Kinetic and thermodynamic study of laccase cross-linked onto glyoxyl Immobead 150P carrier: Characterization and application for beechwood biografting

[Display omitted] •The surface epoxy groups of Immobead 150P carrier were modified to produce active glyoxyl groups.•The animated laccase was immobilized on the modified Immobead 150P surface via cross-linking.•Optimum conditions, stability, and kinetics of free and cross-linked laccases were assess...

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Veröffentlicht in:Enzyme and microbial technology 2021-10, Vol.150, p.109865-109865, Article 109865
Hauptverfasser: Othman, Abdelmageed M., Sanromán, Maria Ángeles, Moldes, Diego
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Sprache:eng
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Zusammenfassung:[Display omitted] •The surface epoxy groups of Immobead 150P carrier were modified to produce active glyoxyl groups.•The animated laccase was immobilized on the modified Immobead 150P surface via cross-linking.•Optimum conditions, stability, and kinetics of free and cross-linked laccases were assessed.•A highly stable bonded hydrophobic compound was grafted on wood samples using immobilized laccase. In this study, we cross-linked aminated Thermothelomyces thermophilus laccase onto Immobead 150P epoxy carrier, and achieved an immobilization yield of 99.84 %. The optimum temperature and pH values for the oxidation of ABTS by laccase were determined to be 70 °C and pH 3.0. After 6 h at 50 °C, laccase activity was diminished by about 13 % in the free form and 28 %, in the immobilized form. Km values for both free and cross-linked laccase were 0.051 and 0.567 mM, whereas Vmax values were 2.027 and 0.854 μmol. min−1, respectively. The immobilized laccase was able to preserve its full activity for 6 weeks, retaining approximately 95 % and 78 % of its initial activity after 8 and 20 weeks, respectively. The contact angles were two-fold higher when the laccase enzyme was occupied in the biografting reaction, revealing that the hydrophobic compound bonded stably onto beechwood samples.
ISSN:0141-0229
1879-0909
DOI:10.1016/j.enzmictec.2021.109865