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Abstract
The cross-linked enzyme aggregate (CLEA) method is used for the dual purpose of combining
both the purification and immobilization of enzyme in one step. The present work involved
the preparation of a carrier-free, highly active reusable biocatalyst (nitrilase)
which encounters least mass-transfer limitations with higher thermal and storage stability.
The effect of type of aggregating agent, its concentration as well as that of cross-linking
agent was studied. Nitrilase aggregates were prepared using ammonium sulphate (35%)
precipitation followed by cross-linking with glutaraldehyde (125 mM) which rendered
70% activity retention. The various cross-linking parameters were optimized in order
to increase the activity retention. Stability in terms of temperature, reusability
and leaching were also examined. The CLEA preparation showed residual nitrilase activity
on repeated use. A highly stable CLEA of nitrilase was finally prepared with maximum
activity recovery.
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