Immobilization of Laccase from T. versicolor on Nanofiber Matrix

Abstract:

Prepared nanofiber matrices based on polyamide 6 and polyamide 6/chitosan with numerous amine groups were tested on enzyme immobilization. Laccase from Trametes versicolor was immobilized on both nanofiber sheets either via glutaraldehyde and hexamethylenediamine activation, or via adsorption followed by glutaraldehyde crosslinking. Both types of the attachment were successful, however, the adsorption method provided immobilized laccase with enhanced operational stability.

• Periodical: Materials Science Forum (Volume 937)
• Pages: 123-128
• DOI: https://doi.org/10.4028/www.scientific.net/MSF.937.123
• Online since: October 2018
• Authors: Milena Maryšková*, Petra Vaňátková, Markéta Schaabová, Jiří Maryška
• Keywords: Immobilization, Laccase, Nanofiber, Polyamide 6, Polyamide 6/Chitosan

References

[1] M. Clara, B. Strenn, O. Gans, E. Martinez, N. Kreuzinger, and H. Kroiss, Removal of selected pharmaceuticals, fragrances and endocrine disrupting compounds in a membrane bioreactor and conventional wastewater treatment plants,, Water Res., vol. 39, no. 19, p.4797–4807, Nov. (2005).

DOI: 10.1016/j.watres.2005.09.015

[2] M.-K. Kim and K.-D. Zoh, Occurrence and removals of micropollutants in water environment,, Environ. Eng. Res., vol. 21, no. 4, p.319–332, Nov. (2016).

[3] E. J. Toone, Advances in Enzymology and Related Areas of Molecular Biology, Volume 75: Protein Evolution. John Wiley & Sons, (2010).

[4] B. Chefetz, Y. Chen, and Y. Hadar, Purification and Characterization of Laccase fromChaetomium thermophilium and Its Role in Humification,, Appl. Environ. Microbiol., vol. 64, no. 9, p.3175–3179, Sep. (1998).

DOI: 10.1128/aem.64.9.3175-3179.1998

[5] V. Madhavi and S. S. Lele, LACCASE: PROPERTIES AND APPLICATIONS,, BioResources, vol. 4, no. 4, p.1694–1717, Aug. (2009).

[6] W. Tischer and F. Wedekind, Immobilized Enzymes: Methods and Applications,, in Biocatalysis - From Discovery to Application, P. D. W.-D. Fessner, A. Archelas, D. C. Demirjian, R. Furstoss, H. Griengl, K.-E. Jaeger, E. Morís-Varas, R. Öhrlein, M. T. Reetz, J.-L. Reymond, M. Schmidt, S. Servi, P. C. Shah, W. Tischer, and F. Wedekind, Eds. Springer Berlin Heidelberg, 1999, p.95.

DOI: 10.1007/3-540-68116-7

[7] M. Maryšková, I. Ardao, C. A. García-González, L. Martinová, J. Rotková, and A. Ševců, Polyamide 6/chitosan nanofibers as support for the immobilization of Trametes versicolor laccase for the elimination of endocrine disrupting chemicals,, Enzyme Microb. Technol., vol. 89, p.31–38, Jul. (2016).

DOI: 10.1016/j.enzmictec.2016.03.001

[8] L. N. Nguyen et al., Continuous biotransformation of bisphenol A and diclofenac by laccase in an enzymatic membrane reactor,, Int. Biodeterior. Biodegrad., vol. 95, p.25–32, Nov. (2014).

[9] M. de Cazes et al., Design and optimization of an enzymatic membrane reactor for tetracycline degradation,, Catal. Today, vol. 236, p.146–152, Nov. (2014).

DOI: 10.1016/j.cattod.2014.02.051

[10] M. Fernández-Fernández, M. Á. Sanromán, and D. Moldes, Recent developments and applications of immobilized laccase,, Biotechnol. Adv., vol. 31, no. 8, p.1808–1825, Dec. (2013).

DOI: 10.1016/j.biotechadv.2012.02.013

[11] S. Yang, F. I. Hai, L. D. Nghiem, L. N. Nguyen, F. Roddick, and W. E. Price, Removal of bisphenol A and diclofenac by a novel fungal membrane bioreactor operated under non-sterile conditions,, Int. Biodeterior. Biodegrad., vol. 85, p.483–490, Nov. (2013).

DOI: 10.1016/j.ibiod.2013.03.012

[12] R. R. Nair, P. Demarche, and S. N. Agathos, Formulation and characterization of an immobilized laccase biocatalyst and its application to eliminate organic micropollutants in wastewater,, New Biotechnol., vol. 30, no. 6, p.814–823, Sep. (2013).

DOI: 10.1016/j.nbt.2012.12.004

[13] G. Hommes et al., Production of a robust nanobiocatalyst for municipal wastewater treatment,, Bioresour. Technol., vol. 115, p.8–15, Jul. (2012).

[14] G. Songulashvili, G. A. Jimenéz-Tobón, C. Jaspers, and M. J. Penninckx, Immobilized laccase of Cerrena unicolor for elimination of endocrine disruptor micropollutants,, Fungal Biol., vol. 116, no. 8, p.883–889, Aug. (2012).

DOI: 10.1016/j.funbio.2012.05.005

[15] P. Galliker, G. Hommes, D. Schlosser, P. F.-X. Corvini, and P. Shahgaldian, Laccase-modified silica nanoparticles efficiently catalyze the transformation of phenolic compounds,, J. Colloid Interface Sci., vol. 349, no. 1, p.98–105, Sep. (2010).

DOI: 10.1016/j.jcis.2010.05.031

[16] I. Matijošytė, I. W. C. E. Arends, S. de Vries, and R. A. Sheldon, Preparation and use of cross-linked enzyme aggregates (CLEAs) of laccases,, J. Mol. Catal. B Enzym., vol. 62, no. 2, p.142–148, Feb. (2010).

DOI: 10.1016/j.molcatb.2009.09.019

[17] H. Cabana, C. Alexandre, S. N. Agathos, and J. P. Jones, Immobilization of laccase from the white rot fungus Coriolopsis polyzona and use of the immobilized biocatalyst for the continuous elimination of endocrine disrupting chemicals,, Bioresour. Technol., vol. 100, no. 14, p.3447–3458, Jul. (2009).

DOI: 10.1016/j.biortech.2009.02.052

[18] D. S. Tawfik, Directed enzyme evolution: Screening and selection methods. Methods in molecular biology Vol. 230 edited by Frances H. Arnold and George Georgiou. 2003.,, Protein Sci. Publ. Protein Soc., vol. 13, no. 10, p.2836–2837, Oct. (2004).

DOI: 10.1002/cbic.200490009

[19] T. Hassani, S. Ba, and H. Cabana, Formation of enzyme polymer engineered structure for laccase and cross-linked laccase aggregates stabilization,, Bioresour. Technol., vol. 128, p.640–645, Jan. (2013).

DOI: 10.1016/j.biortech.2012.10.058

[20] R. Xu, R. Tang, Q. Zhou, F. Li, and B. Zhang, Enhancement of catalytic activity of immobilized laccase for diclofenac biodegradation by carbon nanotubes,, Chem. Eng. J., vol. 262, p.88–95, Feb. (2015).

DOI: 10.1016/j.cej.2014.09.072

[21] Y. Liu et al., Immobilization of laccase on magnetic bimodal mesoporous carbon and the application in the removal of phenolic compounds,, Bioresour. Technol., vol. 115, p.21–26, Jul. (2012).