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Frontiers of Chemical Science and Engineering

ISSN 2095-0179

ISSN 2095-0187(Online)

CN 11-5981/TQ

Postal Subscription Code 80-969

2018 Impact Factor: 2.809

Front. Chem. Sci. Eng.    2023, Vol. 17 Issue (7) : 867-879    https://doi.org/10.1007/s11705-022-2277-5
RESEARCH ARTICLE
Immobilization of laccase on organic–inorganic nanocomposites and its application in the removal of phenolic pollutants
Wei Zhang, Runtang Liu, Xu Yang, Binbin Nian, Yi Hu()
State Key Laboratory of Materials-Oriented Chemical Engineering, School of Pharmaceutical Sciences, Nanjing Tech University, Nanjing 210009, China
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Abstract

Polydopamine-functionalized nanosilica was synthesized using an inexpensive and easily obtainable raw material, mild reaction conditions, and simple operation. Subsequently, a flexible spacer arm was introduced by using dialdehyde starch as a cross-linking agent to bind with laccase. A high loading amount (77.8 mg∙g‒1) and activity retention (75.5%) could be achieved under the optimum immobilization conditions. Thermodynamic parameters showed that the immobilized laccase had a lower thermal deactivation rate constant and longer half-life. The enhancement of thermodynamic parameters indicated that the immobilized laccase had better thermal stability than free laccase. The residual activity of immobilized laccase remained at about 50.0% after 30 days, which was 4.0 times that of free laccase. Immobilized laccase demonstrated excellent removal of phenolic pollutants (2,4-dichlorophenol, bisphenol A, phenol, and 4-chlorophenol) and perfect reusability with 70% removal efficiency retention for 2,4-dichlorophenol after seven cycles. These results suggested that immobilized laccase possessed great reusability, improved thermal stability, and excellent storage stability. Organic–inorganic nanomaterials have a good application prospect for laccase immobilization, and the immobilized laccase of this work may provide a practical application for the removal of phenolic pollutants.

Keywords polydopamine      pollutant removal      thermodynamic      phenolic pollutants      immobilized laccase     
Corresponding Author(s): Yi Hu   
About author:

* These authors contributed equally to this work.

Just Accepted Date: 02 December 2022   Online First Date: 03 April 2023    Issue Date: 05 July 2023
 Cite this article:   
Wei Zhang,Runtang Liu,Xu Yang, et al. Immobilization of laccase on organic–inorganic nanocomposites and its application in the removal of phenolic pollutants[J]. Front. Chem. Sci. Eng., 2023, 17(7): 867-879.
 URL:  
https://academic.hep.com.cn/fcse/EN/10.1007/s11705-022-2277-5
https://academic.hep.com.cn/fcse/EN/Y2023/V17/I7/867
  Scheme1 Schematic illustration of the synthesis of PDA-functionalized nanoparticles, laccase immobilization, and application for pollutant removal.
SupportAdded laccase /(mL?mL?1)Laccase loading /(mg?g?1)Activity retention/%
SiO20.619.232.5
PDA/SiO20.668.366.3
DAS/PDA/SiO20.677.875.5
Tab.1  Result of immobilization of laccase
Fig.1  (a) FTIR spectra and (b) TGA curves of carriers.
Fig.2  SEM and TEM images of (a–c) SiO2 and (d–f) DAS/PDA/SiO2.
SupportSpecific surface area/(cm2?g?1)Average pore diameter/nmTotal pore volume/(cm3?g?1)
SiO2111.139.240.26
PDA/SiO289.8212.150.27
DAS/PDA/SiO2135.4812.770.43
Tab.2  Pore structure properties of supports
Fig.3  Nitrogen sorption isotherms of SiO2, PDA/SiO2, and DAS/PDA/SiO2.
Fig.4  Effect of (a) pH and (b) temperature on the relative activity of free and immobilized laccase.
SampleKm/(mmol?L?1)Vmax/(mmol?L?1?min?1)Vmax?Km–1/min?1
Free laccase0.851149.254175.387
Immobilized laccase0.870129.870149.276
Tab.3  Kinetic parameters of immobilized laccase
Fig.5  Lineweaver–Burk plots of free and immobilized laccase.
Temperature/°CKd/min?1t?/sEd/(kJ?mol?1)
304050304050
Free laccase0.00160.00710.0132433.2297.6352.5186.20
Immobilized laccase0.00050.00070.00441386.29990.20157.5387.80
Tab.4  Kinetic parameters of thermal deactivation of free and immobilized laccase
Fig.6  Dynamic curves of thermal deactivation of (a) free laccase and (b) immobilized laccase; (c) Arrhenius plots for the thermal deactivation of free laccase and immobilized laccase.
Temperature/°C?H/(kJ?mol?1)?G/(kJ?mol?1)?S/(J?mol?1?K?1)
304050304050304050
Free laccase83.6883.5983.51102.2398.2694.63?61.22?44.59?39.25
Immobilized laccase85.2885.1985.11103.71102.9498.39?60.84?56.71?41.12
Tab.5  Thermodynamic parameters for thermal deactivation of free and immobilized laccase
SupportPollutantsConcentration/(mg?L?1)Reaction time/hRemoval efficiency/%Ref.
Amino-functionalized magnetic metal–organic framework2,4-DCP101287.0[47]
Halloysite nanotubes2,4-DCP102494.6[48]
Multi-walled carbon nanotubesBPA102480.0[50]
Amino-functionalized ionic liquid4-CP102489.3[28]
2,4-DCP10100.0
PH1083.4
PDA functionalized nano-silica2,4-DCP1012100.0This work
BPA1088.2
PH1085.1
4-CP1084.2
Tab.6  Removals of phenolic compounds by different immobilized laccase catalysts
Fig.7  Degradation curves of (a) 2,4-DCP, (b) BPA, (c) PH, and (d) 4-CP.
Fig.8  (a) 2,4-DCP removal efficiencies of recycled immobilized laccase and (b) the residual activity of free laccase and immobilized laccase after storage.
1 W Zhou, W Zhang, Y Cai. Laccase immobilization for water purification: a comprehensive review. Chemical Engineering Journal, 2020, 403: 126272
https://doi.org/10.1016/j.cej.2020.126272
2 P K Arora, H Bae. Bacterial degradation of chlorophenols and their derivatives. Microbial Cell Factories, 2014, 13(1): 1–17
https://doi.org/10.1186/1475-2859-13-31
3 A Rostami, A Abdelrasoul, Z Shokri, Z Shirvandi. Applications and mechanisms of free and immobilized laccase in detoxification of phenolic compounds—a review. Korean Journal of Chemical Engineering, 2022, 39(4): 821–832
https://doi.org/10.1007/s11814-021-0984-0
4 J X Fan, J Q Luo, Y H Wan. Aquatic micro-pollutants removal with a biocatalytic membrane prepared by metal chelating affinity membrane chromatography. Chemical Engineering Journal, 2017, 327: 1011–1020
https://doi.org/10.1016/j.cej.2017.06.172
5 Y Y Liu, Z T Zeng, G M Zeng, L Tang, Y Pang, Z Li, C Liu, X X Lei, M S Wu, P Y Ren, Z Liu, M Chen, G Xie. Immobilization of laccase on magnetic bimodal mesoporous carbon and the application in the removal of phenolic compounds. Bioresource Technology, 2012, 115: 21–26
https://doi.org/10.1016/j.biortech.2011.11.015
6 J X Fan, J Q Luo, Y H Wan. Membrane chromatography for fast enzyme purification, immobilization and catalysis: a renewable biocatalytic membrane. Journal of Membrane Science, 2017, 538: 68–76
https://doi.org/10.1016/j.memsci.2017.05.053
7 M Bilal, S S Ashraf, J D Cui, W Y Lou, M Franco, S I Mulla, H M N Iqbal. Harnessing the biocatalytic attributes and applied perspectives of nanoengineered laccases—a review. International Journal of Biological Macromolecules, 2021, 166: 352–373
https://doi.org/10.1016/j.ijbiomac.2020.10.195
8 X Qiu, J Qin, M Xu, L F Kang, Y Hu. Organic–inorganic nanocomposites fabricated via functional ionic liquid as the bridging agent for laccase immobilization and its application in 2,4-dichlorophenol removal. Colloids and Surfaces B: Biointerfaces, 2019, 179: 260–269
https://doi.org/10.1016/j.colsurfb.2019.04.002
9 R A Sheldon, S van Pelt. Enzyme immobilisation in biocatalysis: why, what and how. Chemical Society Reviews, 2013, 42(15): 6223–6235
https://doi.org/10.1039/C3CS60075K
10 R Dicosimo, J Mcauliffe, A J Poulose, G Bohlmann. Industrial use of immobilized enzymes. Chemical Society Reviews, 2013, 42(15): 6437–6474
https://doi.org/10.1039/c3cs35506c
11 J X Zhao, M M Ma, X H Yan, G H Zhang, J H Xia, Z L Zeng, P Yu, Q Deng, D M Gong. Green synthesis of polydopamine functionalized magnetic mesoporous biochar for lipase immobilization and its application in interesterification for novel structured lipids production. Food Chemistry, 2022, 379: 132148
https://doi.org/10.1016/j.foodchem.2022.132148
12 L Zhong, Y X Feng, G Y Wang, Z Y Wang, M Bilal, H X Lv, S R Jia, J D Cui. Production and use of immobilized lipases in/on nanomaterials: a review from the waste to biodiesel production. International Journal of Biological Macromolecules, 2020, 152: 207–222
https://doi.org/10.1016/j.ijbiomac.2020.02.258
13 P G Jeelani, P Mulay, R Venkat, C Ramalingam. Multifaceted application of silica nanoparticles: a review. Silicon, 2020, 12(6): 1337–1354
https://doi.org/10.1007/s12633-019-00229-y
14 B Silvestri, G Vitiello, G Luciani, V Calcagno, A Costantini, M Gallo, S Parisi, S Paladino, M Iacomino, G D’Errico, M F Caso, A Pezzella, M d’Ischia. Probing the eumelanin-silica interface in chemically engineered bulk hybrid nanoparticles for targeted subcellular antioxidant protection. ACS Applied Materials & Interfaces, 2017, 9(43): 37615–37622
https://doi.org/10.1021/acsami.7b11839
15 Y Ni, Z X Lv, Z Wang, S Y Kang, D W He, R J Liu. Immobilization and evaluation of penicillin G acylase on hydroxy and aldehyde functionalized magnetic α-Fe2O3/Fe3O4 heterostructure nanosheets. Frontiers in Bioengineering and Biotechnology, 2022, 9(1): 812403
https://doi.org/10.3389/fbioe.2021.812403
16 J Lin, Y Liu, C Shi, X Le, X Zhou, Z Zhao, Y Ou, J Yang. Reversible immobilization of laccase onto metal-ion-chelated magnetic microspheres for bisphenol A removal. International Journal of Biological Macromolecules, 2016, 84: 189–199
https://doi.org/10.1016/j.ijbiomac.2015.12.013
17 Y Chen, H Ding, B Wang, Q Shi, J Gao, Z Cui, Y Wan. Dopamine functionalization for improving crystallization behaviour of polyethylene glycol in shape-stable phase change material with silica fume as the matrix. Journal of Cleaner Production, 2019, 208: 951–959
https://doi.org/10.1016/j.jclepro.2018.10.207
18 L Wang, Y Shi, S Chen, W Wang, M Tian, N Ning, L Zhang. Highly efficient mussel-like inspired modification of aramid fibers by UV-accelerated catechol/polyamine deposition followed chemical grafting for high-performance polymer composites. Chemical Engineering Journal, 2017, 314: 583–593
https://doi.org/10.1016/j.cej.2016.12.015
19 M Deng, H Zhao, S Zhang, C Tian, D Zhang, P Du, C Liu, H Cao, H Li. High catalytic activity of immobilized laccase on core-shell magnetic nanoparticles by dopamine self-polymerization. Journal of Molecular Catalysis B: Enzymatic, 2015, 112: 15–24
https://doi.org/10.1016/j.molcatb.2014.11.012
20 H Chen, Z Hao, Y Li, Y Li, X Wang. Facile synthesis of oxidic PEG-modified magnetic polydopamine nanospheres for candida rugosa lipase immobilization. Applied Microbiology and Biotechnology, 2015, 99(3): 1249–1259
https://doi.org/10.1007/s00253-014-5990-2
21 Y Chen, Y Jiang, J Gao, W Wu, L Dong, Z Yang. Facile immobilization of nitrile hydratase in SBA-15 via a biomimetic coating. Journal of Porous Materials, 2017, 24(3): 787–793
https://doi.org/10.1007/s10934-016-0317-6
22 H R Zhang, J Q Luo, S S Li, Y P Wei, Y H Wan. Biocatalytic membrane based on polydopamine coating: a platform for studying immobilization mechanisms. Langmuir, 2018, 34(8): 2585–2594
https://doi.org/10.1021/acs.langmuir.7b02860
23 M K Khan, J Q Luo, Z S Wang, R Khan, X R Chen, Y H Wan. Alginate dialdehyde meets nylon membrane: a versatile platform for facile and green fabrication of membrane adsorbers. Journal of Materials Chemistry B: Materials for Biology and Medicine, 2018, 6(11): 1640–1649
https://doi.org/10.1039/C7TB02966G
24 S S Wang, S Li, R T Liu, W Zhang, H J Xu, Y Hu. Immobilization of interfacial activated candida rugosa lipase onto magnetic chitosan using dialdehyde cellulose as cross-linking agent. Frontiers in Bioengineering and Biotechnology, 2022, 10: 946117
https://doi.org/10.3389/fbioe.2022.946117
25 F Ran, Y Zou, Y Xu, X Liu, H Zhang. Fe3O4@MoS2@PEI-facilitated enzyme tethering for efficient removal of persistent organic pollutants in water. Chemical Engineering Journal, 2019, 375(1): 121947
https://doi.org/10.1016/j.cej.2019.121947
26 T T Xia, C Z Liu, J H Hu, C Guo. Improved performance of immobilized laccase on amine-functioned magnetic Fe3O4 nanoparticles modified with polyethylenimine. Chemical Engineering Journal, 2016, 295: 201–206
https://doi.org/10.1016/j.cej.2016.03.044
27 X Y Yang, Y F Chen, S Yao, J Q Qian, H Guo, X H Cai. Preparation of immobilized lipase on magnetic nanoparticles dialdehyde starch. Carbohydrate Polymers, 2019, 218: 324–332
https://doi.org/10.1016/j.carbpol.2019.05.012
28 X Qiu, Y Wang, Y Xue, W X Li, Y Hu. Laccase immobilized on magnetic nanoparticles modified by amino-functionalized ionic liquid via dialdehyde starch for phenolic compounds biodegradation. Chemical Engineering Journal, 2020, 391: 123564
https://doi.org/10.1016/j.cej.2019.123564
29 R Tang, Y Du, L Fan. Dialdehyde starch-crosslinked chitosan films and their antimicrobial effects. Journal of Polymer Science Part B: Polymer Physics, 2003, 41(9): 993–997
https://doi.org/10.1002/polb.10405
30 J Gao, J Zhou, X Zhang, Q Shi, Z Han, Y Chen. Facile functionalized mesoporous silica using biomimetic method as new matrix for preparation of shape: tabilized phase-change material with improved enthalpy. International Journal of Energy Research, 2019, 43(14): 8649–8659
https://doi.org/10.1002/er.4861
31 M M Bradford. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein–dye binding. Analytical Biochemistry, 1976, 72(1-2): 248–254
https://doi.org/10.1016/0003-2697(76)90527-3
32 W A A Wahab, E A Karam, M E Hassan, A L Kansoh, M A Esawy, G E A Awad. Optimization of pectinase immobilization on grafted alginate-agar gel beads by 2(4) full factorial CCD and thermodynamic profiling for evaluating of operational covalent immobilization. International Journal of Biological Macromolecules, 2018, 113: 159–170
https://doi.org/10.1016/j.ijbiomac.2018.02.086
33 E Birhanli, S A A Noma, F Boran, A Ulu, O Yesilada, B Ates. Design of laccase–metal–organic framework hybrid constructs for biocatalytic removal of textile dyes. Chemosphere, 2022, 292: 133382
https://doi.org/10.1016/j.chemosphere.2021.133382
34 V Gascón, C Márquez-Álvarez, R M Blanco. Efficient retention of laccase by non-covalent immobilization on amino-functionalized ordered mesoporous silica. Applied Catalysis A: General, 2014, 482: 116–126
https://doi.org/10.1016/j.apcata.2014.05.035
35 X R Xiang, S Ding, H B Suo, C Xu, Z Gao, Y Hu. Fabrication of chitosan-mesoporous silica SBA-15 nanocomposites via functional ionic liquid as the bridging agent for PPL immobilization. Carbohydrate Polymers, 2018, 182: 245–253
https://doi.org/10.1016/j.carbpol.2017.11.031
36 H Guo, B S Lei, J W Yu, Y F Chen, J Q Qian. Immobilization of lipase by dialdehyde cellulose crosslinked magnetic nanoparticles. International Journal of Biological Macromolecules, 2021, 185: 287–296
https://doi.org/10.1016/j.ijbiomac.2021.06.073
37 C Chen, W Sun, H Y Lv, H Li, Y B Wang, P Wang. Spacer arm-facilitated tethering of laccase on magnetic polydopamine nanoparticles for efficient biocatalytic water treatment. Chemical Engineering Journal, 2018, 350: 949–959
https://doi.org/10.1016/j.cej.2018.06.008
38 T G Hu, J H Cheng, B B Zhang, W Y Lou, M H Zong. Immobilization of alkaline protease on amino-functionalized magnetic nanoparticles and its efficient use for preparation of oat polypeptides. Industrial & Engineering Chemistry Research, 2015, 54(17): 4689–4698
https://doi.org/10.1021/ie504691j
39 W L Xie, X Z Zang. Lipase immobilized on ionic liquid-functionalized magnetic silica composites as a magnetic biocatalyst for production of trans-free plastic fats. Food Chemistry, 2018, 257: 15–22
https://doi.org/10.1016/j.foodchem.2018.03.010
40 C Hou, Z G Qi, H Zhu. Preparation of core–shell magnetic polydopamine/alginate biocomposite for candida rugosa lipase immobilization. Colloids and Surfaces B: Biointerfaces, 2015, 128: 544–551
https://doi.org/10.1016/j.colsurfb.2015.03.007
41 R J Liu, W Huang, S Pan, Y Li, L L Yu, D W He. Covalent immobilization and characterization of penicillin G acylase on magnetic Fe2O3/Fe3O4 heterostructure nanoparticles prepared via a novel solution combustion and gel calcination process. International Journal of Biological Macromolecules, 2020, 162(21): 1587–1596
https://doi.org/10.1016/j.ijbiomac.2020.07.283
42 W Huang, S Pan, Y Li, L L Yu, R J Liu. Immobilization and characterization of cellulase on hydroxy and aldehyde functionalized magnetic Fe2O3/Fe3O4 nanocomposites prepared via a novel rapid combustion process. International Journal of Biological Macromolecules, 2020, 162(21): 845–852
https://doi.org/10.1016/j.ijbiomac.2020.06.209
43 S Dhiman, B Srivastava, G Singh, M Khatri, S K Arya. Immobilization of mannanase on sodium alginate-grafted-beta-cyclodextrin: an easy and cost effective approach for the improvement of enzyme properties. International Journal of Biological Macromolecules, 2020, 156: 1347–1358
https://doi.org/10.1016/j.ijbiomac.2019.11.175
44 S A Ahmed, S A A Saleh, S A M Abdel-Hameed, A M Fayad. Catalytic, kinetic and thermodynamic properties of free and immobilized caseinase on mica glass-ceramics. Heliyon, 2019, 5(5): 1–12
https://doi.org/10.1016/j.heliyon.2019.e01674
45 H R Wehaidy, M A Abdel-Naby, H M El-Hennawi, H F Youssef. Nanoporous zeolite-x as a new carrier for laccase immobilization and its application in dyes decolorization. Biocatalysis and Agricultural Biotechnology, 2019, 19: 101135
https://doi.org/10.1016/j.bcab.2019.101135
46 X Qiu, S S Wang, S S Miao, H B Suo, H J Xu, Y Hu. Co-immobilization of laccase and ABTS onto amino-functionalized ionic liquid-modified magnetic chitosan nanoparticles for pollutants removal. Journal of Hazardous Materials, 2021, 401: 123353
https://doi.org/10.1016/j.jhazmat.2020.123353
47 E H Wu, Y X Li, Q Huang, Z K Yang, A Y Wei, Q Hu. Laccase immobilization on amino-functionalized magnetic metal organic framework for phenolic compound removal. Chemosphere, 2019, 233: 327–335
https://doi.org/10.1016/j.chemosphere.2019.05.150
48 C Chao, J D Liu, J T Wang, Y W Zhang, B Zhang, Y T Zhang, X Xiang, R F Chen. Surface modification of halloysite nanotubes with dopamine for enzyme immobilization. ACS Applied Materials & Interfaces, 2013, 5(21): 10559–10564
https://doi.org/10.1021/am4022973
49 M Mohammadi, M A As’habi, P Salehi, M Yousefi, M Nazari, J Brask. Immobilization of laccase on epoxy-functionalized silica and its application in biodegradation of phenolic compounds. International Journal of Biological Macromolecules, 2018, 109: 443–447
https://doi.org/10.1016/j.ijbiomac.2017.12.102
50 R Pang, M Z Li, C D Zhang. Degradation of phenolic compounds by laccase immobilized on carbon nanomaterials: diffusional limitation investigation. Talanta, 2015, 131: 38–45
https://doi.org/10.1016/j.talanta.2014.07.045
51 D J Ren, S Jiang, L J Fu, Z B Wang, S Q Zhang, X Q Zhang, X Y Gong, W S Chen. Laccase immobilized on amino-functionalized magnetic Fe3O4–SiO2 core–shell material for 2,4-dichlorophenol removal. Environmental Technology, 2021, 3: 1–22
52 Z H Chen, J Yao, B Ma, B Liu, J Kim, H Li, X Z Zhu, C C Zhao, M Amde. A robust biocatalyst based on laccase immobilized superparamagnetic Fe3O4@SiO2-NH2 nanoparticles and its application for degradation of chlorophenols. Chemosphere, 2022, 291(1): 132727
https://doi.org/10.1016/j.chemosphere.2021.132727
53 W W Huan, Y X Yang, B Wu, H M Yuan, Y N Zhang, X N Liu. Degradation of 2,4-DCP by theimmobilized laccase on the carrier of Fe3O4@SiO2-NH2. Chinese Journal of Chemistry, 2012, 30(12): 2849–2860
https://doi.org/10.1002/cjoc.201200718
54 J Yang, Y Hu, L Jiang, B Zou, R Jia, H Huang. Enhancing the catalytic properties of porcine pancreatic lipase by immobilization on SBA-15 modified by functionalized ionic liquid. Biochemical Engineering Journal, 2013, 70: 46–54
https://doi.org/10.1016/j.bej.2012.09.016
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