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.