Jump to main content
Jump to site search

Issue 23, 2012
Previous Article Next Article

Paper-immobilized enzyme as a green microstructured catalyst

Author affiliations


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

Back to tab navigation

Supplementary files

Publication details

The article was received on 08 Feb 2012, accepted on 03 Apr 2012 and first published on 03 Apr 2012

Article type: Paper
DOI: 10.1039/C2JM30759F
J. Mater. Chem., 2012,22, 11591-11597

  •   Request permissions

    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

Search articles by author