Degradation of Bisphenol A by cross-linked laccase aggregates in a continuously operated membrane reactor and implications of its modeling

Junghanns, Charles;Soete, Bastien;Demarche, Philippe;Nair, Rakesh;Agathos, Spiros N.
(2010) 5th European meeting in Oxizymes — Location: Leipzig, Germany (14.June.2010)

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  • Junghanns, CharlesUCLouvain
    Author
  • Soete, BastienUCLouvain
    Author
  • Demarche, PhilippeUCLouvain
    Author
  • Nair, RakeshUCLouvain
    Author
  • Agathos, Spiros N.orcid-logoUCLouvain
    Author
Abstract
Laccases (E.C. 1.10.3.2) are very well known to oxidise a wide variety of xenobiotics, including micropollutants such as nonylphenol and bisphenol A (BPA). However, their application in continuous reactor systems is hampered by difficulties in separation, recycling and reuse. Binding to or encapsulation in a support, or cross-linking of the protein molecules are ways to overcome these difficulties. A disadvantage of carrier-bound enzymes is the dilution of catalytic activity resulting from the large amount of non-catalytic support material. Thus, the third type of immobilisation, via cross-linking of enzyme molecules with a bifunctional agent has gained attention as it does not suffer from these drawbacks and the biocatalyst formed consists almost entirely of active enzyme (cross-linked enzyme aggregates, CLEAs). By cross-linking laccases from the white-rot fungus Coriolopsis polyzona (strain MUCL 38443) using polyethylene glycol and glutaraldehyde, it was possible to obtain CLEAs with a uniform size of 1-2 µm in diameter suitable for an application in a lab-scale membrane reactor (membrane pore size 0.2 µm, total volume 50 mL, hydraulic retention time 111 min). The reactor was continuously fed with a BPA-solution (50 µM), from which the BPA was successfully removed for up to three days without significant washout of the CLEAs. A mathematical model was developed to describe the time course of BPA concentration and enzyme activity. The model was optimised by the implementation of terms for enzyme inactivation and will serve as a rational basis for an upscaling of the reactor system used.
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Junghanns, C., Soete, B., Demarche, P., Nair, R., & Agathos, S. N. (2010). Degradation of Bisphenol A by cross-linked laccase aggregates in a continuously operated membrane reactor and implications of its modeling. 5th European meeting in Oxizymes, Leipzig, Germany. https://hdl.handle.net/2078.5/214884