Immobilization of Myceliophthora thermophila laccase on poly(glycidyl methacrylate) microspheres enhances the degradation of azinphos‐methyl

Abstract

Laccase enzymes are multicopper oxidases capable of oxidizing different compounds. However, to be able to use this biocatalyst for industrial applications, their immobilization is needed. The present work investigates the immobilization of Myceliophthora thermophila laccase (MtL) on monodisperse microspheres of poly(glycidyl methacrylate) (PGMA) to be used in azinphos‐methyl degradation. The immobilization was optimized to achieve the highest activity of the immobilized enzyme. As result, the protein load obtained was 2.5 mg protein g−1 carrier (35 U g−1 of carrier). The immobilized enzymes showed a broadened pH and temperature range of optimum activity and significantly improved the storage and operational stability. Finally, the complete degradation of azinphos‐methyl using immobilized laccase was achieved after 1 h of reaction. The collected data indicate that the immobilization of MtL on PGMA microspheres is an excellent alternative to improve biochemical properties in the enzyme and to allow their efficient use in pesticides degradation. © 2018 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2019, 136, 47417.

Mitigation of bisphenol A using an array of laccase-based robust bio-catalytic cues – A review

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Polymer supports for the removal and degradation of hazardous organic pollutants: an overview

“…Among the most important properties of polymers for immobilization are thermal and physical properties and the presence of functional groups. The thermal properties of polymers are a highly important feature in immobilized enzyme systems since enzymes usually have higher catalytic capacity at high temperatures than at room temperature …”

Multienzymatic immobilization of laccases on polymeric microspheres: A strategy to expand the maximum catalytic efficiency

“…This percentage was determined in previous studies to avoid interference due to blockage of the active site or aggregations between molecules due to immobilization. [20] The immobilization procedure was the same as performed for the immobilization of the single laccases (described previously). Finally, the coimmobilized laccases were characterized and compared with the free and single immobilized laccases.…”

“…The parameters were determined from the Lineweaver-Burk plot as detailed before. [20] 2.7 | Reusability and storage stability…”