Article Text |
id | pubmed-10618774 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-106187742023-11-02 Chitosan‐Based metal-organic framework for Stabilization of β-glucosidase: Reusability and storage stability() Zeyadi, Mustafa Almulaiky, Yaaser Q. Heliyon Research Article Enzyme immobilization is a powerful tool for protecting enzymes from harsh reaction conditions and improving enzyme activity, stability, and reusability. In this study, metal organic frameworks (MIL-Fe composites) were synthesized via solvothermal reactions and then modified with chitosan (CS). β-Glucosidase was immobilized on the chitosan-metal organic framework (CS-MIL-Fe), and the resulting composites were characterized with various analytical techniques. The β-glucosidase immobilized on a CS-MIL-Fe composite had an immobilization yield of 85 % and a recovered activity of 74 %. The immobilized enzyme retained 81 % of its initial activity after ten successive cycles and preserved 69 % of its original activity after 30 days of storage at 4 °C. In contrast, the free enzyme had only preserved 32 % of its original activity after 30 days. Under various temperature and pH conditions, the immobilized enzyme showed greater stability than the free enzyme, and the optimal temperature and pH were 60 °C and 6.0 for the immobilized enzyme and 50 °C and 5.0 for the free enzyme. The kinetic parameters were also determined, with the Km values of 13.4 and 6.98 mM for the immobilized and free β-glucosidase, respectively, and Vmax values of 3.96 and 1.72 U/mL, respectively. Overall, these results demonstrate that the CS-MIL-Fe@β-glucosidase is a promising matrix showing high catalytic efficiency and enhanced stability. Elsevier 2023-10-18 /pmc/articles/PMC10618774/ /pubmed/37920506 http://dx.doi.org/10.1016/j.heliyon.2023.e21169 Text en © 2023 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Research Article Zeyadi, Mustafa Almulaiky, Yaaser Q. Chitosan‐Based metal-organic framework for Stabilization of β-glucosidase: Reusability and storage stability() |
title | Chitosan‐Based metal-organic framework for Stabilization of β-glucosidase: Reusability and storage stability() |
title_full | Chitosan‐Based metal-organic framework for Stabilization of β-glucosidase: Reusability and storage stability() |
title_fullStr | Chitosan‐Based metal-organic framework for Stabilization of β-glucosidase: Reusability and storage stability() |
title_full_unstemmed | Chitosan‐Based metal-organic framework for Stabilization of β-glucosidase: Reusability and storage stability() |
title_short | Chitosan‐Based metal-organic framework for Stabilization of β-glucosidase: Reusability and storage stability() |
title_sort | chitosan‐based metal-organic framework for stabilization of β-glucosidase: reusability and storage stability() |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10618774/ https://www.ncbi.nlm.nih.gov/pubmed/37920506 http://dx.doi.org/10.1016/j.heliyon.2023.e21169 |
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