Commercial multicomponent enzyme preparations, Ultraflo L, Depol 740L and Depol 670L, with feruloyl esterase activity, were tested for the transesterification of methyl ferulate to 1-butyl ferulate in their free and immobilized form using as a reaction system a ternary water–organic mixture consisting of n-hexane, 1-butanol and water. A number of factors affecting enzymes precipitation and cross-linking into cross-linked enzyme aggregates (CLEAs) have been investigated. Consecutive optimization of the precipitant type and cross-linker concentration resulted in CLEAs showing higher operational stability and synthetic activity compared to the free enzymes’ forms. Under certain optimization conditions, conversion yields of 97%, 87% and 5%, were obtained by CLEAs prepared from Ultraflo L, Depol 740L and Depol 670L, respectively. The activities initially present in the three commercial preparations were completely retained after cross-linking resulting in multipurpose biocatalysts which have the potential to carry out different and independent reactions. This work is consistent to the novel CLEA concept called combi-CLEA.