The Immobilization of Laccase on Mixed Polymeric Microspheres for Methyl Red Decomposition
Source abstract
Abstract
Means of eliminating water pollutants or transforming them into less hazardous compounds by green catalysis are desired. The current work was developed with the goal of discovering supports suited for laccase (Lc) immobilization. The effect of the chitosan (CS) molecular weight (Mw) or the polyacrylic acid (PAA) addition was evaluated in microsphere formulation and enzyme immobilization by ESEM, rheology, operational stability, and kinetics. As a practical application, the synthesized products were tested in the methyl red (MR) decomposition and the product identification was performed by high-resolution mass spectrometry. Depending on the required properties, the laccase activity profile (pH, temperature, storage, and Michaelis–Menten parameters) and rheological strength can be modulated by varying the molecular mass of CS or by adding PAA in the support formulation. The immobilized products having the best features regarding MR degradation and recycling abilities were the medium Mw CS microspheres and the system with low Mw CS complexed by PAA, respectively. The degradation mechanism of the dye was proposed accordingly with the identified products by mass spectroscopy. The findings emphasize the potential of the proposed immobilization products to be exploited as viable biocatalysts for dye-contaminated water.
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Research context
OpenAlex topics: Enzyme-mediated dye degradation · Electrochemical sensors and biosensors · Analytical chemistry methods development
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
“Ilie Murgulescu” Institute of Physical Chemistry, Romanian Academy, 060021 Bucharest, Romania
Department of Physical Chemistry, Faculty of Chemistry, University of Bucharest, 030018 Bucharest, Romania
National Institute for Research and Development in Chemistry and Petrochemistry—ICECHIM, 060021 Bucharest, Romania
Department of Organic Chemistry “Costin Nenițescu”, Faculty of Applied Chemistry and Materials Science, University Politehnica of Bucharest, 011061 Bucharest, Romania
Funding
Ministry of Research, Innovation and Digitization
References (59)
Show source-provided references
1. A simulation-optimization approach to integrate process design and planning decisions under technical and market uncertainties: A case from the chemical-pharmaceutical industry10.1016/j.compchemeng.2017.04.008 ↗
2. Guangorena Zarzosa, G.I., and Kobayashi, T. (2022). Sustainable Polymer Used as Renewable Source for Medical Industry. Encyclopedia of Materials: Plastics and Polymers, Elsevier.10.1016/B978-0-12-820352-1.00235-2 ↗
3. Santos, A.S., Raydan, D., Cunha, J.C., Viduedo, N., Silva, A.M.S., and Marques, M.M.B. (2021). Advances in green catalysis for the synthesis of medicinally relevant N-heterocycles. Catalyst, 11.10.3390/catal11091108 ↗
4. Islama, S., Basumatary, B., Rokhum, S.L., Mochahari, P., and Basumatary, S. (2022). Advancement in utilization of nanomaterials as efficient and recyclable solid catalyst for biodiesel synthesis. Chem. Eng. Technol., 3.10.1016/j.clce.2022.100043 ↗
5. Harnessing the biocatalytic attributes and applied perspectives of nanoengineered laccases—A review10.1016/j.ijbiomac.2020.10.195 ↗
6. Martínková, L., Křístková, B., and Křen, V. (2022). Laccases and Tyrosinases in Organic Synthesis. Int. J. Mol. Sci., 23.10.3390/ijms23073462 ↗
7. Dăscălescu, D., and Apetrei, C. (2022). Development of a Novel Electrochemical Biosensor Based on Organized Mesoporous Carbon and Laccase for the Detection of Serotonin in Food Supplements. Chemosensors, 10.10.3390/chemosensors10090365 ↗
8. Dahiya, D., and Nigam, P.S. (2022). Sustainable Biosynthesis of Esterase Enzymes of Desired Characteristics of Catalysis for Pharmaceutical and Food Industry Employing Specific Strains of Microorganisms. Sustainability, 14.10.3390/su14148673 ↗
9. Laccase-mediated synthesis of bioactive natural products and their analogues10.1039/D1CB00259G ↗
10. Othman, A.M., Sanroman, A., and Molde, D. (2022). Laccase-Oriented Immobilization Using Concanavalin A as an Approach for Efficient Glycoproteins Immobilization and Its Application to the Removal of Aqueous Phenolics. Sustainability, 14.10.3390/su142013306 ↗
11. Cost analysis in laccase production10.1016/j.jenvman.2011.06.052 ↗
12. Arregui, L., Ayala, M., Gómez-Gil, X., Gutiérrez-Soto, G., Hernández-Luna, C.E., De los Santos, M.H., Levin, L., Rojo-Domínguez, A., Romero-Martínez, D., and Saparrat, M.C.N. (2019). Laccases: Structure, function, and potential application in water bioremediation. Microb. Cell Fact., 18.10.1186/s12934-019-1248-0 ↗
13. Potential of different enzyme immobilization strategies to improve enzyme performance10.1002/adsc.201100163 ↗
14. Polymer/Enzyme Composite Materials-Versatile Catalysts with Multiple Applications10.3390/chemistry4040087 ↗
15. Silva, A.R.M., Alexandre, J.Y.N.H., Souza, J.E.S., Lima Neto, J.G., de Sousa Júnior, P.G., Rocha, M.V.P., and dos Santos, J.C.S. (2022). The Chemistry and Applications of Metal-Organic Frameworks (MOFs) as Industrial Enzyme Immobilization Systems. Molecules, 27.10.3390/molecules27144529 ↗
16. Immobilization as a strategy for improving enzyme properties- Application to oxidoreductases10.3390/molecules19078995 ↗
17. Santa Cruz Matins de Queiroz, A., Fook, B.R.P.L., De Oliveira Lima, V.A., De Farias Rached, R.I., Lima, E.P.N., Da Silva Lima, R.J., Covas, C.A.P., and Fook, M.V.L. (2017). Preparation and characterization of chitosan obtained from shells of shrimp (Litopenaeus vannamei Boone). Mar. Drugs, 15.10.3390/md15050141 ↗
18. Recent insights into the extraction, characterization, and bioactivities of chitin and chitosan from insects10.1016/j.tifs.2020.08.016 ↗
19. Isolation and Characterization of Chitosans from Different Fungi with Special Emphasis on Zygomycetous Dimorphic Fungus Benjaminiella poitrasii: Evaluation of Its Chitosan Nanoparticles for the Inhibition of Human Pathogenic Fungi10.1021/acs.biomac.1c01248 ↗
20. Pellis, A., Guebitz, G.M., and Nyanhongo, G.S. (2022). Chitosan: Sources, Processing and Modification Techniques. Gels, 8.10.3390/gels8070393 ↗
21. Preparation of chitosan particles suitable for enzyme immobilization10.1016/j.jprot.2007.11.005 ↗
22. Degórska, O., Zdarta, J., Synoradzki, K., Zgola-Grzeskowiak, A., Ciesielczyk, F., and Jesionowski, T. (2021). From core-shell like structured zirconia/magnetite hybrid towards novel biocatalytic systems for tetracycline removal: Synthesis, enzyme immobilization, degradation and toxicity study. J. Environ. Chem. Eng., 9.10.1016/j.jece.2021.105701 ↗
23. Preparation and characterization of chitosan-poly(acrylic acid) polymer magnetic microspheres10.1016/j.polymer.2006.05.017 ↗
24. Laccase immobilized on chitosan-polyacrylic acid microspheres as highly efficient biocatalyst for naphthol green B and indigo carmine degradation10.1016/j.cej.2022.135654 ↗
25. Song, X., Chen, Y., Zhao, G., Sun, H., Che, H., and Leng, X. (2020). Effect of molecular weight of chitosan and its oligosaccharides on antitumor activities of chitosan-selenium nanoparticles. Carbohydr. Polym., 231.10.1016/j.carbpol.2019.115689 ↗
26. Tai, K., Rappolt, M., Mao, L., Gao, Y., Li, X., and Yuan, F. (2020). The stabilization and release performances of curcumin-loaded liposomes coated by high and low molecular weight chitosan. Food Hydrocoll., 99.10.1016/j.foodhyd.2019.105355 ↗
27. Ahmad, M.A., Ahmed, N.B., Adegoke, K.A., and Bello, O.S. (2019). Sorption studies of methyl red dye removal using lemon grass (Cymbopogon citratus). Chem. Data Collect., 22.10.1016/j.cdc.2019.100249 ↗
28. Takkar, S., Tyagi, B., Kumar, N., Kumari, T., Iqbal, K., Varma, A., Thakur, I.S., and Mishra, A. (2022). Biodegradation of methyl red dye by a novel actinobacterium Zhihengliuella sp. ISTPL4: Kinetic studies, isotherm and biodegradation pathway. Environ. Technol. Innov., 26.10.1016/j.eti.2022.102348 ↗
29. New insights into the self-assembling of some hydrophobically modified polyacrylates in aqueous solution10.1007/s00396-015-3825-z ↗
30. Novel enzymatic oxidation of Mn2+ to Mn3+ catalyzed by a fungal laccase10.1016/S0014-5793(99)00566-9 ↗
31. Liu, Y., Yan, M., Geng, Y., and Huang, J. (2015). ABTS-modified silica nanoparticles as laccase mediators for decolorization of indigo carmine dye. J. Chem., 2015.10.1155/2015/670194 ↗
32. Aricov, L., Leonties, A.R., Gîfu, I.C., Preda, D., Raducan, A., and Anghel, D.F. (2020). Enhancement of laccase immobilization onto wet chitosan microspheres using an iterative protocol and its potential to remove micropollutants. J. Environ. Manag., 276.10.1016/j.jenvman.2020.111326 ↗
33. Copper active sites in biology10.1021/cr400327t ↗
34. AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading10.1002/jcc.21334 ↗
35. Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-Å resolution containing a full complement of coppers10.1074/jbc.M204571200 ↗
36. Frisch, M.J., Trucks, G.W., Schlegel, H.B., Scuseria, G.E., Robb, M.A., Cheeseman, J.R., Montgomery, J.A., Vreven, T., Kudin, K.N., and Burant, J.C. (2004). Gaussian 03, Revision C.01, Gaussian, Inc.
37. Precupas, A., Leonties, A.R., Neacsu, A., Angelescu, D.G., and Popa, V.T. (2022). Bovine hemoglobin thermal stability in the presence of naringenin: Calorimetric, spectroscopic and molecular modeling studies. J. Mol. Liq., 361.10.1016/j.molliq.2022.119617 ↗
38. Hillebrand, Exploring the capabilities of TDDFT calculations to explain the induced chirality upon a binding process: A simple case, 3- M. carboxycoumarin10.1016/j.molstruc.2012.11.060 ↗
39. Software news and updates AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility10.1002/jcc.21256 ↗
40. Exploring the interaction of 5,6-benzocoumarin-3-carboxylic acid with bovine serum albumin at the molecular level: A biophysical investigation using molecular dynamics10.33224/rrch.2021.66.1.05 ↗
41. (2022, August 03). Dassault Systèmes BIOVIA. Discovery Studio, San Diego: Dassault Systèmes. Available online: http://accelrys.com/products/discovery-studio.
42. Synthesis of chitosan-lysozyme microspheres, physicochemical characterization, enzymatic and antimicrobial activity10.1016/j.ijbiomac.2021.06.178 ↗
43. Bilal, M., Jing, Z., Zhao, Y., and Iqbal, H.M.N. (2019). Immobilization of fungal laccase on glutaraldehyde cross-linked chitosan beads and its bio-catalytic potential to degrade bisphenol A. Biocatal. Agric. Biotechnol., 19.10.1016/j.bcab.2019.101174 ↗
44. Immobilization of fungal (Trametes versicolor) laccase onto Amberlite IR-120 H beads: Optimization and characterization10.1016/j.procbio.2012.12.005 ↗
45. Characterization and immobilization of Trametes versicolor laccase on magnetic chitosan-clay composite beads for phenol removal10.3109/21691401.2015.1058809 ↗
46. Optimization of enzyme immobilization on functionalized magnetic nanoparticles for laccase biocatalytic reactions10.1016/j.cep.2017.03.009 ↗
47. Catalytic properties of lipases immobilized onto ultrasound-treated chitosan supports10.1007/s12257-013-0285-5 ↗
48. Activities, stabilities, and reaction kinetics of three free and chitosan-clay composite immobilized enzymes10.1016/j.enzmictec.2004.06.013 ↗
49. Setting the stage for electron transfer: Molecular basis of ABTS-binding to four laccases from Trametes versicolor at variable pH and protein oxidation state10.1016/j.molcatb.2013.11.017 ↗
50. Toxicity of the azo dye methyl red to the organisms in microcosms, with special reference to the Guppy (Poecilia reticulata Peters)10.1007/s00128-003-0047-8 ↗
51. Vršanská, M., Voběrková, S., Jiménez, A.M., Strmiska, V., and Adam, V. (2018). Preparation and optimisation of cross-linked enzyme aggregates using native isolate white rot fungi Trametes versicolor and Fomes fomentarius for the decolourisation of synthetic dyes. Int. J. Environ. Res. Public Health, 15.10.3390/ijerph15010023 ↗
52. Substrate specificity and enzyme recycling using Chitosan immobilized laccase10.3390/molecules191016794 ↗
53. Immobilization of laccase onto chitosan beads to enhance its capability to degrade synthetic dyes10.1016/j.ibiod.2016.03.004 ↗
54. An antioxidant, N,N’-diphenyl-p-phenylenediamine (DPPD), affects labor and delivery in rats: A 28-day repeated dose test and reproduction/developmental toxicity test10.1016/j.fct.2013.02.029 ↗
55. (2022, November 03). Available online: https://echa.europa.eu/documents/10162/81052d17-6bc1-972a-ebfd-7f9aa40644e7.
56. Sari, I.P., and Simarani, K. (2019). Comparative static and shaking culture of metabolite derived from methyl red degradation by Lysinibacillus fusiformis strain W1B6. R. Soc. Open Sci., 6.10.1098/rsos.190152 ↗
57. Decolourization and biodegradation of N,N’-dimethyl-p-phenylenediamine by Klebsiella pneumoniae RS-13 and Acetobacter liquefaciens S-110.1046/j.1365-2672.1998.00479.x ↗
58. Mittal, Y., Dash, S., Srivastava, P., Mishra, P.M., Aminabhavi, T.M., and Yadav, A.K. (2022). Azo dye containing wastewater treatment in earthen membrane based unplanted two chambered constructed wetlands-microbial fuel cells: A new design for enhanced performance. Chem. Eng. J., 427.10.1016/j.cej.2021.131856 ↗
59. Li, Z., Lu, Y., Wang, X., Vekaria, A., Jiang, M., and Zhang, H. (2020). Enhancing anthranilic acid biosynthesis using biosensor-assisted cell selection and in situ product removal. Biochem. Eng. J., 62.10.1016/j.bej.2020.107722 ↗