Laccase multi-point covalent immobilization: characterization, kinetics, and its hydrophobicity applications
Autor: | Abdelmageed M. Othman, Ángeles Sanromán, Diego Moldes |
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Rok vydání: | 2023 |
Předmět: | |
Zdroj: | Applied Microbiology and Biotechnology. 107:719-733 |
ISSN: | 1432-0614 0175-7598 |
Popis: | Laccase from Myceliophthora thermophila was immobilized using one-point and multi-point covalent attachment on both a native and a modified new commercial epoxy carrier (Immobead 150P). After 10 cycles of operation at pH 3.0 and temperature 70 °C, the multi-point covalently immobilized laccase on the modified Immobead 150P performed best in terms of immobilization characteristics, retaining 95% of its initial activity. Thermodynamic parameters of thermal inactivation emphasized the positive impact of the immobilization procedure. At 50 °C, the immobilized and free enzyme activity levels dropped by 27 and 73%, respectively, after 48 h of incubation. The immobilized enzyme enhanced its stability in alkaline conditions, resuming 95% of its original activity after 3 h at pH 9.0. Immobilization reduced substrate affinity because the free laccase's K |
Databáze: | OpenAIRE |
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