A general Ca-MOM platform with enhanced acid-base stability for enzyme biocatalysis
A general Ca-MOM platform with enhanced acid-base stability for enzyme biocatalysis
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DOI：
10.1016/j.checat.2021.03.001
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发表时间：
2021-06-17
期刊：
影响因子：
--
通讯作者：
Yang, Zhongyu
中科院分区：
文献类型：
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作者：
Pan, Yanxiong;Li, Qiaobin;Yang, Zhongyu
在金属-有机框架中共沉淀酶是一种独特的酶固定化策略，但受到弱酸碱稳定性的挑战。为了克服这个缺点，我们发现Ca 2+可以在环境水性条件下与羧酸根配体和酶共沉淀，并形成在宽范围的pH（3.7-9.5）下稳定的酶@金属有机材料复合物。我们证明了这一战略上的四种酶具有不同的等电点，分子量和底物大小的溶菌酶，脂肪酶，葡萄糖氧化酶（GOx），辣根过氧化物酶（HRP），以及集群的HRP和GOx。有趣的是，所研究的酶的催化效率被发现依赖于配体，探测其起源导致酶骨架动力学，配体选择和催化效率之间的相关性。我们的方法解决了水相共沉淀的长期稳定性问题，并且可以推广到与其他酶的生物催化，以使研究和工业都受益。
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@metalorganic 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 bio-catalysis with other enzymes to benefit both research and industry.