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In this work, porous cross-linked enzyme aggregates (p-CLEAs) of Saccharomyces cerevisiae invertase are reported for the first time. Porous CLEAs were prepared by adding starch as a pore-making agent in crude invertase solution and co-precipitating with invertase using ammonium sulfate as a precipitating agent. The resultant co-precipitate was cross-linked for 8 h with 20 mM glutaraldehyde and in the end starch was removed by alpha amylase. The highest catalytic efficiency was obtained at 0.4% (w/v) starch. The scanning electron microscopy analysis of invertase p-CLEAs showed a porous structure. The p-CLEAs were shown to have improved internal mass transfer compared to conventional CLEAs.

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