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Porous cross-linked enzyme aggregates (p-CLEAs) were prepared by adding starch as a pore-making agent, which facilitates CLEAs in cases where the substrates of enzyme are macromolecules. This novel strategy for preparation of p-CLEAs involves co-precipitation, cross-linking and removal of starch by α-amylase. The resulting papain p-CLEAs were characterized by scanning electron microscope (SEM) images, showing a porous structure. The 95.9% and 90.4% increased catalytic efficiencies of p-CLEAs than conventional CLEAs on bovine serum albumin (BSA) and ovalbumin verified the feasibility of this protocol.
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