Two enzymes, lipase and β-galactosidase, have been encapsulated within
sol-gel matrices. Enzymatic activity of encapsulated lipase for hydrolysis
and trans-esterification reactions is maintained. Encapsulation yields
depend not only on the sol-gel porous texture but also on the water amount
added for the sol-gel synthesis and the hydratation history of the enzyme.
When the water amount is low, the highly active enzyme conformation
generated by the phase separation is frozen during gelation.
Escherichia Coli have been also encapsulated. The
cellular organization appears to be well preserved. Their β-galactosidase
activity seems to be better in wet gels but decreases dramatically upon
drying.
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