Co-immobilization of an Enzyme System on a Metal-Organic Framework to Produce a More Effective Biocatalyst
In many respects, enzymes offer advantages over traditional chemical processes due to their decreased energy requirements for function and inherent greener processing. However, significant barriers exist for the utilization of enzymes in industrial processes due to their limited stabilities and inab...
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MDPI AG
2020-05-01
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| Series: | Catalysts |
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| Online Access: | https://www.mdpi.com/2073-4344/10/5/499 |
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| author | Raneem Ahmad Jordan Shanahan Sydnie Rizaldo Daniel S. Kissel Kari L. Stone |
| author_facet | Raneem Ahmad Jordan Shanahan Sydnie Rizaldo Daniel S. Kissel Kari L. Stone |
| author_sort | Raneem Ahmad |
| collection | DOAJ |
| description | In many respects, enzymes offer advantages over traditional chemical processes due to their decreased energy requirements for function and inherent greener processing. However, significant barriers exist for the utilization of enzymes in industrial processes due to their limited stabilities and inability to operate over larger temperature and pH ranges. Immobilization of enzymes onto solid supports has gained attention as an alternative to traditional chemical processes due to enhanced enzymatic performance and stability. This study demonstrates the co-immobilization of glucose oxidase (GO<i><sub>x</sub></i>) and horseradish peroxidase (HRP) as an enzyme system on Metal-Organic Frameworks (MOFs), UiO-66 and UiO-66-NH<sub>2</sub>, that produces a more effective biocatalyst as shown by the oxidation of pyrogallol. The two MOFs utilized as solid supports for immobilization were chosen to investigate how modifications of the MOF linker affect stability at the enzyme/MOF interface and subsequent activity of the enzyme system. The enzymes work in concert with activation of HRP through the addition of glucose as a substrate for GO<i><sub>x</sub></i>. Enzyme immobilization and leaching studies showed HRP/GO<i><sub>x</sub></i>@UiO-66-NH<sub>2</sub> immobilized 6% more than HRP/GO<i><sub>x</sub></i>@UiO-66, and leached only 36% of the immobilized enzymes over three days in the solution. The enzyme/MOF composites also showed increased enzyme activity in comparison with the free enzyme system: the composite HRP/GO<i><sub>x</sub></i>@UiO-66-NH<sub>2</sub> displayed 189 U/mg activity and HRP/GO<i><sub>x</sub></i>@UiO-66 showed 143 U/mg while the free enzyme showed 100 U/mg enzyme activity. This increase in stability and activity is due to the amine group of the MOF linker in HRP/GO<i><sub>x</sub></i>@UiO-66-NH<sub>2</sub> enhancing electrostatic interactions at the enzyme/MOF interface, thereby producing the most stable biocatalyst material in solution. The HRP/GO<i><sub>x</sub></i>@UiO-66-NH<sub>2</sub> also showed long-term stability in the solid state for over a month at room temperature. |
| first_indexed | 2024-03-10T20:04:41Z |
| format | Article |
| id | doaj.art-a3b614d3285f4eeea0384c70796eae87 |
| institution | Directory Open Access Journal |
| issn | 2073-4344 |
| language | English |
| last_indexed | 2024-03-10T20:04:41Z |
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| spelling | doaj.art-a3b614d3285f4eeea0384c70796eae872023-11-19T23:21:41ZengMDPI AGCatalysts2073-43442020-05-0110549910.3390/catal10050499Co-immobilization of an Enzyme System on a Metal-Organic Framework to Produce a More Effective BiocatalystRaneem Ahmad0Jordan Shanahan1Sydnie Rizaldo2Daniel S. Kissel3Kari L. Stone4Department of Chemistry, Lewis University, Romeoville, IL 60446, USADepartment of Chemistry, Lewis University, Romeoville, IL 60446, USADepartment of Chemistry, Lewis University, Romeoville, IL 60446, USADepartment of Chemistry, Lewis University, Romeoville, IL 60446, USADepartment of Chemistry, Lewis University, Romeoville, IL 60446, USAIn many respects, enzymes offer advantages over traditional chemical processes due to their decreased energy requirements for function and inherent greener processing. However, significant barriers exist for the utilization of enzymes in industrial processes due to their limited stabilities and inability to operate over larger temperature and pH ranges. Immobilization of enzymes onto solid supports has gained attention as an alternative to traditional chemical processes due to enhanced enzymatic performance and stability. This study demonstrates the co-immobilization of glucose oxidase (GO<i><sub>x</sub></i>) and horseradish peroxidase (HRP) as an enzyme system on Metal-Organic Frameworks (MOFs), UiO-66 and UiO-66-NH<sub>2</sub>, that produces a more effective biocatalyst as shown by the oxidation of pyrogallol. The two MOFs utilized as solid supports for immobilization were chosen to investigate how modifications of the MOF linker affect stability at the enzyme/MOF interface and subsequent activity of the enzyme system. The enzymes work in concert with activation of HRP through the addition of glucose as a substrate for GO<i><sub>x</sub></i>. Enzyme immobilization and leaching studies showed HRP/GO<i><sub>x</sub></i>@UiO-66-NH<sub>2</sub> immobilized 6% more than HRP/GO<i><sub>x</sub></i>@UiO-66, and leached only 36% of the immobilized enzymes over three days in the solution. The enzyme/MOF composites also showed increased enzyme activity in comparison with the free enzyme system: the composite HRP/GO<i><sub>x</sub></i>@UiO-66-NH<sub>2</sub> displayed 189 U/mg activity and HRP/GO<i><sub>x</sub></i>@UiO-66 showed 143 U/mg while the free enzyme showed 100 U/mg enzyme activity. This increase in stability and activity is due to the amine group of the MOF linker in HRP/GO<i><sub>x</sub></i>@UiO-66-NH<sub>2</sub> enhancing electrostatic interactions at the enzyme/MOF interface, thereby producing the most stable biocatalyst material in solution. The HRP/GO<i><sub>x</sub></i>@UiO-66-NH<sub>2</sub> also showed long-term stability in the solid state for over a month at room temperature.https://www.mdpi.com/2073-4344/10/5/499enzyme co-immobilizationmetal-organic frameworkbiocatalysis |
| spellingShingle | Raneem Ahmad Jordan Shanahan Sydnie Rizaldo Daniel S. Kissel Kari L. Stone Co-immobilization of an Enzyme System on a Metal-Organic Framework to Produce a More Effective Biocatalyst Catalysts enzyme co-immobilization metal-organic framework biocatalysis |
| title | Co-immobilization of an Enzyme System on a Metal-Organic Framework to Produce a More Effective Biocatalyst |
| title_full | Co-immobilization of an Enzyme System on a Metal-Organic Framework to Produce a More Effective Biocatalyst |
| title_fullStr | Co-immobilization of an Enzyme System on a Metal-Organic Framework to Produce a More Effective Biocatalyst |
| title_full_unstemmed | Co-immobilization of an Enzyme System on a Metal-Organic Framework to Produce a More Effective Biocatalyst |
| title_short | Co-immobilization of an Enzyme System on a Metal-Organic Framework to Produce a More Effective Biocatalyst |
| title_sort | co immobilization of an enzyme system on a metal organic framework to produce a more effective biocatalyst |
| topic | enzyme co-immobilization metal-organic framework biocatalysis |
| url | https://www.mdpi.com/2073-4344/10/5/499 |
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