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Issue 23, 2012
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Paper-immobilized enzyme as a green microstructured catalyst

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Abstract

The facile and direct introduction of methacryloxy groups into cellulose paper was carried out using a silane coupling technique, leading to the improvement of hydrophobicity and both dry and wet physical strengths of the paper. Immobilization of lipase enzymes onto the methacrylate-modified paper was then accomplished, possibly due to hydrophobic interaction. The as-prepared immobilized lipase on methacrylate-modified paper possessed paper-specific practical utility. During a batch process for the nonaqueous transesterification between 1-phenylethanol and vinyl acetate to produce 1-phenylethylacetate, the paper-immobilized lipase showed high catalytic activity, selectivity and reusability, suggesting that the methacryloxy groups introduced into the cellulose paper played a key role in the hyperactivation of lipases. In addition, a higher productivity of 1-phenylethylacetate was achieved in a continuous flow reaction system than in the batch system, indicating that the interconnected porous microstructure of the paper provided favorable flow paths for the reactant solution. Thus, the paper-immobilized enzyme is expected to offer a green catalytic material for the effective production of useful chemicals.

Graphical abstract: Paper-immobilized enzyme as a green microstructured catalyst

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Supplementary files

Article information


Submitted
08 Feb 2012
Accepted
03 Apr 2012
First published
03 Apr 2012

J. Mater. Chem., 2012,22, 11591-11597
Article type
Paper

Paper-immobilized enzyme as a green microstructured catalyst

H. Koga, T. Kitaoka and A. Isogai, J. Mater. Chem., 2012, 22, 11591
DOI: 10.1039/C2JM30759F

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