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通过仿生矿化原位杂交酶及其具有增强活性和稳定性的金属有机框架类似物。

In situ hybridization of enzymes and their metal-organic framework analogues with enhanced activity and stability by biomimetic mineralisation.

机构信息

School of Chemistry and Chemical Engineering, South China University of Technology, Guangzhou 510640, China.

出版信息

Nanoscale. 2017 Oct 19;9(40):15298-15302. doi: 10.1039/c7nr06315f.

DOI:10.1039/c7nr06315f
PMID:28991303
Abstract

By incorporating Cytochrome c (peroxidase, Cyt c) into a skeleton of its corresponding synthetic MOF analogue (peroxidase mimic, CuBDC), approximately 12-fold catalytic efficiency (k/K) enhancement is observed compared to free Cyt c. Meanwhile, the shield endowed by CuBDC prevents encapsulated enzymes from deactivation by trypsin digestion, thermal treatment and long-term storage in vitro. This concept of combining enzymes and their MOF mimics with enhanced enzymatic activity and stability may provide new insights into the design of highly active, stable enzyme-MOF composite catalysts and holds promise for applications in biocatalysis, biosensing and drug delivery systems.

摘要

通过将细胞色素 c(过氧化物酶,Cyt c)整合到其相应的合成 MOF 类似物(过氧化物酶模拟物,CuBDC)的骨架中,与游离 Cyt c 相比,观察到大约 12 倍的催化效率(k/K)增强。同时,CuBDC 赋予的屏蔽作用防止包封的酶被胰蛋白酶消化、热处理和体外长期储存失活。将酶与其 MOF 模拟物结合以提高酶活性和稳定性的这种概念可能为设计高活性、稳定的酶-MOF 复合催化剂提供新的见解,并有望在生物催化、生物传感和药物输送系统中得到应用。

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