Immobilization of Maxilact by cross-linked enzyme aggregates

• Autorzy: Miłek J. , Verschelde W.
• Języki publikacji: EN

Abstrakty

EN

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.

Słowa kluczowe

EN

Maxilact; immobilization; cross-linked enzyme aggregates

• Wydawca: Faculty of Chemical Technology and Engineering, University of Technology and Life Sciences, Bydgoszcz
• Czasopismo: Ars Separatoria Acta
• Rocznik: 2012/2013
• Tom: No. 9/10
• Strony: 65--76
• Opis fizyczny: Bibliogr. 14 poz., rys.

Twórcy

autor

Miłek J.

• Department of Chemical and Biochemical Engineering, Faculty of Chemical Technology and Engineering, University of Technology and Life Sciences Seminaryjna 3, 85-326 Bydgoszcz, Poland

autor

Verschelde W.

• Department of Electrical Engineering, Ku Leuven Gebroeders Desmetstraat 1, 9000 Gent, Belgium

Bibliografia

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