Laccase from Trametes versicolor was immobilized on Amberlite IR-120 H beads. Maximum immobilization obtained was 78.7% at pH = 4.5 and temperature T = 45 degrees C. Kinetic parameters, K-m and V-max values, were determined respectively as 0.051 mM and 2.77 x 10(-2) mM/s for free and 4.70 mM and 5.27 x 10(-3) mM/s for immobilized laccase. The Amberlite-laccase system showed a 30% residual activity after 7 cycles. On the other hand, the loss of activity for free laccase after 7 days of storage at 4 degrees C was 18.5% in comparison to Amberlite-laccase system with a loss of 1.4%, during the same period. Improved operational, thermal and storage stabilities of the immobilized laccase were obtained compared to the free counterpart. Therefore, the use of low-cost matrices, like Amberlite for enzyme immobilization represents a promising product for enzymatic industrial applications. (C) 2012 Elsevier Ltd. All rights reserved.

Spinelli, D., Fatarella, E., Di Michele, A., Pogni, R. (2013). Immobilization of fungal (Trametes versicolor) laccase onto Amberlite IR-120 H beads: Optimization and characterization. PROCESS BIOCHEMISTRY, 48(2), 218-223 [10.1016/j.procbio.2012.12.005].

Immobilization of fungal (Trametes versicolor) laccase onto Amberlite IR-120 H beads: Optimization and characterization

Spinelli, Daniele;Pogni, Rebecca
2013-01-01

Abstract

Laccase from Trametes versicolor was immobilized on Amberlite IR-120 H beads. Maximum immobilization obtained was 78.7% at pH = 4.5 and temperature T = 45 degrees C. Kinetic parameters, K-m and V-max values, were determined respectively as 0.051 mM and 2.77 x 10(-2) mM/s for free and 4.70 mM and 5.27 x 10(-3) mM/s for immobilized laccase. The Amberlite-laccase system showed a 30% residual activity after 7 cycles. On the other hand, the loss of activity for free laccase after 7 days of storage at 4 degrees C was 18.5% in comparison to Amberlite-laccase system with a loss of 1.4%, during the same period. Improved operational, thermal and storage stabilities of the immobilized laccase were obtained compared to the free counterpart. Therefore, the use of low-cost matrices, like Amberlite for enzyme immobilization represents a promising product for enzymatic industrial applications. (C) 2012 Elsevier Ltd. All rights reserved.
2013
Spinelli, D., Fatarella, E., Di Michele, A., Pogni, R. (2013). Immobilization of fungal (Trametes versicolor) laccase onto Amberlite IR-120 H beads: Optimization and characterization. PROCESS BIOCHEMISTRY, 48(2), 218-223 [10.1016/j.procbio.2012.12.005].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/45688
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