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 journalArticlepeer-review

24 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 languageEnglish (US)
Pages (from-to)146-161
Number of pages16
JournalChem Catalysis
Volume1
Issue number1
DOIs
StatePublished - Jun 17 2021

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