Stabilization of an enzyme cytochrome c in a metal-organic framework against denaturing organic solvents

Fanrui Sha; Yijing Chen; Riki J. Drout; Karam B. Idrees; Xuan Zhang; Omar K. Farha

doi:10.1016/j.isci.2021.102641

Stabilization of an enzyme cytochrome c in a metal-organic framework against denaturing organic solvents

Fanrui Sha, Yijing Chen, Riki J. Drout, Karam B. Idrees, Xuan Zhang^*, Omar K. Farha^*

^*Corresponding author for this work

Chemistry

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

18 Scopus citations

Abstract

Enzymes are promising catalysts with high selectivity and activity under mild reaction conditions. However, their practical application has largely been hindered by their high cost and poor stability. Metal-organic frameworks (MOFs) as host materials show potential in protecting proteins against denaturing conditions, but a systematic study investigating the stabilizing mechanism is still lacking. In this study, we stabilized enzyme cytochrome c (cyt c) by encapsulating it in a hierarchical mesoporous zirconium-based MOF, NU-1000 against denaturing organic solvents. Cyt c@NU-1000 showed a significantly enhanced activity compared to the native enzyme, and the composite retained this enhanced activity after treatment with five denaturing organic solvents. Moreover, the composite was recyclable without activity loss for at least three cycles. Our cyt c@NU-1000 model system demonstrates that enzyme@MOF composites prepared via post-synthetic encapsulation offer a promising route to overcome the challenges of enzyme stability and recyclability that impede the widespread adoption of biocatalysis.

Original language	English (US)
Article number	102641
Journal	iScience
Volume	24
Issue number	6
DOIs	https://doi.org/10.1016/j.isci.2021.102641
State	Published - Jun 25 2021

Funding

The authors kindly acknowledge financial support from Defense Threat Reduction Agency (HDTRA1-19-1-0007), Merck & Co., Inc, and Northwestern University . This research made use of the X-ray diffraction capability of Northwestern University's IMSERC facilities, which receive support from the NSF ( CHE-1048773 and DMR0521267 ), Northwestern University Quantitative Bio-element Imaging Center generously supported by NASA Ames Research Center NNA06CB93G for metal analysis, the imaging instrumentation in the EPIC facility and Zetasizer in the Keck-II facility of Northwestern University's NUANCE Center, which has received support from the Soft and Hybrid Nanotechnology Experimental ( SHyNE ) Resource ( NSF ECCS-2025633 ), the MRSEC program ( NSF DMR-1720139 ), the International Institute for Nanotechnology (IIN), the Keck Foundation , and the State of Illinois through the IIN.

Keywords

Biocatalysis
Chemistry
Engineering
Green chemistry
Materials chemistry

ASJC Scopus subject areas

General

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10.1016/j.isci.2021.102641

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title = "Stabilization of an enzyme cytochrome c in a metal-organic framework against denaturing organic solvents",

abstract = "Enzymes are promising catalysts with high selectivity and activity under mild reaction conditions. However, their practical application has largely been hindered by their high cost and poor stability. Metal-organic frameworks (MOFs) as host materials show potential in protecting proteins against denaturing conditions, but a systematic study investigating the stabilizing mechanism is still lacking. In this study, we stabilized enzyme cytochrome c (cyt c) by encapsulating it in a hierarchical mesoporous zirconium-based MOF, NU-1000 against denaturing organic solvents. Cyt c@NU-1000 showed a significantly enhanced activity compared to the native enzyme, and the composite retained this enhanced activity after treatment with five denaturing organic solvents. Moreover, the composite was recyclable without activity loss for at least three cycles. Our cyt c@NU-1000 model system demonstrates that enzyme@MOF composites prepared via post-synthetic encapsulation offer a promising route to overcome the challenges of enzyme stability and recyclability that impede the widespread adoption of biocatalysis.",

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author = "Fanrui Sha and Yijing Chen and Drout, {Riki J.} and Idrees, {Karam B.} and Xuan Zhang and Farha, {Omar K.}",

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AU - Sha, Fanrui

AU - Chen, Yijing

AU - Drout, Riki J.

AU - Idrees, Karam B.

AU - Zhang, Xuan

AU - Farha, Omar K.

PY - 2021/6/25

Y1 - 2021/6/25

N2 - Enzymes are promising catalysts with high selectivity and activity under mild reaction conditions. However, their practical application has largely been hindered by their high cost and poor stability. Metal-organic frameworks (MOFs) as host materials show potential in protecting proteins against denaturing conditions, but a systematic study investigating the stabilizing mechanism is still lacking. In this study, we stabilized enzyme cytochrome c (cyt c) by encapsulating it in a hierarchical mesoporous zirconium-based MOF, NU-1000 against denaturing organic solvents. Cyt c@NU-1000 showed a significantly enhanced activity compared to the native enzyme, and the composite retained this enhanced activity after treatment with five denaturing organic solvents. Moreover, the composite was recyclable without activity loss for at least three cycles. Our cyt c@NU-1000 model system demonstrates that enzyme@MOF composites prepared via post-synthetic encapsulation offer a promising route to overcome the challenges of enzyme stability and recyclability that impede the widespread adoption of biocatalysis.

AB - Enzymes are promising catalysts with high selectivity and activity under mild reaction conditions. However, their practical application has largely been hindered by their high cost and poor stability. Metal-organic frameworks (MOFs) as host materials show potential in protecting proteins against denaturing conditions, but a systematic study investigating the stabilizing mechanism is still lacking. In this study, we stabilized enzyme cytochrome c (cyt c) by encapsulating it in a hierarchical mesoporous zirconium-based MOF, NU-1000 against denaturing organic solvents. Cyt c@NU-1000 showed a significantly enhanced activity compared to the native enzyme, and the composite retained this enhanced activity after treatment with five denaturing organic solvents. Moreover, the composite was recyclable without activity loss for at least three cycles. Our cyt c@NU-1000 model system demonstrates that enzyme@MOF composites prepared via post-synthetic encapsulation offer a promising route to overcome the challenges of enzyme stability and recyclability that impede the widespread adoption of biocatalysis.

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Stabilization of an enzyme cytochrome c in a metal-organic framework against denaturing organic solvents

Abstract

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