Laccase from Aspergillus sp. (LC) was immobilized within Fe-BTC and ZIF-zni metal organic frameworks through a one-pot synthesis carried out under mild conditions (room temperature and aqueous solution). The Fe-BTC, ZIF-zni MOFs, and the LC@Fe-BTC, LC@ZIF-zni immobilized LC samples were characterized by X-ray diffraction, scanning electron microscopy, Fourier transform infrared spectroscopy, and thermogravimetric analysis. The kinetic parameters (KM and Vmax) and the specific activity of the free and immobilized laccase were determined. Immobilized LCs resulted in a lower specific activity compared with that of the free LC (7.7 µmol min-1 mg-1). However, LC@ZIF-zni was almost 10 times more active than LC@Fe-BTC (1.32 µmol min-1 mg-1 vs 0.17 µmol min-1 mg-1) and only 5.8 times less active than free LC. The effect of enzyme loading showed that LC@Fe-BTC had an optimal loading of 45.2 mg g-1, at higher enzyme loadings the specific activity decreased. In contrast, the specific activity of LC@ZIF-zni increased linearly over the loading range investigated. The storage stability of LC@Fe-BTC was low with a significant decrease in activity after 5 days, while LC@ZIF retained up to 50% of its original activity after 30 days storage. The difference in activity and stability between LC@Fe-BTC and LC@ZIF-zni is likely due to release of Fe3+ and the low stability of Fe-BTC MOF. Together, these results indicate that ZIF-zni is a superior support for the immobilization of laccase.

Enzyme immobilization on metal organic frameworks: Laccase from Aspergillus sp. is better adapted to ZIF-zni rather than Fe-BTC

Tocco D.
Primo
;
Carucci C.
Secondo
;
Todde D.;Sanjust E.
Penultimo
;
Salis A.
Ultimo
2021-01-01

Abstract

Laccase from Aspergillus sp. (LC) was immobilized within Fe-BTC and ZIF-zni metal organic frameworks through a one-pot synthesis carried out under mild conditions (room temperature and aqueous solution). The Fe-BTC, ZIF-zni MOFs, and the LC@Fe-BTC, LC@ZIF-zni immobilized LC samples were characterized by X-ray diffraction, scanning electron microscopy, Fourier transform infrared spectroscopy, and thermogravimetric analysis. The kinetic parameters (KM and Vmax) and the specific activity of the free and immobilized laccase were determined. Immobilized LCs resulted in a lower specific activity compared with that of the free LC (7.7 µmol min-1 mg-1). However, LC@ZIF-zni was almost 10 times more active than LC@Fe-BTC (1.32 µmol min-1 mg-1 vs 0.17 µmol min-1 mg-1) and only 5.8 times less active than free LC. The effect of enzyme loading showed that LC@Fe-BTC had an optimal loading of 45.2 mg g-1, at higher enzyme loadings the specific activity decreased. In contrast, the specific activity of LC@ZIF-zni increased linearly over the loading range investigated. The storage stability of LC@Fe-BTC was low with a significant decrease in activity after 5 days, while LC@ZIF retained up to 50% of its original activity after 30 days storage. The difference in activity and stability between LC@Fe-BTC and LC@ZIF-zni is likely due to release of Fe3+ and the low stability of Fe-BTC MOF. Together, these results indicate that ZIF-zni is a superior support for the immobilization of laccase.
2021
laccase; enzyme; metal organic frameworks; aspergillus; enzyme stability; enzymes immobilized; kinetics
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11584/323359
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