Literature reports biocatalytically active static emulsions (BASE) as promising systems for the preparation of biocatalysts designed for synthetic use in organic media. Their excellent catalytic performance is attributed to the numerous micropools of dissolved enzymes independently dispersed in silicone beads. Here, a systematic study of the structure and morphology of BASE and optimization in terms of bead size distribution and overall catalytic performance is presented. The study relies on beads obtained by using a novel preparation method that enables a considerably improved reproducibility of the particle size and catalytic activity in separate batches. A large interfacial area of 0.023 m2 g−1 material was calculated. The adjustment of bead composition increased the apparent catalytic activity of entrapped lipase A from Candida antarctica (CalA) to 0.71 U gBASE−1, which is almost twofold higher than that previously reported. The specific activity remained in the range of prototype BASE (0.21 U mgprotein−1), which nevertheless is about 53 times higher than that reported for CalA entrapped in a sol–gel.