A general Ca-MOM platform with enhanced acid-base stability for enzyme biocatalysis

Yanxiong Pan; Qiaobin Li; Hui Li; Jasmin Farmakes; Angel Ugrinov; Xiao Zhu; Zhiping Lai; Bingcan Chen; Zhongyu Yang

doi:10.1016/j.checat.2021.03.001

A general Ca-MOM platform with enhanced acid-base stability for enzyme biocatalysis

Yanxiong Pan, Qiaobin Li, Hui Li, Jasmin Farmakes, Angel Ugrinov, Xiao Zhu, Zhiping Lai, Bingcan Chen, Zhongyu Yang

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

29 Scopus citations

Abstract

Co-precipitation of enzymes in metal-organic frameworks is a unique enzyme-immobilization strategy but is challenged by weak acid-base stability. To overcome this drawback, we discovered that Ca2+ can co-precipitate with carboxylate ligands and enzymes under ambient aqueous conditions and form enzyme@metal-organic material composites stable under a wide range of pHs (3.7–9.5). We proved this strategy on four enzymes with varied isoelectric points, molecular weights, and substrate sizes—lysozyme, lipase, glucose oxidase (GOx), and horseradish peroxidase (HRP)—as well as the cluster of HRP and GOx. Interestingly, the catalytic efficiency of the studied enzymes was found to depend on the ligand, probing the origins of which resulted in a correlation among enzyme backbone dynamics, ligand selection, and catalytic efficiency. Our approach resolved the long-lasting stability issue of aqueous-phase co-precipitation and can be generalized to biocatalysis with other enzymes to benefit both research and industry.

Original language	English (US)
Pages (from-to)	146-161
Number of pages	16
Journal	Chem Catalysis
Volume	1
Issue number	1
DOIs	https://doi.org/10.1016/j.checat.2021.03.001
State	Published - Jun 17 2021

Bibliographical note

KAUST Repository Item: Exported on 2022-03-18
Acknowledgements: This work was supported by the National Science Foundation (grant MCB 1942596 to Z.Y.), North Dakota State University New Faculty Startup Funds, and USDA-NIFA grant 2021-67021-34002 (to B.C.). We appreciate Prof. Hubbell for generously providing the EPR spectral simulation package. Z.L, B.C. and Z.Y. conceived and designed the research. Y.P. and Q.L. performed the synthesis and catalytic assays. Y.P. H.L. and J.F. acquired the EPR data and carried out the data analysis. A.U. and X.Z. assisted in all data analysis and interpretation. All authors participated in drafting the manuscript and gave approval to the final version. The authors declare no competing interests.

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10.1016/j.checat.2021.03.001

Cite this

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title = "A general Ca-MOM platform with enhanced acid-base stability for enzyme biocatalysis",

abstract = "Co-precipitation of enzymes in metal-organic frameworks is a unique enzyme-immobilization strategy but is challenged by weak acid-base stability. To overcome this drawback, we discovered that Ca2+ can co-precipitate with carboxylate ligands and enzymes under ambient aqueous conditions and form enzyme@metal-organic material composites stable under a wide range of pHs (3.7–9.5). We proved this strategy on four enzymes with varied isoelectric points, molecular weights, and substrate sizes—lysozyme, lipase, glucose oxidase (GOx), and horseradish peroxidase (HRP)—as well as the cluster of HRP and GOx. Interestingly, the catalytic efficiency of the studied enzymes was found to depend on the ligand, probing the origins of which resulted in a correlation among enzyme backbone dynamics, ligand selection, and catalytic efficiency. Our approach resolved the long-lasting stability issue of aqueous-phase co-precipitation and can be generalized to biocatalysis with other enzymes to benefit both research and industry.",

author = "Yanxiong Pan and Qiaobin Li and Hui Li and Jasmin Farmakes and Angel Ugrinov and Xiao Zhu and Zhiping Lai and Bingcan Chen and Zhongyu Yang",

note = "KAUST Repository Item: Exported on 2022-03-18 Acknowledgements: This work was supported by the National Science Foundation (grant MCB 1942596 to Z.Y.), North Dakota State University New Faculty Startup Funds, and USDA-NIFA grant 2021-67021-34002 (to B.C.). We appreciate Prof. Hubbell for generously providing the EPR spectral simulation package. Z.L, B.C. and Z.Y. conceived and designed the research. Y.P. and Q.L. performed the synthesis and catalytic assays. Y.P. H.L. and J.F. acquired the EPR data and carried out the data analysis. A.U. and X.Z. assisted in all data analysis and interpretation. All authors participated in drafting the manuscript and gave approval to the final version. The authors declare no competing interests.",

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AU - Pan, Yanxiong

AU - Li, Qiaobin

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AU - Ugrinov, Angel

AU - Zhu, Xiao

AU - Lai, Zhiping

AU - Chen, Bingcan

AU - Yang, Zhongyu

N1 - KAUST Repository Item: Exported on 2022-03-18 Acknowledgements: This work was supported by the National Science Foundation (grant MCB 1942596 to Z.Y.), North Dakota State University New Faculty Startup Funds, and USDA-NIFA grant 2021-67021-34002 (to B.C.). We appreciate Prof. Hubbell for generously providing the EPR spectral simulation package. Z.L, B.C. and Z.Y. conceived and designed the research. Y.P. and Q.L. performed the synthesis and catalytic assays. Y.P. H.L. and J.F. acquired the EPR data and carried out the data analysis. A.U. and X.Z. assisted in all data analysis and interpretation. All authors participated in drafting the manuscript and gave approval to the final version. The authors declare no competing interests.

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N2 - Co-precipitation of enzymes in metal-organic frameworks is a unique enzyme-immobilization strategy but is challenged by weak acid-base stability. To overcome this drawback, we discovered that Ca2+ can co-precipitate with carboxylate ligands and enzymes under ambient aqueous conditions and form enzyme@metal-organic material composites stable under a wide range of pHs (3.7–9.5). We proved this strategy on four enzymes with varied isoelectric points, molecular weights, and substrate sizes—lysozyme, lipase, glucose oxidase (GOx), and horseradish peroxidase (HRP)—as well as the cluster of HRP and GOx. Interestingly, the catalytic efficiency of the studied enzymes was found to depend on the ligand, probing the origins of which resulted in a correlation among enzyme backbone dynamics, ligand selection, and catalytic efficiency. Our approach resolved the long-lasting stability issue of aqueous-phase co-precipitation and can be generalized to biocatalysis with other enzymes to benefit both research and industry.

AB - Co-precipitation of enzymes in metal-organic frameworks is a unique enzyme-immobilization strategy but is challenged by weak acid-base stability. To overcome this drawback, we discovered that Ca2+ can co-precipitate with carboxylate ligands and enzymes under ambient aqueous conditions and form enzyme@metal-organic material composites stable under a wide range of pHs (3.7–9.5). We proved this strategy on four enzymes with varied isoelectric points, molecular weights, and substrate sizes—lysozyme, lipase, glucose oxidase (GOx), and horseradish peroxidase (HRP)—as well as the cluster of HRP and GOx. Interestingly, the catalytic efficiency of the studied enzymes was found to depend on the ligand, probing the origins of which resulted in a correlation among enzyme backbone dynamics, ligand selection, and catalytic efficiency. Our approach resolved the long-lasting stability issue of aqueous-phase co-precipitation and can be generalized to biocatalysis with other enzymes to benefit both research and industry.

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A general Ca-MOM platform with enhanced acid-base stability for enzyme biocatalysis

Abstract

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CCDC 1987259: Experimental Crystal Structure Determination : catena-((mu-terephthalato)-(mu-aqua)-diaqua-calcium(ii))

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A general Ca-MOM platform with enhanced acid-base stability for enzyme biocatalysis

Abstract

Bibliographical note

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CCDC 1987259: Experimental Crystal Structure Determination : catena-((mu-terephthalato)-(mu-aqua)-diaqua-calcium(ii))

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