Nickel-Carnosine complex: A new carrier for enzymes immobilization by affinity adsorption

doi:10.1016/j.cjche.2021.04.019

摘要/Abstract

摘要： Immobilization is an effective method to promote the application of enzyme industry for improving the stability and realizing recovery of enzyme. To some extent, the performance of immobilized enzyme depends on the choice of carrier material. Therefore, the development of new carrier materials has been one of the key issues concerned by enzyme immobilization researchers. In this work, a novel organic-inorganic hybrid material, nickel-carnosine complex (NiCar), was synthesized for the first time by solvothermal method. The obtained NiCar exhibits spherical morphology, hierarchical porosity and abundant unsaturated coordination nickel ions, which provide excellent anchoring sites for the immobilization of proteins. His-tagged organophosphate-degrading enzyme (OpdA) and ω-transaminase (ω-TA) were used as model enzymes to evaluate the performance of NiCar as a carrier. By a simple adsorption process, the enzyme molecules can be fixed on the particles of NiCar, and the stability and reusability are significantly improved. The analysis of protein adsorption on NiCar verified that the affinity adsorption between the imidazole functional group on the protein and the unsaturated coordination nickel ions on NiCar was the main force in the immobilization process, which provided an idea way for the development of new enzyme immobilization carriers.

关键词: Nickel carnosine complex, Organic-inorganic hybrid materials, Carrier, Enzymes, Immobilization

Abstract: Immobilization is an effective method to promote the application of enzyme industry for improving the stability and realizing recovery of enzyme. To some extent, the performance of immobilized enzyme depends on the choice of carrier material. Therefore, the development of new carrier materials has been one of the key issues concerned by enzyme immobilization researchers. In this work, a novel organic-inorganic hybrid material, nickel-carnosine complex (NiCar), was synthesized for the first time by solvothermal method. The obtained NiCar exhibits spherical morphology, hierarchical porosity and abundant unsaturated coordination nickel ions, which provide excellent anchoring sites for the immobilization of proteins. His-tagged organophosphate-degrading enzyme (OpdA) and ω-transaminase (ω-TA) were used as model enzymes to evaluate the performance of NiCar as a carrier. By a simple adsorption process, the enzyme molecules can be fixed on the particles of NiCar, and the stability and reusability are significantly improved. The analysis of protein adsorption on NiCar verified that the affinity adsorption between the imidazole functional group on the protein and the unsaturated coordination nickel ions on NiCar was the main force in the immobilization process, which provided an idea way for the development of new enzyme immobilization carriers.

Key words: Nickel carnosine complex, Organic-inorganic hybrid materials, Carrier, Enzymes, Immobilization

Junyang Xu, Yanjun Jiang, Liya Zhou, Li Ma, Zhihong Huang, Jiafu Shi, Jing Gao, Ying He. Nickel-Carnosine complex: A new carrier for enzymes immobilization by affinity adsorption[J]. 中国化学工程学报, 2021, 38(10): 237-246.

参考文献

[1] S. Jemli, D. Ayadi-Zouari, H.B. Hlima, S. Bejar, Biocatalysts: application and engineering for industrial purposes, Crit. Rev. Biotechnol. 36 (2016) 246-258
[2] R.A. Sheldon, J.M. Woodley, Role of biocatalysis in sustainable chemistry, Chem. Rev. 118 (2017) 801-838
[3] R.A. Sheldon, S.V. Pelt, Enzyme immobilisation in biocatalysis: why, what and how, Chem. Soc. Rev. 42 (2013) 6223-6235
[4] R.C. Rodrigues, C. Ortiz, á. Berenguer-Murcia, R. Torres, R. Fernández-Lafuente, Modifying enzyme activity and selectivity by immobilization, Chem. Soc. Rev., 42 (2013) 6290-6307.
[5] X. Wu, M. Hou, J. Ge, Metal-organic frameworks and inorganic nanoflowers: a type of emerging inorganic crystal nanocarrier for enzyme immobilization, Catal. Sci. Technol. 5 (2015) 5077-5085
[6] J. Cui, S. Jia, Optimization protocols and improved strategies of cross-linked enzyme aggregates technology: current development and future challenges, Crit. Rev. Biotechnol. 35 (2015) 15-28
[7] M. Bilal, T. Rasheed, Y. Zhao, H.M.N. Iqbal, J. Cui, “Smart” chemistry and its application in peroxidase immobilization using different support materials, Int. J. Biol. Macromol. 119 (2018) 278-290
[8] J. Cui, S. Ren, B. Sun, S. Jia, Optimization protocols and improved strategies for metal-organic frameworks for immobilizing enzymes: Current development and future challenges, Coord. Chem. Rev. 370 (2018) 22-41
[9] S. Ren, C. Li, X. Jiao, S. Jia, Y. Jiang, M. Bilal, J. Cui, Recent progress in multienzymes co-immobilization and multienzyme system applications, Chem. Eng. J. 373 (2019) 1254-1278
[10] A. Liese, L. Hilterhaus, Evaluation of immobilized enzymes for industrial applications, Cheminform 42 (2013) 6236-6249
[11] D.I. Fried, F.J. Brieler, M. Fröba, Designing inorganic porous materials for enzyme adsorption and applications in biocatalysis, ChemCatChem 5 (2013) 862-884
[12] J.S. Qin, S. Yuan, C. Lollar, J. Pang, A. Alsalme, H.C. Zhou, Stable metal-organic frameworks as a host platform for catalysis and biomimetics, Chem. Commun. 54 (2018) 4231-4249
[13] J. He, S. Sun, M. Lu, Q. Yuan, Y. Liu, H. Liang, Metal-nucleobase hybrid nanoparticles for enhancing the activity and stability of metal-activated enzymes, Chem. Commun. 55 (2019) 6293-6296
[14] C. Doonan, R. Ricco, K. Liang, D. Bradshaw, P. Falcaro, Metal-organic frameworks at the biointerface: synthetic strategies and applications, Acc. Chem. Res. 50 (2017) 1423-1432
[15] G. Chen, S. Huang, X. Kou, F. Zhu, G. Ouyang, Embedding functional biomacromolecules within peptide-directed metal-organic framework (MOF) nanoarchitectures enables activity enhancement, Angew. Chem. Int. Ed. Engl. 59 (2020) 13947-13954
[16] J. Liang, K. Liang, Biocatalytic metal-organic frameworks: Prospects beyond bioprotective porous matrices, Adv. Funct. Mater. 30 (2020) 2001648
[17] L. Chen, Q. Xu, Metal-organic framework composites for catalysis, Matter 1 (2019) 57-89
[18] Y. Chen, S. Han, X. Li, Z. Zhang, S. Ma, Why does enzyme not leach from metal-organic frameworks (MOFs)? Unveiling the interactions between an enzyme molecule and a MOF, Inorg. Chem. 53 (2014) 10006-10008
[19] S.S. Nadar, L. Vaidya, V.K. Rathod, Enzyme embedded metal organic framework (enzyme-MOF): De novo approaches for immobilization, Int. J. Biol. Macromol. 149 (2020) 861-876
[20] V. Lykourinou, Y. Chen, X.S. Wang, L. Meng, T. Hoang, L.J. Ming, R.L. Musselman, S. Ma, Immobilization of MP-11 into a mesoporous metal-organic framework, MP-11@mesoMOF: A new platform for enzymatic catalysis, J. Am. Chem. Soc. 133 (2011) 10382-10385
[21] T.J. Pisklak, M. Macías, D.H. Coutinho, R.S. Huang, K.J. Balkus, Hybrid materials for immobilization of MP-11 catalyst, Top. Catal. 38 (2006) 269-278
[22] S. Jung, S. Park, Dual-surface functionalization of metal-organic frameworks for enhancing the catalytic activity of candida antarctica Lipase B in polar organic media, ACS Catal. 7 (2017) 438-442
[23] P. Adlercreutz, Immobilisation and application of lipases in organic media, Chem. Soc. Rev. 42 (2013) 6406-6436
[24] R. Röder, T. Preiß, P. Hirschle, B. Steinborn, A. Zimpel, M. Hoehn, J.O. Rädler, T. Bein, E. Wagner, S. Wuttke, U. Lächelt, Multifunctional nanoparticles by coordinative self-assembly of his-tagged units with metal-organic frameworks, J. Am. Chem. Soc. 139 (2017) 2359-2368
[25] J. Sun, Y. Fu, R. Li, W. Feng, Multifunctional hollow-shell microspheres derived from cross-Linking of MnO₂-nanoneedles by zirconium-based coordination polymer: enzyme mimicking, micromotors, and protein immobilization, Chem. Mater. 30 (2018) 1625-1634
[26] E.J. Baran, Metal complexes of carnosine, Biochemistry 65 (2000) 789-797
[27] A. Torreggiani, G. Fini, G. Bottura, Effect of transition metal binding on the tautomeric equilibrium of the carnosine imidazolic ring, J. Mol. Struct. 565-566 (2001) 341-346
[28] A.P. Katsoulidis, K.S. Park, D. Antypov, C. Marti-Gastaldo, G.J. Miller, J.E. Warren, C.M. Robertson, F. Blanc, G.R. Darling, N.G. Berry, J.A. Purton, D.J. Adams, M.J. Rosseinsky, Guest-adaptable and water-stable peptide-based porous materials by imidazolate side chain control, Angew. Chem. Int. Ed. Engl. 53 (2014) 193-198
[29] S. Kamari Kaverlavani, S.E. Moosavifard, A. Bakouei, Self-templated synthesis of uniform nanoporous CuCo₂O₄ double-shelled hollow microspheres for high-performance asymmetric supercapacitors, Chem. Commun. (Camb.) 53 (2017) 1052-1055
[30] L. Zhou, J. Li, J. Gao, H. Liu, S. Xue, L. Ma, G. Cao, Z. Huang, Y. Jiang, Facile oriented immobilization and purification of his-tagged organophosphohydrolase on viruslike mesoporous silica nanoparticles for organophosphate bioremediation, ACS Sustain. Chem. Eng. 6 (2018) 13588-13598
[31] G. Cao, J. Gao, L. Zhou, Z. Huang, Y. He, M. Zhu, Y. Jiang, Fabrication of Ni²⁺-nitrilotriacetic acid functionalized magnetic mesoporous silica nanoflowers for one pot purification and immobilization of His-tagged ω-transaminase, Biochem. Eng. J. 128 (2017) 116-125
[32] G. Cao, J. Gao, L. Zhou, Y. He, J. Li, Y. Jiang, Enrichment and coimmobilization of cofactors and His-tagged ω-transaminase into nanoflowers: A facile approach to constructing self-sufficient biocatalysts, ACS Applied Nano Materials 1 (2018) 3417-3425
[33] P. Yang, L.J. Yang, Q. Gao, Q. Luo, X.C. Zhao, X.M. Mai, Q.L. Fu, M.Y. Dong, J.C. Wang, Y.W. Hao, R.Z. Yang, X.C. Lai, S.D. Wu, Q. Shao, T. Ding, J. Lin, Z.H. Guo, Anchoring carbon nanotubes and post-hydroxylation treatment enhanced Ni nanofiber catalysts towards efficient hydrous hydrazine decomposition for effective hydrogen generation, Chem. Commun. 55 (2019) 9011-9014
[34] L. Feng, S. Yuan, L.L. Zhang, K. Tan, J.-L. Li, A. Kirchon, L.-M. Liu, P. Zhang, Y. Han, Y.J. Chabal, Creating hierarchical pores by controlled linker thermolysis in multivariate metal-organic frameworks, J. Am. Chem. Soc. 140 (2018) 2363-2372
[35] P.Q. Trombley, M.S. Horning, L.J. Blakemore, Interactions between carnosine and zinc and copper: implications for neuromodulation and neuroprotection, Biochemistry (Mosc) 65 (2000) 807-816
[36] H.C. Freeman, J.T. Szymanski, Crystallographic studies of metal-peptide complexes. V. (β-Alanyl-l-histidinato)copper(II) dihydrate, Acta Crystallogr. 22 (1967) 406-417
[37] J.L.A. Kirchon, F. Xia, G.S. Day, B. Becker, W. Chen, H.J. Sue, Y. Fang, H.C. Zhou, Modulation versus templating: fine-tuning of hierarchally porous PCN-250 using fatty acids to engineer guest adsorption, Angew. Chem. 58 (2019) 12425-12430
[38] S. Storck, H. Bretinger, W.F. Maier, Characterization of micro- and mesoporous solids by physisorption methods and pore-size analysis, Appl. Catal. A-Gen. 174 (1998) 137-146
[39] F. Zhang, M. Chen, X. Wu, W. Wang, H. Li, Highly active, durable and recyclable ordered mesoporous magnetic organometallic catalysts for promoting organic reactions in water, J. Mater. Chem. A 2 (2014) 484-491
[40] L. Jeong Woo, A. Taebin, S. Devaraj, K. Jang Myoun, K. Jong-Duk, Non-aqueous approach to the preparation of reduced graphene oxide/α-Ni(OH)₂ hybrid composites and their high capacitance behavior, Chem. Commun. 47 (2011) 6305-6307
[41] X. Luo, M. Huang, D. He, M. Wang, Y. Zhang, P. Jiang, Porous NiCo₂O₄ nanoarray-integrated binder-free 3D open electrode offers a highly efficient sensing platform for enzyme-free glucose detection, Analyst 143 (2018) 2546-2554
[42] J. Zhang, J. Zhang, Z. Jin, Z. Wu, Z. Zhang, Electrochemical lithium storage capacity of nickel mono-oxide loaded anatase titanium dioxide nanotubes, Ionics 18 (2012) 861-866
[43] G. Schenk, I. Mateen, T.K. Ng, M.M. Pedroso, N. Mitić, M.J. Jr, R.F.C. Marques, L.R. Gahan, D.L. Ollis, Organophosphate-degrading metallohydrolases: Structure and function of potent catalysts for applications in bioremediation, Coord. Chem. Rev. 317 (2016) 122-131
[44] F. Ely, K.S. Hadler, N. Mitić, L.R. Gahan, D.L. Ollis, N.M. Plugis, M.T. Russo, J.A. Larrabee, G. Schenk, Electronic and geometric structures of the organophosphate-degrading enzyme from Agrobacterium radiobacter (OpdA), J. Biol. Inorg. Chem. 16 (2011) 777-787
[45] J. Yang, K. Ni, D. Wei, Y. Ren, One-step purification and immobilization of his-tagged protein via Ni²⁺-functionalized Fe₃O₄@polydopamine magnetic nanoparticles, Biotechnol. Bioproc. E. 20 (2015) 901-907
[46] H. Irene, T.D. Sutherland, R.L. Harcourt, R.J. Russell, J.G. Oakeshott, Identification of an opd (organophosphate degradation) gene in an Agrobacterium isolate, Appl. Environ. Microbiol. 68 (2002) 3371-3376
[47] Y. Jiang, L. Ma, L. Zhou, L. Ma, Y. He, X. Zhang, J. Gao, Structured interlocked-microcapsules: A novel scaffold for enzyme immobilization, Catal. Commun. 88 (2017) 35-38
[48] M.A. Prieto, J.A. Vazquez, M.A. Murado, A new and general model to describe, characterize, quantify and classify the interactive effects of temperature and pH on the activity of enzymes, Analyst 140 (2015) 3587-3602
[49] M. Taheran, M. Naghdi, S.K. Brar, E.J. Knystautas, M. Verma, R.Y. Surampalli, Degradation of chlortetracycline using immobilized laccase on polyacrylonitrile-biochar composite nanofibrous membrane, Sci. Total Environ. 315 (2017) 605-606
[50] M. Sarı, S. Akgöl, M. Karataş, A. Denizli, Reversible immobilization of catalase by metal chelate affinity interaction on magnetic beads, Ind. Eng. Chem. Res. 45 (2006) 3036-3043
[51] B. Koohshekan, A. Divsalar, M. Saiedifar, A.A. Saboury, B. Ghalandari, A. Gholamian, A. Seyedarabi, Protective effects of aspirin on the function of bovine liver catalase: a spectroscopy and molecular docking study, J. Mol. Liq. 218 (2016) 8-15
[52] L. Wang, L. Wei, Y. Chen, R. Jiang, Specific and reversible immobilization of NADH oxidase on functionalized carbon nanotubes, J. Biotechnol. 150 (2010) 57-63
[53] S. Xue, J. Li, L. Zhou, J. Gao, G. Liu, L. Ma, Y. He, Y. Jiang, simple purification and immobilization of his-tagged organophosphohydrolase from cell culture supernatant by metal organic frameworks for degradation of organophosphorus pesticides, J. Agric. Food Chem. 67 (2019) 13518-13525