Insights into the interaction between immobilized biocatalysts and metal–organic frameworks: a case study of PCN-333

Wenjie Yang; Weibin Liang; Luke A. O'Dell; Hamish D. Toop; Natasha Maddigan; Xingmo Zhang; Alena Kochubei; Christian J. Doonan; Yijiao Jiang; Jun Huang

doi:10.1021/jacsau.1c00226

Insights into the interaction between immobilized biocatalysts and metal–organic frameworks: a case study of PCN-333

Wenjie Yang, Weibin Liang^*, Luke A. O'Dell, Hamish D. Toop, Natasha Maddigan, Xingmo Zhang, Alena Kochubei, Christian J. Doonan, Yijiao Jiang, Jun Huang^*

^*Corresponding author for this work

School of Engineering

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

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Abstract

The immobilization of enzymes in metal–organic frameworks (MOFs) with preserved biofunctionality paves a promising way to solve problems regarding the stability and reusability of enzymes. However, the rational design of MOF-based biocomposites remains a considerable challenge as very little is known about the state of the enzyme, the MOF support, and their host–guest interactions upon immobilization. In this study, we elucidate the detailed host–guest interaction for MOF immobilized enzymes in the biointerface. Two enzymes with different sizes, lipase and insulin, have been immobilized in a mesoporous PCN-333(Al) MOF. The dynamic changes of local structures of the MOF host and enzyme guests have been experimentally revealed for the existence of the confinement effect to enzymes and van der Waals interaction in the biointerface between the aluminum oxo-cluster of the PCN-333 and the -NH2 species of enzymes. This kind of host–guest interaction renders the immobilization of enzymes in PCN-333 with high affinity and highly preserved enzymatic bioactivity.

[Graphic presents]

Original language	English
Pages (from-to)	2172-2181
Number of pages	10
Journal	JACS Au
Volume	1
Issue number	12
Early online date	15 Nov 2021
DOIs	https://doi.org/10.1021/jacsau.1c00226
Publication status	Published - 27 Dec 2021

Bibliographical note

Copyright the Author(s) 2021. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.

Keywords

metal-organic frameworks
enzyme immobilization
solid-state NMR
biointerface interaction
biocatalysis

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10.1021/jacsau.1c00226Licence: CC BY-NC-ND

Publisher version (open access)Final published version, 2.72 MBLicence: CC BY-NC-ND

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title = "Insights into the interaction between immobilized biocatalysts and metal–organic frameworks: a case study of PCN-333",

abstract = "The immobilization of enzymes in metal–organic frameworks (MOFs) with preserved biofunctionality paves a promising way to solve problems regarding the stability and reusability of enzymes. However, the rational design of MOF-based biocomposites remains a considerable challenge as very little is known about the state of the enzyme, the MOF support, and their host–guest interactions upon immobilization. In this study, we elucidate the detailed host–guest interaction for MOF immobilized enzymes in the biointerface. Two enzymes with different sizes, lipase and insulin, have been immobilized in a mesoporous PCN-333(Al) MOF. The dynamic changes of local structures of the MOF host and enzyme guests have been experimentally revealed for the existence of the confinement effect to enzymes and van der Waals interaction in the biointerface between the aluminum oxo-cluster of the PCN-333 and the -NH2 species of enzymes. This kind of host–guest interaction renders the immobilization of enzymes in PCN-333 with high affinity and highly preserved enzymatic bioactivity.[Graphic presents]",

keywords = "metal-organic frameworks, enzyme immobilization, solid-state NMR, biointerface interaction, biocatalysis",

author = "Wenjie Yang and Weibin Liang and O'Dell, {Luke A.} and Toop, {Hamish D.} and Natasha Maddigan and Xingmo Zhang and Alena Kochubei and Doonan, {Christian J.} and Yijiao Jiang and Jun Huang",

note = "Copyright the Author(s) 2021. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.",

year = "2021",

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doi = "10.1021/jacsau.1c00226",

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T1 - Insights into the interaction between immobilized biocatalysts and metal–organic frameworks

T2 - a case study of PCN-333

AU - Yang, Wenjie

AU - Liang, Weibin

AU - O'Dell, Luke A.

AU - Toop, Hamish D.

AU - Maddigan, Natasha

AU - Zhang, Xingmo

AU - Kochubei, Alena

AU - Doonan, Christian J.

AU - Jiang, Yijiao

AU - Huang, Jun

N1 - Copyright the Author(s) 2021. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.

PY - 2021/12/27

Y1 - 2021/12/27

N2 - The immobilization of enzymes in metal–organic frameworks (MOFs) with preserved biofunctionality paves a promising way to solve problems regarding the stability and reusability of enzymes. However, the rational design of MOF-based biocomposites remains a considerable challenge as very little is known about the state of the enzyme, the MOF support, and their host–guest interactions upon immobilization. In this study, we elucidate the detailed host–guest interaction for MOF immobilized enzymes in the biointerface. Two enzymes with different sizes, lipase and insulin, have been immobilized in a mesoporous PCN-333(Al) MOF. The dynamic changes of local structures of the MOF host and enzyme guests have been experimentally revealed for the existence of the confinement effect to enzymes and van der Waals interaction in the biointerface between the aluminum oxo-cluster of the PCN-333 and the -NH2 species of enzymes. This kind of host–guest interaction renders the immobilization of enzymes in PCN-333 with high affinity and highly preserved enzymatic bioactivity.[Graphic presents]

AB - The immobilization of enzymes in metal–organic frameworks (MOFs) with preserved biofunctionality paves a promising way to solve problems regarding the stability and reusability of enzymes. However, the rational design of MOF-based biocomposites remains a considerable challenge as very little is known about the state of the enzyme, the MOF support, and their host–guest interactions upon immobilization. In this study, we elucidate the detailed host–guest interaction for MOF immobilized enzymes in the biointerface. Two enzymes with different sizes, lipase and insulin, have been immobilized in a mesoporous PCN-333(Al) MOF. The dynamic changes of local structures of the MOF host and enzyme guests have been experimentally revealed for the existence of the confinement effect to enzymes and van der Waals interaction in the biointerface between the aluminum oxo-cluster of the PCN-333 and the -NH2 species of enzymes. This kind of host–guest interaction renders the immobilization of enzymes in PCN-333 with high affinity and highly preserved enzymatic bioactivity.[Graphic presents]

KW - metal-organic frameworks

KW - enzyme immobilization

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KW - biointerface interaction

KW - biocatalysis

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UR - http://purl.org/au-research/grants/arc/DP170103531

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JF - JACS Au

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ER -

Insights into the interaction between immobilized biocatalysts and metal–organic frameworks: a case study of PCN-333

Abstract

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Keywords

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