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Immobilization of Maxilact by cross-linked enzyme aggregates

Miłek J., Verschelde W.

Ars Separatoria Acta

2012/2013

No. 9/10

65--76

Maxilact L2000 (β-galactosidase from Kluyveromyces lactis) was aggregated using ammonium sulphate and the resultant aggregates, on cross-linking with glutaraldehyde, produced an insoluble and catalytically active enzyme. These cross-linked enzyme aggregates (CLEAs) Maxilact were obtained in the optimal conditions. The activity of a biocatalyst, immobilized with the obtained preparation, was 5.89 U/mg. The operating stability of the immobilized Maxilact was determined for 10 successive batches. Residual activity was 8.24 U/mg after 10 cycles of batch operation. The above studies show that moderately stable preparation of catalase can be economically prepared by the cross-linked enzyme aggregates. The preparation and characterization of CLEAs Maxilact is reported for the first time.