Endopectinlyase (EC 4.2.2.10), endopolygalacturonase (EC 3.2.1.15) and pectinesterase (EC 3.1.1.11) present in a commercial mixture were co-immobilized on gamma-alumina spheres activated with organophosphate compounds. Staining of the alumina-enzyme complexes with a dye specific for protein showed that only the carrier external surface was available for protein binding. When confined in a packed bed reactor, the activity of the co-immobilized enzymes brought about a viscosity decrease of 70-90% in pectin and polygalacturonic acid solutions, respectively. Sixty per cent of the initial activity was retained from the immobilized enzymes after the sixth utilization cycle on both the substrates used. The immobilized enzymes were also active against fresh apple juice producing a 90% reduction in viscosity in the first five cycles of utilization.