Immobilization of laccase from the white rot fungus Coriolopsis polyzona and use of the immobilized biocatalyst for the continuous elimination of endocrine disrupting chemicals

Cabana, Hubert; Alexandre, Céline; Agathos, Spiros N.; Jones, J. Peter

doi:10.1016/j.biortech.2009.02.052

Cited by 121 publications

(69 citation statements)

References 51 publications

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“…Additionally, the biocatalyst retained 84% of its initial activity after the treatment and negligible leaching of the immobilised enzyme was detected during the operation. Similar results were reported by Cabana et al (2009) during the elimination of 5 mg/l of nonylphenol, bisphenol A and triclosan in a PBR by laccase covalently immobilised on Celite R-633 supports. The adsorption of those compounds on the support with inactivated laccase varied from 40 to 60% and this physical removal was also linked to the solubility and hydrophobicity of the different EDCs.…”

Section: Decolourisation Of a Model Synthetic Dye By Immobilised Laccasesupporting

confidence: 87%

“…pH (2-8) and temperature (20-80°C) were tested with 50 lM ABTS in 0.1 M citrate-phosphate-borate laccase activity (31.9 and 15.1%). Similar conclusions were attained with Coriolopsis polyzona laccase immobilised through the formation of cross-linked aggregates (Cabana et al 2007) and covalently immobilised on Celite R-33 support (Cabana et al 2009) and with Trametes pubescens laccase immobilised on alumina pellets (Osma et al 2010). …”

Section: Stability Against Chemical Inactivationsupporting

confidence: 71%

“…The continuous elimination of EDCs by immobilised laccase has been reported for bisphenol A using laccase carried on nylon membrane (Diano et al 2007) and covalently bound onto alkylaminated controlled porosity glass (Iida et al 2002). Cabana et al (2007Cabana et al ( , 2009) tested the elimination of bisphenol A, triclosan and nonylphenol by laccase immobilised through the formation of crosslinked enzyme aggregates and on support Celite R-633. In our study, E1, E2 and EE2 were degraded for the first time by Myceliophthora thermophila laccase immobilised on Eupergit C 250L support.…”

Section: Decolourisation Of a Model Synthetic Dye By Immobilised Laccasementioning

confidence: 99%

“…Furthermore, immobilisation may shift the enzyme properties such as the kinetic parameters and the optimum values of pH and temperature. It may also strengthen the protein structure (Cabana et al 2009;Durán et al 2002).…”

Section: Introductionmentioning

confidence: 99%

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Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

et al. 2011

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Laccase from Myceliophthora thermophila was covalently immobilised on Eupergit C and Eupergit C 250L yielding specific activities of up to 17 and 80 U/g, respectively. Due to its superior activity, Eupergit C 250L was chosen for further research. The somewhat lower catalytic efficiency (based on the ratio between the turnover number and the Michaelis constant, k cat /K M ) of the immobilised enzyme in comparison with that of the free enzyme was balanced by its increased stability and broader operational window related to temperature and pH. The feasibility of the immobilised laccase was tested by using a packed bed reactor (PBR) operating in consecutive cycles for the removal of Acid Green 27 dye as model substrate. High degrees of elimination were achieved (88, 79, 69 and 57% in 4 consecutive cycles), while the levels of adsorption on the support varied from 18 to 6%, proving that dye removal took place mainly due to the action of the enzyme. Finally, a continuous PBR with the solid biocatalyst was applied for the treatment of a solution containing the following endocrine disrupting chemicals: estrone (E1), 17b-estradiol (E2) and 17a-ethinylestradiol (EE2). At steady-state operation, E1 was degraded by 65% and E2 and EE2 were removed up to 80% and only limited adsorption of these compounds on the support, between 12 and 22%, was detected. In addition, a 79% decrease in estrogenic activity was detected in the effluent of the enzymatic reactor while only 14% was attained by inactivated laccase.

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Section: Decolourisation Of a Model Synthetic Dye By Immobilised Laccasesupporting

confidence: 87%

Section: Stability Against Chemical Inactivationsupporting

confidence: 71%

Section: Decolourisation Of a Model Synthetic Dye By Immobilised Laccasementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

et al. 2011

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“…[1][2][3] In LAM, hallmark cystic destruction of the pulmonary parenchyma impairs lung function and induces debilitating dyspnea. 4,5 In most patients, hypoxemia develops within a decade of symptom onset.…”

mentioning

confidence: 99%

St. George's Respiratory Questionnaire Has Longitudinal Construct Validity in Lymphangioleiomyomatosis

Swigris

Lee

Inoue

et al. 2013

Chest

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Immobilizing white‐rot fungi laccase: Toward bio‐derived supports as a circular economy approach in organochlorine removal

Serbent,

Magario,

Saux

2023

Biotech & Bioengineering

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Despite their high persistence in the environment, organochlorines (OC) are widely used in the pharmaceutical industry, in plastics, and in the manufacture of pesticides, among other applications. These compounds and the byproducts of their decomposition deserve attention and efficient proposals for their treatment. Among sustainable alternatives, the use of ligninolytic enzymes (LEs) from fungi stands out, as these molecules can catalyze the transformation of a wide range of pollutants. Among LEs, laccases (Lac) are known for their efficiency as biocatalysts in the conversion of organic pollutants. Their application in biotechnological processes is possible, but the enzymes are often unstable and difficult to recover after use, driving up costs. Immobilization of enzymes on a matrix (support or solid carrier) allows recovery and stabilization of this catalytic capacity. Agricultural residual biomass is a passive environmental asset. Although underestimated and still treated as an undesirable component, residual biomass can be used as a low‐cost adsorbent and as a support for the immobilization of enzymes. In this review, the adsorption capacity and immobilization of fungal Lac on supports made from residual biomass, including compounds such as biochar, for the removal of OC compounds are analyzed and compared with the use of synthetic supports. A qualitative and quantitative comparison of the reported results was made. In this context, the use of peanut shells is highlighted in view of the increasing peanut production worldwide. The linkage of methods with circular economy approaches that can be applied in practice is discussed.

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Immobilization of laccase from the white rot fungus Coriolopsis polyzona and use of the immobilized biocatalyst for the continuous elimination of endocrine disrupting chemicals

Cited by 121 publications

References 51 publications

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

St. George's Respiratory Questionnaire Has Longitudinal Construct Validity in Lymphangioleiomyomatosis

Immobilizing white‐rot fungi laccase: Toward bio‐derived supports as a circular economy approach in organochlorine removal

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