Toward Design Rules for Enzyme Immobilization in Hierarchical Mesoporous Metal-Organic Frameworks (2024)

Li, P., Modica, J. A., Howarth, A. J., Vargas L., E., Moghadam, P. Z., Snurr, R. Q., Mrksich, M., Hupp, J. T. (2016). Toward Design Rules for Enzyme Immobilization in Hierarchical Mesoporous Metal-Organic Frameworks. Chem, 1(1), 154-169. https://doi.org/10.1016/j.chempr.2016.05.001

Li, Peng ; Modica, Justin A. ; Howarth, Ashlee J. et al. / Toward Design Rules for Enzyme Immobilization in Hierarchical Mesoporous Metal-Organic Frameworks. In: Chem. 2016 ; Vol. 1, No. 1. pp. 154-169.

@article{5d2afebdcffb46e8bb409f86171a2c1f,

title = "Toward Design Rules for Enzyme Immobilization in Hierarchical Mesoporous Metal-Organic Frameworks",

abstract = "The immobilization of enzymes on or in solid supports is crucial for the industrialization of enzymes as chemical catalysts because immobilization provides stabilization, easy separation, and recyclability. Here, we show that a water-stable metal-organic framework, NU-1000, with hierarchical pore structure has the right combination of properties to be particularly well-suited as a scaffold for immobilizing enzymes such that they maintain full enzymatic catalytic activity. The immobilized enzyme shows greater resistance to organic solvent and denaturant than does the free enzyme and is characterized by greater reactant accessibility and higher activity than the same enzyme encapsulated in topologically simpler metal-organic frameworks. These findings suggest design rules for hierarchical pore structuring of host frameworks for enzyme-encapsulation applications by demonstrating enzyme immobilization in a solid support whereby the enzyme is highly accessible and retains catalytic activity under chemically challenging conditions.",

keywords = "SDG3: Good health and well-being",

author = "Peng Li and Modica, {Justin A.} and Howarth, {Ashlee J.} and {Vargas L.}, Ernesto and Moghadam, {Peyman Z.} and Snurr, {Randall Q.} and Milan Mrksich and Hupp, {Joseph T.} and Farha, {Omar K.}",

note = "Funding Information: O.K.F., J.T.H., and R.Q.S. gratefully acknowledge DTRA for financial support (HDTRA1-14-1-0014), and M.M. acknowledges the AFOSR (FA9550-16-1-0150). The authors thank Dr. Brian Pate (Joint Science & Technology Office for Chemical& Biological Defense, Defense Threat Reduction Agency) for helpful discussions and Jessica Hornick and Dr. Keith MacRenaris for helpful discussionsonCLSM and ICP-OES experiments, respectively. We also thank Dr.NicolaasA. Vermeulen for designing and producing the MOF graphs. Imaging work was done at the Northwestern University Biological Imaging Facility, generously supported by the NU Office for Research. Confocal microscopy wasperformed on a Leica TCS SP5 laser scanning confocal microscope system purchased with funds from the NU Office for Research. ICP-OES analysis was performed at the Northwestern University Quantitative Bio-element Imaging Center, generously supported by a NASA Ames Research Center grant (NNA04CC36G). Publisher Copyright: {\textcopyright} 2016 Elsevier Inc.",

year = "2016",

month = dec,

day = "1",

doi = "10.1016/j.chempr.2016.05.001",

language = "English (US)",

volume = "1",

pages = "154--169",

journal = "Chem",

issn = "2451-9294",

publisher = "Elsevier Inc.",

number = "1",

}

Li, P, Modica, JA, Howarth, AJ, Vargas L., E, Moghadam, PZ, Snurr, RQ, Mrksich, M, Hupp, JT 2016, 'Toward Design Rules for Enzyme Immobilization in Hierarchical Mesoporous Metal-Organic Frameworks', Chem, vol. 1, no. 1, pp. 154-169. https://doi.org/10.1016/j.chempr.2016.05.001

Toward Design Rules for Enzyme Immobilization in Hierarchical Mesoporous Metal-Organic Frameworks. / Li, Peng; Modica, Justin A.; Howarth, Ashlee J. et al.
In: Chem, Vol. 1, No. 1, 01.12.2016, p. 154-169.

Research output: Contribution to journal › Article › peer-review

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T1 - Toward Design Rules for Enzyme Immobilization in Hierarchical Mesoporous Metal-Organic Frameworks

AU - Li, Peng

AU - Modica, Justin A.

AU - Howarth, Ashlee J.

AU - Vargas L., Ernesto

AU - Moghadam, Peyman Z.

AU - Snurr, Randall Q.

AU - Mrksich, Milan

AU - Hupp, Joseph T.

AU - Farha, Omar K.

N1 - Funding Information:O.K.F., J.T.H., and R.Q.S. gratefully acknowledge DTRA for financial support (HDTRA1-14-1-0014), and M.M. acknowledges the AFOSR (FA9550-16-1-0150). The authors thank Dr. Brian Pate (Joint Science & Technology Office for Chemical& Biological Defense, Defense Threat Reduction Agency) for helpful discussions and Jessica Hornick and Dr. Keith MacRenaris for helpful discussionsonCLSM and ICP-OES experiments, respectively. We also thank Dr.NicolaasA. Vermeulen for designing and producing the MOF graphs. Imaging work was done at the Northwestern University Biological Imaging Facility, generously supported by the NU Office for Research. Confocal microscopy wasperformed on a Leica TCS SP5 laser scanning confocal microscope system purchased with funds from the NU Office for Research. ICP-OES analysis was performed at the Northwestern University Quantitative Bio-element Imaging Center, generously supported by a NASA Ames Research Center grant (NNA04CC36G).Publisher Copyright:© 2016 Elsevier Inc.

PY - 2016/12/1

Y1 - 2016/12/1

N2 - The immobilization of enzymes on or in solid supports is crucial for the industrialization of enzymes as chemical catalysts because immobilization provides stabilization, easy separation, and recyclability. Here, we show that a water-stable metal-organic framework, NU-1000, with hierarchical pore structure has the right combination of properties to be particularly well-suited as a scaffold for immobilizing enzymes such that they maintain full enzymatic catalytic activity. The immobilized enzyme shows greater resistance to organic solvent and denaturant than does the free enzyme and is characterized by greater reactant accessibility and higher activity than the same enzyme encapsulated in topologically simpler metal-organic frameworks. These findings suggest design rules for hierarchical pore structuring of host frameworks for enzyme-encapsulation applications by demonstrating enzyme immobilization in a solid support whereby the enzyme is highly accessible and retains catalytic activity under chemically challenging conditions.

AB - The immobilization of enzymes on or in solid supports is crucial for the industrialization of enzymes as chemical catalysts because immobilization provides stabilization, easy separation, and recyclability. Here, we show that a water-stable metal-organic framework, NU-1000, with hierarchical pore structure has the right combination of properties to be particularly well-suited as a scaffold for immobilizing enzymes such that they maintain full enzymatic catalytic activity. The immobilized enzyme shows greater resistance to organic solvent and denaturant than does the free enzyme and is characterized by greater reactant accessibility and higher activity than the same enzyme encapsulated in topologically simpler metal-organic frameworks. These findings suggest design rules for hierarchical pore structuring of host frameworks for enzyme-encapsulation applications by demonstrating enzyme immobilization in a solid support whereby the enzyme is highly accessible and retains catalytic activity under chemically challenging conditions.

KW - SDG3: Good health and well-being

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Li P, Modica JA, Howarth AJ, Vargas L. E, Moghadam PZ, Snurr RQ et al. Toward Design Rules for Enzyme Immobilization in Hierarchical Mesoporous Metal-Organic Frameworks. Chem. 2016 Dec 1;1(1):154-169. doi: 10.1016/j.chempr.2016.05.001