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Synthesis and Characterization of Laccase Enzyme Aggregates From Trametes villosa for Simultaneous Elimination of Rifampicin and Isoniazid

Synthesis and Characterization of Laccase Enzyme Aggregates From Trametes villosa for... Laccase from Trametes villosa was immobilized by CLEAs (cross-linked enzyme aggregates), biochemically characterized and applied for the degradation of the antibiotics rifampicin (RIF) and isoniazid (INH). The extracellular laccase purified by Sephadex G-100 chromatography presented a specific activity of 530.07 U/mg with a purification factor of 6.3-fold. SDS–PAGE followed by zymogram provided a single band, indicating that laccase from T. villosa was a monomeric protein with molecular mass of about 45 kDa. The optimum pH and temperature values for the laccase CLEAs (Lac-CLEAs) were 4.0 and 60 °C, respectively, and they remained more active over a broader range of pH and temperature during 60 min of incubation as compared to the partially purified free form. Lac-CLEAs presented less affinity for ABTS than their corresponding free enzyme, and the values for Km and Vmax were 3.521 mM and 137.0 mM min, respectively. Free laccases and Lac-CLEAs were used for simultaneous biodegradation of 5 mg/L RIF and INH in aqueous solutions. Results obtained by high-performance liquid chromatography (HPLC) revealed that 95% and 94% of RIF were biodegraded by free and immobilized laccase, respectively. Lac-CLEAs degraded more than twofold (71%) the amount of INH degraded by the free enzyme (32%). A microbial susceptibility assay demonstrated a stronger inhibition of Staphylococcus aureus by laccase-treated samples, with lower MIC values in comparison to control samples.Graphical abstract[graphic not available: see fulltext] http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png International Journal of Environmental Research Springer Journals

Synthesis and Characterization of Laccase Enzyme Aggregates From Trametes villosa for Simultaneous Elimination of Rifampicin and Isoniazid

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References (76)

Publisher
Springer Journals
Copyright
Copyright © University of Tehran 2022
ISSN
1735-6865
eISSN
2008-2304
DOI
10.1007/s41742-022-00403-y
Publisher site
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Abstract

Laccase from Trametes villosa was immobilized by CLEAs (cross-linked enzyme aggregates), biochemically characterized and applied for the degradation of the antibiotics rifampicin (RIF) and isoniazid (INH). The extracellular laccase purified by Sephadex G-100 chromatography presented a specific activity of 530.07 U/mg with a purification factor of 6.3-fold. SDS–PAGE followed by zymogram provided a single band, indicating that laccase from T. villosa was a monomeric protein with molecular mass of about 45 kDa. The optimum pH and temperature values for the laccase CLEAs (Lac-CLEAs) were 4.0 and 60 °C, respectively, and they remained more active over a broader range of pH and temperature during 60 min of incubation as compared to the partially purified free form. Lac-CLEAs presented less affinity for ABTS than their corresponding free enzyme, and the values for Km and Vmax were 3.521 mM and 137.0 mM min, respectively. Free laccases and Lac-CLEAs were used for simultaneous biodegradation of 5 mg/L RIF and INH in aqueous solutions. Results obtained by high-performance liquid chromatography (HPLC) revealed that 95% and 94% of RIF were biodegraded by free and immobilized laccase, respectively. Lac-CLEAs degraded more than twofold (71%) the amount of INH degraded by the free enzyme (32%). A microbial susceptibility assay demonstrated a stronger inhibition of Staphylococcus aureus by laccase-treated samples, with lower MIC values in comparison to control samples.Graphical abstract[graphic not available: see fulltext]

Journal

International Journal of Environmental Research – Springer Journals

Published: Jun 1, 2022

Keywords: Antibiotics; Antituberculosis drugs; Cross-linked enzyme aggregates; Trametes villosa; Wastewater treatment

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