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- W3159968678 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 [email protected] 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." @default.
- W3159968678 created "2021-05-10" @default.
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- W3159968678 date "2021-06-01" @default.
- W3159968678 modified "2023-10-15" @default.
- W3159968678 title "A general Ca-MOM platform with enhanced acid-base stability for enzyme biocatalysis" @default.
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- W3159968678 doi "https://doi.org/10.1016/j.checat.2021.03.001" @default.
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