Abstract
In this study, an amino-functionalized ionic liquid-modified magnetic chitosan (MACS-NIL) containing 2,2-diamine-di-3-ethylbenzothiazolin-6-sulfonic acid (ABTS) was used as a carrier, and dialdehyde starch (DAS) was used as a cross-linking agent to covalently immobilize laccase (MACS-NIL-DAS-lac), which realized the co-immobilization of laccase and ABTS. The carrier was characterized by Fourier infrared transform spectroscopy, scanning electron microscopy, thermogravimetric analysis, X-ray diffraction analysis, electron paramagnetic resonance, etc. The immobilization efficiency and activity retention of MACS-NIL-DAS-lac could reach 76.7% and 69.8%, respectively. At the same time, its pH stability, thermal stability, and storage stability had been significantly improved. In the organic pollutant removal performance test, the removal rate of 2,4-dichlorophenol (10 mg/L) by MACS-NIL-DAS-lac (1 U) could reach 100% within 6 h, and the removal efficiency could still reach 88.6% after six catalytic runs. In addition, MACS-NIL-DAS-lac also showed excellent degradation ability for other conventional phenolic pollutants and polycyclic aromatic hydrocarbons. The research results showed that MACS-NIL-DAS fabricated by the combination inorganic material, organic biomacromolecules, ionic liquid, and electron mediator could be used as a novel carrier for laccase immobilization and the immobilized laccase showed excellent removal efficiency for organic pollutants.
Similar content being viewed by others
References
Haritash AK, Kaushik CP (2009) Kaushik, Biodegradation aspects of polycyclic aromatic hydrocarbons (PAHs): a review. J Hazard Mater 169:1–15. https://doi.org/10.1016/j.jhazmat.2009.03.137
Zhou W, Zhang W, Cai Y (2021) Laccase immobilization for water purification: A comprehensive review. Chem Eng J 403:126272. https://doi.org/10.1016/j.cej.2020.126272
Olaniran AO, Igbinosa EO (2011) Chlorophenols and other related derivatives of environmental concern: Properties, distribution and microbial degradation processes. Chemosphere 83(10):1297–1306. https://doi.org/10.1016/j.chemosphere.2011.04.009
Couto SR, Herrera JLT (2006) Industrial and biotechnological applications of laccases: A review. Biotechnol Adv 24(5):500–513. https://doi.org/10.1016/j.biotechadv.2006.04.003
Mahmoodi NM, Taghizadeh A, Taghizadeh M, Abdi J (2019) In situ deposition of Ag/AgCl on the surface of magnetic metal-organic framework nanocomposite and its application for the visible-light photocatalytic degradation of Rhodamine dye. J Hazard Mater 378:120741. https://doi.org/10.1016/j.jhazmat.2019.06.018
Torres E, Bustos-Jaimes I, Le Borgne S (2003) Potential use of oxidative enzymes for the detoxification of organic pollutants. Appl Catal B 46(1):1–15. https://doi.org/10.1016/s0926-3373(03)00228-5
Alcalde M, Ferrer M, Plou FJ, Ballesteros A (2006) Environmental biocatalysis: from remediation with enzymes to novel green processes. Trends Biotechnol 24(6):281–287. https://doi.org/10.1016/j.tibtech.2006.04.002
Singh J, Saharan V, Kumar S, Gulati P, Kapoor RK (2018) Laccase grafted membranes for advanced water filtration systems: a green approach to water purification technology. Crit Rev Biotechnol 38(6):883–901. https://doi.org/10.1080/07388551.2017.1417234
Riva S (2013) Laccases: blue enzymes for green chemistry. FEBS J 280:590–590. https://doi.org/10.1016/j.tibtech.2006.03.006
Jiang YJ, Wang Q, He Y, Zhou LY, Gao J (2014) Co-aggregation of laccase and nature egg white: a simple method to prepare stable and recyclable biocatalyst. Appl Biochem Biotechnol 172(5):2496–2506. https://doi.org/10.1007/s12010-013-0697-x
Altinkaynak C, Tavlasoglu S, Ozdemir N, Ocsoy I (2016) A new generation approach in enzyme immobilization: Organic-inorganic hybrid nanoflowers with enhanced catalytic activity and stability. Enzyme Microb Technol 93–94:105–112. https://doi.org/10.1016/j.enzmictec.2016.06.011
Alvarado-Ramirez L, Rostro-Alanis M, Rodriguez-Rodriguez J, Castillo-Zacarias C, Sosa-Hernandez JE, Barcelo D, Iqbal HMN, Parra-Saldivar R (2021) Exploring current tendencies in techniques and materials for immobilization of laccases-A review. Int J Biol Macromol 181:683–696. https://doi.org/10.1016/j.ijbiomac.2021.03.175
Zhang Y, Gao J, Xin X, Wang LH, Li HY, Zheng XB, Jiang YJ (2020) Immobilization laccase on heterophase TiO2 microsphere as a photo-enzyme integrated catalyst for emerging contaminants degradation under visible light. Appl Mater Today 21:100810. https://doi.org/10.1016/j.apmt.2020.100810
Bilal M, Zhao YP, Rasheed T, Iqbal HMN (2018) Magnetic nanoparticles as versatile carriers for enzymes immobilization: A review. Int J Biol Macromol 120:2530–2544. https://doi.org/10.1016/j.ijbiomac.2018.09.025
Zheng MM, Wang S, Xiang X, Shi J, Huang J, Deng QC, Huang FH, Xiao JY (2017) Facile preparation of magnetic carbon nanotubes-immobilized lipase for highly efficient synthesis of 1,3-dioleoyl-2-palmitoylglycerol-rich human milk fat substitutes. Food Chem 228:476–483. https://doi.org/10.1016/j.foodchem.2017.01.129
Wang XY, Jiang XP, Li Y, Zeng S, Zhang YW (2015) Preparation Fe3O4@chitosan magnetic particles for covalent immobilization of lipase from Thermomyces lanuginosus. Int J Biol Macromol 75:44–50. https://doi.org/10.1016/j.ijbiomac.2015.01.020
Zhang K, Yang WZ, Liu Y, Zhang KG, Chen Y, Yin XS (2020) Laccase immobilized on chitosan-coated Fe3O4 nanoparticles as reusable biocatalyst for degradation of chlorophenol. J Mol Struct 1220:128769. https://doi.org/10.1016/j.molstruc.2020.128769
Xiang XR, Ding S, Suo HB, Xu C, Gao Z, Hu Y (2018) Fabrication of chitosan-mesoporous silica SBA-15 nanocomposites via functional ionic liquid as the bridging agent for PPL immobilization. Carbohydr Polym 182:245–253. https://doi.org/10.1016/j.carbpol.2017.11.031
Qiu X, Qin J, Xu M, Kang LF, Hu Y (2019) Organic-inorganic nanocomposites fabricated via functional ionic liquid as the bridging agent for Laccase immobilization and its application in 2,4-dichlorophenol removal. Colloids Surfac B Biointerfaces 179:260–269. https://doi.org/10.1016/j.colsurfb.2019.04.002
Suo HB, Xu LL, Xu C, Qu X, Chen HY, Huang H, Hu Y (2019) Graphene oxide nanosheets shielding of lipase immobilized on magnetic composites for the improvement of enzyme stability. ACS Sustain Chem Eng 7(4):4486–4494. https://doi.org/10.1021/acssuschemeng.8b06542
Sojitra UV, Nadar SS, Rathod VK (2017) Immobilization of pectinase onto chitosan magnetic nanoparticles by macromolecular cross-linker. Carbohydr Polym 157:677–685. https://doi.org/10.1016/j.carbpol.2016.10.018
Lu WS, Shen YH, Xie AJ, Zhang WQ (2013) Preparation and Protein Immobilization of Magnetic Dialdehyde Starch Nanoparticles. J Phys Chem B 117(14):3720–3725. https://doi.org/10.1021/jp3110908
Tang RP, Du YM, Fan LH (2003) Dialdehyde starch-crosslinked chitosan films and their antimicrobial effects. J Polym Sci Part B Polym Phys 41(9):993–997. https://doi.org/10.1002/polb.10405
Qiu X, Wang Y, Xue Y, Li WX, Hu Y (2020) Laccase immobilized on magnetic nanoparticles modified by amino-functionalized ionic liquid via dialdehyde starch for phenolic compounds biodegradation. Chem Eng J 391:123564. https://doi.org/10.1016/j.cej.2019.123564
Feng YP, Shen MY, Wang Z, Liu GG (2019) Transformation of atenolol by a laccase-mediator system: Efficiencies, effect of water constituents, and transformation pathways. Ecotoxicol Environ Saf 183:109555. https://doi.org/10.1016/j.ecoenv.2019.109555
Gu YH, Xue P, Jia F, Shi KR (2019) Co-immobilization of laccase and ABTS onto novel dual-functionalized cellulose beads for highly improved biodegradation of indole. J Hazard Mater 365:118–124. https://doi.org/10.1016/j.jhazmat.2018.10.076
Xue P, Liu XP, Gu YH, Zhang WW, Ma L, Li R (2020) Laccase-mediator system assembling co-immobilized onto functionalized calcium alginate beads and its high-efficiency catalytic degradation for acridine. Colloids Surf B Biointerfaces 196:111348. https://doi.org/10.1016/j.colsurfb.2020.111348
Suo HB, Gao Z, Xu LL, Xu C, Yu DH, Xiang XR, Huang H, Hu Y (2019) Synthesis of functional ionic liquid modified magnetic chitosan nanoparticles for porcine pancreatic lipase immobilization. Mater Sci Eng C Mater Biol Appl 96:356–364. https://doi.org/10.1016/j.msec.2018.11.041
Suo HB, Xu LL, Xu C, Chen HY, Yu DH, Gao Z, Huang H, Hu Y (2018) Enhancement of catalytic performance of porcine pancreatic lipase immobilized on functional ionic liquid modified Fe3O(4)-Chitosan nanocomposites. Int J Biol Macromol 119:624–632. https://doi.org/10.1016/j.ijbiomac.2018.07.187
Chao C, Liu JD, Wang JT, Zhang YW, Zhang B, Zhang YT, Xiang X, Chen RF (2013) Surface modification of halloysite nanotubes with dopamine for enzyme immobilization. ACS Appl Mater Interfaces 5(21):10559–10564. https://doi.org/10.1021/am4022973
Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254. https://doi.org/10.1006/abio.1976.9999
Zou B, Hu Y, Cui FJ, Jiang L, Yu DH, Huang H (2014) Effect of surface modification of low cost mesoporous SiO2 carriers on the properties of immobilized lipase. J Colloid Interface Sci 417:210–216. https://doi.org/10.1016/j.jcis.2013.11.029
Chen C, Sun W, Lv HY, Li H, Wang YB, Wang P (2018) Spacer arm-facilitated tethering of laccase on magnetic polydopamine nanoparticles for efficient biocatalytic water treatment, Chem. Eng J 350:949–959. https://doi.org/10.1016/j.cej.2018.06.008
Nguyen XS, Zhang GK, Yang XF (2017) Mesocrystalline Zn-Doped Fe3O4 hollow submicrospheres: formation mechanism and enhanced photo-fenton catalytic performance. Acs Appl Mater Interfaces 9(10):8900–8909. https://doi.org/10.1021/acsami.6b16839
Chen M, Xu P, Zeng GM, Yang CP, Huang DL, Zhang JC (2015) Bioremediation of soils contaminated with polycyclic aromatic hydrocarbons, petroleum, pesticides, chlorophenols and heavy metals by composting: Applications, microbes and future research needs. Biotechnol Adv 33(6):745–755. https://doi.org/10.1016/j.biotechadv.2015.05.003
Zappi D, Masci G, Sadun C, Tortolini C, Antonelli ML, Bollella P (2018) Evaluation of new cholinium-amino acids based room temperature ionic liquids (RTILs) as immobilization matrix for electrochemical biosensor development: Proof-of-concept with Trametes Versicolor laccase. Microchem J 141:346–352. https://doi.org/10.1016/j.microc.2018.05.045
De Diego T, Manjon A, Lozano P, Vaultier M, Iborra JL (2011) An efficient activity ionic liquid-enzyme system for biodiesel production. Green Chem 13(2):444–451. https://doi.org/10.1039/c0gc00230e
Guan ZB, Luo Q, Wang HR, Chen Y, Liao XR (2018) Bacterial laccases: promising biological green tools for industrial applications. Cell Mol Life Sci 75(19):3569–3592. https://doi.org/10.1007/s00018-018-2883-z
Kadam AA, Jang J, Jee SC, Sung JS, Lee DS (2018) Chitosan-functionalized supermagnetic halloysite nanotubes for covalent laccase immobilization. Carbohydr Polym 194:208–216. https://doi.org/10.1016/j.carbpol.2018.04.046
Yang XY, Chen YF, Yao S, Qian JQ, Guo H, Cai XH (2019) Preparation of immobilized lipase on magnetic nanoparticles dialdehyde starch. Carbohydr Polym 218:324–332. https://doi.org/10.1016/j.carbpol.2019.05.012
Ziegler-Borowska M, Chelminiak-Dudkiewicz D, Siodmiak T, Sikora A, Wegrzynowska-Drzymalska K, Skopinska-Wisniewska J, Kaczmarek H, Marszall MP (2017) Chitosan-collagen coated magnetic nanoparticles for lipase immobilization-new type of “enzyme friendly” polymer shell crosslinking with squaric acid. Catalysts 7(1):26. https://doi.org/10.3390/catal7010026
Ss A, Zgn B, Sg C (2020) Smba, removal of bisphenol A in aqueous solution using magnetic cross-linked laccase aggregates from Trametes hirsuta -ScienceDirect. Bioresour Technol 306:123169. https://doi.org/10.1016/j.biortech.2020.123169
Gascon V, Marquez-Alvarez C, Blanco RM (2014) Efficient retention of laccase by non-covalent immobilization on amino-functionalized ordered mesoporous silica. Appl Catal Gen 482:116–126. https://doi.org/10.1016/j.apcata.2014.05.035
Lee KM, Kalyani D, Tiwari MK, Kim TS, Dhiman SS, Lee JK, Kim IW (2012) Enhanced enzymatic hydrolysis of rice straw by removal of phenolic compounds using a novel laccase from yeast Yarrowia lipolytica. Bioresour Technol 123:636–645. https://doi.org/10.1016/j.biortech.2012.07.066
Hou C, Qi ZG, Zhu H (2015) Preparation of core-shell magnetic polydopamine/alginate biocomposite for Candida rugosa lipase immobilization. Colloid Surf B Biointerfaces 128:544–551. https://doi.org/10.1016/j.colsurfb.2015.03.007
Ulu A, Birhanli E, Boran F, Koytepe S, Ates B (2020) Laccase-conjugated thiolated chitosan-Fe3O4 hybrid composite for biocatalytic degradation of organic dyes. Int J Biol Macromol 150:871–884. https://doi.org/10.1016/j.ijbiomac.2020.02.006
Zhang ST, Wu ZF, Chen G, Wang Z (2018) An improved method to encapsulate laccase from trametes versicolor with enhanced stability and catalytic activity. Catalysts 8(7):286–297. https://doi.org/10.3390/catal8070286
Wu EH, Li YX, Huang Q, Yang ZK, Wei AY, Hu Q (2019) Laccase immobilization on amino-functionalized magnetic metal organic framework for phenolic compound removal. Chemosphere 233:327–335. https://doi.org/10.1016/j.chemosphere.2019.05.150
Xu R, Zhou Q, Li F, Zhang B (2013) Laccase immobilization on chitosan/poly(vinyl alcohol) composite nanofibrous membranes for 2,4-dichlorophenol removal, Chem. Eng J 222:321–329. https://doi.org/10.1016/j.cej.2013.02.074
Alver E, Metin AL (2017) Chitosan based metal-chelated copolymer nanoparticles: Laccase immobilization and phenol degradation studies. Int Biodeterior Biodegrad 125:235–242. https://doi.org/10.1016/j.ibiod.2017.07.012
Lin J, Liu Y, Shi C, Le X, Zhou X, Zhao Z, Ou Y, Yang J (2016) Reversible immobilization of laccase onto metal-ion-chelated magnetic microspheres for bisphenol A removal. Int J Biol Macromol 84:189–199. https://doi.org/10.1016/j.ijbiomac.2015.12.013
Fernando Bautista L, Morales G, R. (2015) Sanz, Biodegradation of polycyclic aromatic hydrocarbons (PAHs) by laccase from Trametes versicolor covalently immobilized on amino-functionalized SBA-15. Chemosphere 136:273–280. https://doi.org/10.1016/j.chemosphere.2015.05.071
Acknowledgements
This research was financially supported by National Natural Science Foundation of China (No. 22178174) and National key R&D program of China (No. 2021YFC2103802). The Jiangsu Synergetic Innovation Center for Advanced Bio-Manufacture (No. XTC2206), and Jiangsu Students’ platform for innovation and entrepreneurship training program (No. 202110291109Y).
Funding
This work was supported by the National Natural Science Foundation of China, under Grant 22178174, National key R&D Program of China, under Grant 2021YFC2103802, The Jiangsu Synergetic Innovation Center for Advanced Bio-Manufacture, under Grant XTC2206, and Jiangsu Students’ Platform for Innovation and Entrepreneurship Training Program, under Grant 202110291109Y.
Author information
Authors and Affiliations
Contributions
RL: conceptualization, methodology, formal analysis, investigation, data curation, writing–original draft, and writing–review & editing. SW methodology and investigation. MH methodology and investigation. WZ methodology and investigation. HX conceptualization, methodology, funding acquisition, and supervision. YH funding acquisition, supervision, and writing–review & editing.
Corresponding authors
Ethics declarations
Conflict of interest
The authors declare that they have no conflict of interest.
Additional information
Publisher's Note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Supplementary Information
Below is the link to the electronic supplementary material.
Rights and permissions
Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.
About this article
Cite this article
Liu, R., Wang, S., Han, M. et al. Co-immobilization of electron mediator and laccase onto dialdehyde starch cross-linked magnetic chitosan nanomaterials for organic pollutants’ removal. Bioprocess Biosyst Eng 45, 1955–1966 (2022). https://doi.org/10.1007/s00449-022-02799-5
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00449-022-02799-5