4.8 Article

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

期刊

NANOSCALE
卷 9, 期 40, 页码 15298-15302

出版社

ROYAL SOC CHEMISTRY
DOI: 10.1039/c7nr06315f

关键词

-

资金

  1. National Natural Science Foundation of China [21476086, 21706079]
  2. Fundamental Research Funds for the Central Universities [2017BQ060]

向作者/读者索取更多资源

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(cat)/K-M) 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.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.8
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据