Paper-immobilized enzyme as a green microstructured catalyst

Hirotaka Koga, Takuya Kitaoka, Akira Isogai

Research output: Contribution to journalArticlepeer-review

27 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)11591-11597
Number of pages7
JournalJournal of Materials Chemistry
Issue number23
Publication statusPublished - Jun 21 2012

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Materials Chemistry


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