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Open AccessArticle

Co-immobilization of an Enzyme System on a Metal-Organic Framework to Produce a More Effective Biocatalyst

Department of Chemistry, Lewis University, Romeoville, IL 60446, USA
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Authors to whom correspondence should be addressed.
Catalysts 2020, 10(5), 499; https://doi.org/10.3390/catal10050499
Received: 28 March 2020 / Revised: 28 April 2020 / Accepted: 30 April 2020 / Published: 2 May 2020
(This article belongs to the Special Issue Multienzymatic Catalysis and/or Enzyme Co-immobilization)
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 (GOx) and horseradish peroxidase (HRP) as an enzyme system on Metal-Organic Frameworks (MOFs), UiO-66 and UiO-66-NH2, 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 GOx. Enzyme immobilization and leaching studies showed HRP/GOx@UiO-66-NH2 immobilized 6% more than HRP/GOx@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/GOx@UiO-66-NH2 displayed 189 U/mg activity and HRP/GOx@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/GOx@UiO-66-NH2 enhancing electrostatic interactions at the enzyme/MOF interface, thereby producing the most stable biocatalyst material in solution. The HRP/GOx@UiO-66-NH2 also showed long-term stability in the solid state for over a month at room temperature. View Full-Text
Keywords: enzyme co-immobilization; metal-organic framework; biocatalysis enzyme co-immobilization; metal-organic framework; biocatalysis
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MDPI and ACS Style

Ahmad, R.; Shanahan, J.; Rizaldo, S.; Kissel, D.S.; Stone, K.L. Co-immobilization of an Enzyme System on a Metal-Organic Framework to Produce a More Effective Biocatalyst. Catalysts 2020, 10, 499. https://doi.org/10.3390/catal10050499

AMA Style

Ahmad R, Shanahan J, Rizaldo S, Kissel DS, Stone KL. Co-immobilization of an Enzyme System on a Metal-Organic Framework to Produce a More Effective Biocatalyst. Catalysts. 2020; 10(5):499. https://doi.org/10.3390/catal10050499

Chicago/Turabian Style

Ahmad, Raneem; Shanahan, Jordan; Rizaldo, Sydnie; Kissel, Daniel S.; Stone, Kari L. 2020. "Co-immobilization of an Enzyme System on a Metal-Organic Framework to Produce a More Effective Biocatalyst" Catalysts 10, no. 5: 499. https://doi.org/10.3390/catal10050499

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Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

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