beta-Fructofuranosidases from Aspergillus niger ATCC 20611 and Aspergillus japonicus TIT-KJ1 were purified and immobilized covalently onto methacrylamide-based polymeric beads. The porous, oxriane-containing support was reactive and could bind enzymes in a buffered solution at room temperature with a density up to 0.4 mg of protein g(-1) of support with 100% immobilized yield. Neither the optimum temperature for the highest enzymatic activities nor the batch reaction pattern for fructooligosaccharides formation catalyzed by beta-fructofuranosidases was changed by immobilization. The amount of fructooligosaccharides produced from 50% (w/w) sucrose solution using the prepared immobilized enzymes was determined to be approximately 60% of the total sugars in the reaction mixtures. This level of fructooligosaccharides produced by the immobilized enzymes was comparable to that resulting from processes employing other immobilized biocatalysts as shown in the literature. The fraction of total fructooligosaccharides presented in the final mixture increased with the initial sucrose concentration, while fractions of glucose and fructose decreased with an increase sucrose concentration.