Enhancement of catalytic, reusability, and long-term stability features of Trametes versicolor IBL-04 laccase immobilized on different polymers

Asgher, Muhammad; Noreen, Sadia; Bilal, Muhammad

doi:10.1016/j.ijbiomac.2016.11.012

Cited by 87 publications

(26 citation statements)

References 61 publications

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“…As seen in the table, the enzyme‐substrate affinity was reduced after immobilization on PGMA–NH 2 and it was slightly increased in case of PGMA immobilization. This difference could be due to structural changes in the laccase by immobilization procedure and the type enzyme‐support bond formed . Similar results have been reported previously .…”

Section: Resultssupporting

confidence: 87%

Immobilization of Trametes versicolor laccase on different PGMA‐based polymeric microspheres using response surface methodology: Optimization of conditions

Vera

Rivas

2017

J of Applied Polymer Sci

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Enzymatic immobilization is a versatile alternative to improve enzyme stability and enable its reuse. In this study, the change in the immobilized enzyme properties due to the type of functional group on the carrier was evaluated. For that, monodisperse polymeric microspheres with two functional groups widely used in laccase immobilization—oxirane [poly(glycidyl methacrylate) (PGMA)] and hydrazide—were synthesized by dispersion polymerization to covalently immobilize the laccase Trametes versicolor. Using a response surface methodology, laccase immobilization was optimized for each microsphere type. As a result, laccase immobilization on PGMA carriers appears to broaden the pH and temperature ranges, storage stability, and reusability compared to free and hydrazide enzymes. These aforementioned characteristics indicate that PGMA microspheres could act as an ideal support for enzyme immobilization in biotechnological applications. © 2017 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2017, 134, 45249.

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Section: Resultssupporting

confidence: 87%

Immobilization of Trametes versicolor laccase on different PGMA‐based polymeric microspheres using response surface methodology: Optimization of conditions

Vera

Rivas

2017

J of Applied Polymer Sci

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“…4C, free and immobilized laccases were activated by Cu 2+ and Mn 2+ , which might be owing to the stabilization of the active conformation that stimulates the laccase activity. 35 Besides, compared with the free enzyme, immobilized laccases exhibited lower inhibitory effects when exposed to EDTA, SDS, ACN and DMSO, which might be attributed to the theory that the restricted mobility and compacted conformation of the protein chain aer enzyme immobilization could effectively alleviate the cofactor loss and protein unfolding under unfavorable conditions. 35,36 Considering that the storage stability of an enzyme is also an important aspect for practical application, the storage stability of free and immobilized laccases was also investigated at 4 C. As depicted in Fig.…”

Section: Enzymatic Properties Of Free and Immobilized Laccasesmentioning

confidence: 98%

Laccase-immobilized tannic acid-mediated surface modification of halloysite nanotubes for efficient bisphenol-A degradation

Zhang

Tang

et al. 2019

RSC Adv.

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“…Asgher et al reported a slight decrease of K m in gelatin entrapped laccase compared to free laccase. 57 De Cazes et al reported a value of K m five times lower than free laccase when laccase was covalently immobilized on ceramic membranes coated by a glutaraldehyde crosslinked gelatin layer. 58 Thus, the present results confirm that gelatin seems to have a positive effect probably with less diffusional hindrance than traditional inorganic or polymer supports.…”

Section: Enzymatic Activity Stability and Reusabilitymentioning

confidence: 99%

Gelatin supports with immobilized laccase as sustainable biocatalysts for water treatment

Harguindeguy

Antonelli

Belleville

et al. 2020

J of Applied Polymer Sci

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Millimeter‐size beads of gelatin are manufactured by dripping process to give enzyme supports qualified for micropollutants biodegradation in alternative wastewater treatment. The bead diameter is dependent on the tip diameter, the gelatin solution viscosity and the swelling of polymer chains in the collecting bath. Chemical crosslinking was performed with glutaraldehyde using optimal concentration to give mechanical and thermal properties suitable for application in stirred reactor in aqueous medium. Laccases from Trametes versicolor are grafted on the gelatin beads with glutaraldehyde. Sixty percentage of the initial enzymatic activity, evaluated by the oxidation of 2′‐Azino‐bis(3‐ethylbenzothiazoline‐6‐sulfonic acid)diammonium salt (ABTS) is maintained after 10 successive cycles of reaction. Thermal stability at 60°C of immobilized biocatalysts is improved when compared to free enzymes (45% vs 10% of relative activity after 6 h of incubation). The simplicity of the procedure to form gelatin beads and their properties make them promising bio‐based and biodegradable support for enzyme immobilization.

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Enhancement of catalytic, reusability, and long-term stability features of Trametes versicolor IBL-04 laccase immobilized on different polymers

Cited by 87 publications

References 61 publications

Immobilization of Trametes versicolor laccase on different PGMA‐based polymeric microspheres using response surface methodology: Optimization of conditions

Immobilization of Trametes versicolor laccase on different PGMA‐based polymeric microspheres using response surface methodology: Optimization of conditions

Laccase-immobilized tannic acid-mediated surface modification of halloysite nanotubes for efficient bisphenol-A degradation

Gelatin supports with immobilized laccase as sustainable biocatalysts for water treatment

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