Immobilization of Myceliophthora thermophila laccase on poly(glycidyl methacrylate) microspheres enhances the degradation of azinphos‐methyl. Issue 16 (21st December 2018)

• Record Type: Journal Article
• Authors: Vera, Myleidi; Nyanhongo, Gibson S.; Pellis, Alessandro; Rivas, Bernabé L.; Guebitz, Georg M.
• Is Part Of: Journal of applied polymer science. Volume 136:Issue 16(2019)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2018-12-21
• Subjects: catalysts -- degradation -- morphology -- kinetics -- proteins; Polymers -- Periodicals; Polymerization -- Periodicals; 668.9
• DOI: 10.1002/app.47417
• Languages: English
• ISSNs: 0021-8995

Abstract

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. Abstract :