use of an enzyme attached to a cellulosic carrier in organic synthesis is described. cellulose matrix-supported enzymes constitute useful biological catalysts with broad potential applications in the food, chemical, and pharmaceutical industries. in the current investigation, horseradish peroxidases quantitatively converted 2,4, 6-trimethylaniline in highly colored 2,6-dimethylbenzoquinone in a single pass. the latter compound possesses a labile amine group which undergoes mild acid hydrolysis to yield 2,6-dimethylquinone plus a molecule of the starting material. activities of the bound enzyme were compared with the solution enzyme relative to 2,4, 6-trimethylaniline and hydrogen peroxide concentration. results indicate that the cellulosic-supported immobilized preparation is more stable to heat denaturation than its native-state counterpart the method also was applied successfully for immobilization of aldolase, alpha-amylase, and lysozyme. experiments were performed in a hollow fiber reactor which has the advantage of relatively unrestricted flow rates