Current Advances in Immobilization Techniques of Enzymes

$20.00

Current Advances in Immobilization Techniques of Enzymes

Rajeev Ravindran, Amit K. Jaiswal

Enzymes are biological catalysts that accelerate the rate of a reaction without themselves being consumed. They sustain their activity for long periods of time and therefore are widely used in industrial processes. Enzymes contribute to approximately 28% of the operating cost of a production process; however, in most of the cases, the enzymes involved in production processes cannot be retrieved. Enzyme immobilisation is the process of attaching an enzyme molecule to a solid support with the intentions of its reuse, production and purification. Proper immobilisation of an enzyme on a support is dependent on the properties of the enzyme and carrier material. The binding to a support material can be temporary or permanent depending upon the chemical bond formed between the enzyme and the support. This article discusses in detail the intrinsic factors that influence enzyme immobilisation and the latest techniques such as one-step immobilisation, microencapsulation and cross-linked aggregates that have been proposed in recent years.

Keywords
Enzyme Immobilization, Carrier Material, Entrapment, Affinity Tags, Adsorption, One Step Immobilization

Published online 2/21/2019, 22 pages

DOI: https://dx.doi.org/10.21741/9781644900079-3

Part of the book on Enzymatic Fuel Cells

References
[1] E. García-Urdiales, I. Alfonso, V. Gotor, Update 1 of: enantioselective enzymatic desymmetrizations in organic synthesis, Chem. Rev. 11 (2011) PR110–PR180. https://doi.org/10.1021/cr100330u
[2] C.J. Malemud, Matrix metalloproteinases (MMPs) in health and disease: an overview, Frontiers In Bioscience: A Journal And Virtual Library. 11 (2005) 1696-1701. https://doi.org/10.2741/1915
[3] A. Wolfgang, Enzyme in industry: Production and Applications, Wiley-VCH, Weinheim, 2007.
[4] G. Haki, S. Rakshit, Developments in industrially important thermostable enzymes: a review, Bioresource Technology 89 (2003) 17-34. https://doi.org/10.1016/S0960-8524(03)00033-6
[5] I. Alkorta, C. Garbisu, M.J. Llama, J.L. Serra, Industrial applications of pectic enzymes: a review, Process Biochem. 33 (1998) 21-28. https://doi.org/10.1016/S0032-9592(97)00046-0
[6] H. Neurath, K.A. Walsh, Role of proteolytic enzymes in biological regulation (a review), Proceedings of the National Academy of Sciences 73 (1976) 3825-3832. https://doi.org/10.1073/pnas.73.11.3825
[7] J.R. Cherry, A.L. Fidantsef, Directed evolution of industrial enzymes: an update, Current Opinion in Biotechnology 14 (2003) 438-443. https://doi.org/10.1016/S0958-1669(03)00099-5
[8] B. Joseph, P.W. Ramteke, G. Thomas, Cold active microbial lipases: some hot issues and recent developments, Biotechnology Advances 26 (2008) 457-470. https://doi.org/10.1016/j.biotechadv.2008.05.003
[9] J. Lalonde, A. Margolin, Immobilization of enzymes, Enzyme Catalysis in Organic Synthesis: A Comprehensive Handbook, Second Edition (2008) 163-184.
[10] N. Burgoyne, R. Jackson, Predicting Protein Function from Surface Properties, in: D. Rigden (Ed.) From Protein Structure to Function with Bioinformatics, Springer Netherlands 2009, pp. 167-186. https://doi.org/10.1007/978-1-4020-9058-5_7
[11] L. Cao, Carrier-bound immobilized enzymes: principles, application and design, John Wiley & Sons 2006.
[12] U. Hanefeld, L. Gardossi, E. Magner, Understanding enzyme immobilisation, Chemical Society Reviews 38 (2009) 453-468. https://doi.org/10.1039/B711564B
[13] R.A. Sheldon, S. van Pelt, Enzyme immobilisation in biocatalysis: why, what and how, Chemical Society Reviews 42 (2013) 6223-6235. https://doi.org/10.1039/C3CS60075K
[14] R.Y. Cabrera-Padilla, M.C. Lisboa, A.T. Fricks, E. Franceschi, A.S. Lima, D.P. Silva, C.M. Soares, Immobilization of Candida rugosa lipase on poly (3-hydroxybutyrate-co-hydroxyvalerate): A new eco-friendly support, Journal of Industrial Microbiology & Biotechnology 39 (2012) 289-298. https://doi.org/10.1007/s10295-011-1027-3
[15] G.-W. Xing, X.-W. Li, G.-L. Tian, Y.-H. Ye, Enzymatic peptide synthesis in organic solvent with different zeolites as immobilization matrixes, Tetrahedron 56 (2000) 3517-3522. https://doi.org/10.1016/S0040-4020(00)00261-1
[16] J.F. Díaz, K.J. Balkus, Enzyme immobilization in MCM-41 molecular sieve, Journal of Molecular Catalysis B: Enzymatic 2 (1996) 115-126. https://doi.org/10.1016/S1381-1177(96)00017-3
[17] F. Yagiz, D. Kazan, A.N. Akin, Biodiesel production from waste oils by using lipase immobilized on hydrotalcite and zeolites, Chemical Engineering Journal 134 (2007) 262-267. https://doi.org/10.1016/j.cej.2007.03.041
[18] N. Carlsson, H. Gustafsson, C. Thörn, L. Olsson, K. Holmberg, B. Åkerman, Enzymes immobilized in mesoporous silica: A physical–chemical perspective, Advances in Colloid and Interface Science 205 (2014) 339-360. https://doi.org/10.1016/j.cis.2013.08.010
[19] B. Kalska-Szostko, M. Rogowska, A. Dubis, K. Szymański, Enzymes immobilization on Fe3O4–gold nanoparticles, Applied Surface Science 258 (2012) 2783-2787. https://doi.org/10.1016/j.apsusc.2011.10.132
[20] E. Biró, Á.S. Németh, C. Sisak, T. Feczkó, J. Gyenis, Preparation of chitosan particles suitable for enzyme immobilization, Journal of Biochemical and Biophysical Methods 70 (2008) 1240-1246. https://doi.org/10.1016/j.jprot.2007.11.005
[21] E.W. Nery, L.T. Kubota, Evaluation of enzyme immobilization methods for paper-based devices—A glucose oxidase study, Journal of Pharmaceutical and Biomedical Analysis 117 (2016) 551-559. https://doi.org/10.1016/j.jpba.2015.08.041
[22] P. Hanachi, F. Jafary, F. Jafary, S. Motamedi, Immobilization of the alkaline phosphatase on collagen surface via cross-linking method, Iranian Journal of Biotechnology 13 (2015) 32-38. https://doi.org/10.15171/ijb.1203
[23] T. Coradin, J. Livage, Mesoporous alginate/silica biocomposites for enzyme immobilisation, Comptes Rendus Chimie 6 (2003) 147-152. https://doi.org/10.1016/S1631-0748(03)00006-7
[24] T. Jesionowski, J. Zdarta, B. Krajewska, Enzyme immobilization by adsorption: A review, Adsorption 20 (2014) 801-821. https://doi.org/10.1007/s10450-014-9623-y
[25] H.H.P. Yiu, P.A. Wright, N.P. Botting, Enzyme immobilisation using SBA-15 mesoporous molecular sieves with functionalised surfaces, Journal of Molecular Catalysis B: Enzymatic 15 (2001) 81-92. https://doi.org/10.1016/S1381-1177(01)00011-X
[26] M. Persson, E. Wehtje, P. Adlercreutz, Immobilisation of lipases by adsorption and deposition: high protein loading gives lower water activity optimum, Biotechnology letters 22 (2000) 1571-1575. https://doi.org/10.1023/A:1005689002238
[27] T. Zhao, D.S. No, B.H. Kim, H.S. Garcia, Y. Kim, I.-H. Kim, Immobilized phospholipase A1-catalyzed modification of phosphatidylcholine with n−3 polyunsaturated fatty acid, Food Chemistry 157 (2014) 132-140. https://doi.org/10.1016/j.foodchem.2014.02.024
[28] C.-T. Tsai, A.S. Meyer, Enzymatic cellulose hydrolysis: Enzyme reusability and visualization of β-Glucosidase immobilized in calcium alginate, Molecules 19 (2014) 19390-19406. https://doi.org/10.3390/molecules191219390
[29] S. Khanahmadi, F. Yusof, A. Amid, S.S. Mahmod, M.K. Mahat, Optimized preparation and characterization of CLEA-lipase from cocoa pod husk, Journal of Biotechnology 202 (2015) 153-161. https://doi.org/10.1016/j.jbiotec.2014.11.015
[30] C. Mateo, O. Abian, R. Fernandez–Lafuente, J.M. Guisan, Increase in conformational stability of enzymes immobilized on epoxy-activated supports by favoring additional multipoint covalent attachment, Enzyme and Microbial Technology 26 (2000) 509-515. https://doi.org/10.1016/S0141-0229(99)00188-X
[31] J.C.Y. Wu, C.H. Hutchings, M.J. Lindsay, C.J. Werner, B.C. Bundy, Enhanced enzyme stability through site-directed covalent immobilization, Journal of Biotechnology 193 (2015) 83-90. https://doi.org/10.1016/j.jbiotec.2014.10.039
[32] R.M. Kramer, V.R. Shende, N. Motl, C.N. Pace, J.M. Scholtz, Toward a molecular understanding of protein solubility: increased negative surface charge correlates with increased solubility, Biophysical Journal 102 (2012) 1907-1915. https://doi.org/10.1016/j.bpj.2012.01.060
[33] Y.R. Gokarn, R.M. Fesinmeyer, A. Saluja, V. Razinkov, S.F. Chase, T.M. Laue, D.N. Brems, Effective charge measurements reveal selective and preferential accumulation of anions, but not cations, at the protein surface in dilute salt solutions, Protein Science 20 (2011) 580-587. https://doi.org/10.1002/pro.591
[34] C.M. Halliwell, E. Simon, C.-S. Toh, A.E.G. Cass, P.N. Bartlett, The design of dehydrogenase enzymes for use in a biofuel cell: the role of genetically introduced peptide tags in enzyme immobilization on electrodes, Bioelectrochemistry 55 (2002) 21-23. https://doi.org/10.1016/S1567-5394(01)00172-4
[35] N. Bortone, M. Fidaleo, Immobilization of the recombinant (His)6-tagged l-arabinose isomerase from Thermotoga maritima on epoxy and cupper-chelate epoxy supports, Food and Bioproducts Processing 95 (2015) 155-162. https://doi.org/10.1016/j.fbp.2015.05.002
[36] M. Miyazaki, J. Kaneno, S. Yamaori, T. Honda, M.P. P. Briones, M. Uehara, K. Arima, K. Kanno, K. Yamashita, Y. Yamaguchi, H. Nakamura, H. Yonezawa, M. Fujii, H. Maeda, efficient immobilization of enzymes on microchannel surface through his-tag and application for microreactor, Protein and Peptide Letters 12 (2005) 207-210. https://doi.org/10.2174/0929866053005854
[37] A. Wang, F. Du, F. Wang, Y. Shen, W. Gao, P. Zhang, Convenient one-step purification and immobilization of lipase using a genetically encoded aldehyde tag, Biochemical Engineering Journal 73 (2013) 86-92. https://doi.org/10.1016/j.bej.2013.02.003
[38] H. Kamal, E.L.S.A. Hegazy, H.M. Sharada, S.A. Abd Elhalim, S. Lotfy, R.D. Mohamed, Immobilization of glucose isomerase onto radiation synthesized P(AA-co-AMPS) hydrogel and its application, Journal of Radiation Research and Applied Sciences 7 (2014) 154-162. https://doi.org/10.1016/j.jrras.2014.02.001
[39] M.R. Javed, A. Buthe, M.H. Rashid, P. Wang, Cost-efficient entrapment of β-glucosidase in nanoscale latex and silicone polymeric thin films for use as stable biocatalysts, Bioproducts and Biosystems Engineering 190 (2016) 1078-1085. https://doi.org/10.1016/j.foodchem.2015.06.040
[40] Z. Bibi, F. Shahid, S.A. Ul Qader, A. Aman, Agar–agar entrapment increases the stability of endo-β-1,4-xylanase for repeated biodegradation of xylan, International Journal of Biological Macromolecules 75 (2015) 121-127. https://doi.org/10.1016/j.ijbiomac.2014.12.051
[41] S. Barig, A. Funke, A. Merseburg, K. Schnitzlein, K.P. Stahmann, Dry entrapment of enzymes by epoxy or polyester resins hardened on different solid supports, Enzyme and Microbial Technology 60 (2014) 47-55. https://doi.org/10.1016/j.enzmictec.2014.03.013
[42] I. Mazurenko, W. Ghach, G.-W. Kohring, C. Despas, A. Walcarius, M. Etienne, Immobilization of membrane-bounded (S)-mandelate dehydrogenase in sol–gel matrix for electroenzymatic synthesis, Bioelectrochemistry 104 (2015) 65-70. https://doi.org/10.1016/j.bioelechem.2015.03.004
[43] E.I. Goksu, M.I. Hoopes, B.A. Nellis, C. Xing, R. Faller, C.W. Frank, S.H. Risbud, J.H. Satcher Jr, M.L. Longo, Silica xerogel/aerogel-supported lipid bilayers: Consequences of surface corrugation, Biochimica et Biophysica Acta (BBA) – Biomembranes 1798 (2010) 719-729. https://doi.org/10.1016/j.bbamem.2009.09.007
[44] L. Veum, U. Hanefeld, A. Pierre, The first encapsulation of hydroxynitrile lyase from Hevea brasiliensis in a sol–gel matrix, Tetrahedron 60 (2004) 10419-10425. https://doi.org/10.1016/j.tet.2004.06.135
[45] C. Garcia‐Galan, Á. Berenguer‐Murcia, R. Fernandez‐Lafuente, R.C. Rodrigues, Potential of different enzyme immobilization strategies to improve enzyme performance, Advanced Synthesis and Catalysis 353 (2011) 2885-2904. https://doi.org/10.1002/adsc.201100534
[46] K. Hernandez, R. Fernandez-Lafuente, Control of protein immobilization: Coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance, Enzyme and Microbial Technology 48 (2011) 107-122. https://doi.org/10.1016/j.enzmictec.2010.10.003
[47] A. Fatima, Q. Husain, Polyclonal antibodies mediated immobilization of a peroxidase from ammonium sulphate fractionated bitter gourd (Momordica charantia) proteins, Biomolecular Engineering 24 (2007) 223-230. https://doi.org/10.1016/j.bioeng.2006.10.002
[48] J. Wang, D. Bhattacharyya, L.G. Bachas, Orientation specific immobilization of organophosphorus hydrolase on magnetic particles through gene fusion, Biomacromolecules 2 (2001) 700-705. https://doi.org/10.1021/bm015517x
[49] H. van Tilbeurgh, M.-P. Egloff, C. Martinez, N. Rugani, R. Verger, C. Cambillau, Interfacial activation of the lipase–procolipase complex by mixed micelles revealed by X-ray crystallography, Nature 362 (1993) 814–820. https://doi.org/10.1038/362814a0
[50] A. Brzozowski, U. Derewenda, Z. Derewenda, G. Dodson, D. Lawson, J. Turkenburg, F. Bjorkling, B. Huge-Jensen, S. Patkar, L. Thim, A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex, Nature 351 (1991) 491-494. https://doi.org/10.1038/351491a0
[51] Z.S. Derewenda, U. Derewenda, G.G. Dodson, The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 Å resolution, Journal of Molecular Biology 227 (1992) 818-839. https://doi.org/10.1016/0022-2836(92)90225-9
[52] G. Fernández-Lorente, J.M. Palomo, Z. Cabrera, J.M. Guisán, R. Fernández-Lafuente, Specificity enhancement towards hydrophobic substrates by immobilization of lipases by interfacial activation on hydrophobic supports, Enzyme and Microbial Technology 41 (2007) 565-569. https://doi.org/10.1016/j.enzmictec.2007.05.004
[53] G. Fernandez-Lorente, Z. Cabrera, C. Godoy, R. Fernandez-Lafuente, J.M. Palomo, J.M. Guisan, Interfacially activated lipases against hydrophobic supports: Effect of the support nature on the biocatalytic properties, Process Biochemistry 43 (2008) 1061-1067. https://doi.org/10.1016/j.procbio.2008.05.009
[54] E.A. Manoel, J.C. dos Santos, D.M. Freire, N. Rueda, R. Fernandez-Lafuente, Immobilization of lipases on hydrophobic supports involves the open form of the enzyme, Enzyme and Microbial Technology 71 (2015) 53-57. https://doi.org/10.1016/j.enzmictec.2015.02.001
[55] J.M. Palomo, G. Muñoz, G. Fernández-Lorente, C. Mateo, R. Fernández-Lafuente, J.M. Guisán, Interfacial adsorption of lipases on very hydrophobic support (octadecyl–Sepabeads): immobilization, hyperactivation and stabilization of the open form of lipases, Journal of Molecular Catalysis B: Enzymatic 19 (2002) 279-286. https://doi.org/10.1016/S1381-1177(02)00178-9
[56] J.M. Bolivar, J. Rocha-Martin, C. Godoy, R.C. Rodrigues, J.M. Guisan, Complete reactivation of immobilized derivatives of a trimeric glutamate dehydrogenase from Thermus thermophillus, Process Biochemistry 45 (2010) 107-113. https://doi.org/10.1016/j.procbio.2009.08.014
[57] O. Barbosa, R. Torres, C. Ortiz, A.n. Berenguer-Murcia, R.C. Rodrigues, R. Fernandez-Lafuente, Heterofunctional supports in enzyme immobilization: From traditional immobilization protocols to opportunities in tuning enzyme properties, Biomacromolecules 14 (2013) 2433-2462. https://doi.org/10.1021/bm400762h
[58] C. Mateo, J.M. Palomo, M. Fuentes, L. Betancor, V. Grazu, F. López-Gallego, B.C. Pessela, A. Hidalgo, G. Fernández-Lorente, R. Fernández-Lafuente, Glyoxyl agarose: A fully inert and hydrophilic support for immobilization and high stabilization of proteins, Enzyme and Microbial Technology 39 (2006) 274-280. https://doi.org/10.1016/j.enzmictec.2005.10.014
[59] C. Mateo, O. Abian, M. Bernedo, E. Cuenca, M. Fuentes, G. Fernandez-Lorente, J.M. Palomo, V. Grazu, B.C. Pessela, C. Giacomini, Some special features of glyoxyl supports to immobilize proteins, Enzyme and Microbial Technology 37 (2005) 456-462. https://doi.org/10.1016/j.enzmictec.2005.03.020
[60] J. Pedroche, M. del Mar Yust, C. Mateo, R. Fernández-Lafuente, J. Girón-Calle, M. Alaiz, J. Vioque, J.M. Guisán, F. Millán, Effect of the support and experimental conditions in the intensity of the multipoint covalent attachment of proteins on glyoxyl-agarose supports: correlation between enzyme–support linkages and thermal stability, Enzyme and Microbial Technology 40 (2007) 1160-1166. https://doi.org/10.1016/j.enzmictec.2006.08.023
[61] A.P.M. Tavares, C.G. Silva, G. Dražić, A.M.T. Silva, J.M. Loureiro, J.L. Faria, Laccase immobilization over multi-walled carbon nanotubes: Kinetic, thermodynamic and stability studies, Journal of Colloid and Interface Science 454 (2015) 52-60. https://doi.org/10.1016/j.jcis.2015.04.054
[62] E.-J. Woo, H.-S. Kwon, C.-H. Lee, Preparation of nano-magnetite impregnated mesocellular foam composite with a Cu ligand for His-tagged enzyme immobilization, Chemical Engineering Journal 274 (2015) 1-8. https://doi.org/10.1016/j.cej.2015.03.123