Issue 12, 2012
From the journal:

Chemical Science

Enhanced thermostability of enzymes accommodated in thermo-responsive nanopores†

Jia Liu,ab   Shiyang Bai,ab   Qianru Jin,ab   Can Li*a  and  Qihua Yang*a  

* Corresponding authors

a State Key Laboratory of Catalysis, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, P. R. China
E-mail: yangqh@dicp.ac.cn, canli@dicp.ac.cn
Fax: +86-411-84694447
Tel: +86-411-84379552

b Graduate School of the Chinese Academy of Sciences, Beijing, P. R. China

Abstract

The crowded and hydrophobic microenvironment was created for immobilized enzymes via the thermally-initiated shrinkage of PNIPAM polymers anchored in the nanopores of mesoporous silica. This extraordinary microenvironment can greatly enhance both the catalytic efficiency and thermostability of lipases, which provides a new approach for fabricating robust heterogeneous biocatalysts.

Graphical abstract: Enhanced thermostability of enzymes accommodated in thermo-responsive nanopores

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Article information

DOI
https://doi.org/10.1039/C2SC21026F
Article type
Edge Article
Submitted
20 Jul 2012
Accepted
28 Aug 2012
First published
29 Aug 2012

Chem. Sci., 2012,3, 3398-3402

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Enhanced thermostability of enzymes accommodated in thermo-responsive nanopores

J. Liu, S. Bai, Q. Jin, C. Li and Q. Yang, Chem. Sci., 2012, 3, 3398 DOI: 10.1039/C2SC21026F

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