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Issue 12, 2012
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Enhanced thermostability of enzymes accommodated in thermo-responsive nanopores

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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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Publication details

The article was received on 20 Jul 2012, accepted on 28 Aug 2012 and first published on 29 Aug 2012


Article type: Edge Article
DOI: 10.1039/C2SC21026F
Citation: 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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