Abstract
The entrapment of enzymes in capsules is a smart strategy to concentrate them in confined spaces and control their exposure to outside environments. Enzymes can be caged in the interior of capsules during their formation (preloading) or postloaded within prefabricated and permeable hollow shells. On the other hand, enzymes can also be deposited within the shell or on the surface of the capsules. Each of these strategies has intrinsic limitations, and a common enemy is the undesired desorption of enzymes.
Here, we describe the formation of enzyme-loaded polymeric capsules prepared with the Layer-by-Layer method and the template-assisted entrapment of enzymes through coprecipitation (preloading) within calcium carbonate particles, as an example of an efficient preloading strategy, and draw attention at the key parameters that influence this immobilization method.
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20 March 2020
Chapter 12 was inadvertently published with the contributing authors listed as Mihaela Badea, Akhtar Hayat, and Jean-Louis Marty, whereas it should have been printed as Audrey Sassolas, Akhtar Hayat, and Jean-Louis Marty. This correction has been updated in the book.
References
Kantner K, Rejman J, Kraft KVL, Soliman MG, Zyuzin MV, Escudero A, Del Pino P, Parak WJ (2018) Laterally and temporally controlled intracellular staining by light-triggered release of encapsulated fluorescent markers. Chemistry 24(9):2098–2102
Dergunov SA, Khabiyev AT, Shmakov SN, Kim MD, Ehterami N, Weiss MC, Birman VB, Pinkhassik E (2016) Encapsulation of homogeneous catalysts in porous polymer nanocapsules produces fast-acting selective nanoreactors. ACS Nano 10(12):11397–11406
Lvov Y, Antipov AA, Mamedov A, Möhwald H, Sukhorukov GB (2001) Urease encapsulation in nanoorganized microshells. Nano Lett 1(3):125–128
Sakr OS, Borchard G (2013) Encapsulation of enzymes in Layer-by-Layer (LbL) structures: latest advances and applications. Biomacromolecules 14(7):2117–2135
Ott A, Yu X, Hartmann R, Rejman J, Schütz A, Ochs M, Parak WJ, Carregal-Romero S (2015) Light-addressable and degradable silica capsules for delivery of molecular cargo to the cytosol of cells. Chem Mat 27:1929–1942
Hussain SZ, Zyuzin MV, Hussain I, Parak WJ, Carregal-Romero S (2016) Catalysis by multifunctional polyelectrolyte capsules. RSC Adv 6(85):81569–81577
Liang Z, Wang C, Tong Z, Ye W, Ye S (2005) Bio-catalytic nanoparticles with urease immobilized in multilayer assembled through layer-by-layer technique. React Funct Polym 63(1):85–94
Chang F-P, Hung Y, Chang J-H, Lin C-H, Mou C-Y (2014) Enzyme encapsulated hollow silica nanospheres for intracellular biocatalysis. ACS Appl Mater Interfaces 6(9):6883–6890
González-Domínguez E, Comesaña-Hermo M, Mariño-Fernández R, rodríguez-González B, Arenal R, Salgueiriño V, Moldes D, Othman AM, Pérez-Lorenzo M, Correa-Duarte MA (2016) Hierarchical nanoplatforms for high-performance enzyme biocatalysis under denaturing conditions. ChemCatChem 8(7):1264–1268
Benítez-Mateos AI, Llarena I, Sánchez-Iglesias A, López-Gallego F (2018) Expanding one-pot cell-free protein synthesis and immobilization for O on-demand manufacturing of biomaterials. ACS Synthetic Bio 7(3):875–884
Were LM, Bruce BD, Davidson PM, Weiss J (2003) Size, stability, and entrapment efficiency of phospholipid nanocapsules containing polypeptide antimicrobials. J Agric Food Chem 51(27):8073–8079
Wilkerson JW, Yang SO, Funk PJ, Stanley SK, Bundy BC (2018) Nanoreactors: strategies to encapsulate enzyme biocatalysts in virus-like particles. New Biotechnol 44:59–63
Tsang SC, Yu CH, Gao X, Tam K (2006) Silica-encapsulated nanomagnetic particle as a new recoverable biocatalyst carrier. J Phys Chem B 110(34):16914–16922
Ariga K, Ji Q, Hill JP (2010) Enzyme-encapsulated Layer-by-Layer assemblies: current status and challenges toward ultimate nanodevices. Modern techniques for nano- and microreactors/−reactions. Springer, Berlin, pp 51–87
Walde P, Ichikawa S (2001) Enzymes inside lipid vesicles: preparation, reactivity and applications. Biomol Eng 18(4):143–177
Yoshimoto M, Sakamoto H, Yoshimoto N, Kuboi R, Nakao K (2007) Stabilization of quaternary structure and activity of bovine liver catalase through encapsulation in liposomes. Enzym Microb Technol 41(6):849–858
Zhang R, Feng L, Dong Z, Wang L, Liang C, Chen J, Ma Q, Zhang R, Chen Q, Wang Y, Liu Z Glucose & oxygen exhausting liposomes for combined cancer starvation and hypoxia-activated therapy. Biomaterials 162:123–131
Colletier JP, Chaize B, Winterhalter M, Fournier D (2002) Protein encapsulation in liposomes: efficiency depends on interactions between protein and phospholipid bilayer. BMC Biotechnol 2(9)
Chen C, Han D, Cai C, Tang X (2010) An overview of liposome lyophilization and its future potential. J Control Release 142(3):299–311
Caruso F, Trau D, Möhwald H, Renneberg R (2000) Enzyme encapsulation in layer-by-layer engineered polymer multilayer capsules. Langmuir 16(4):1485–1488
López-Gallego F, Yate L (2015) Selective biomineralization of Co3(PO4)2-sponges triggered by His-tagged proteins: efficient heterogeneous biocatalysts for redox processes. Chem Commun 51(42):8753–8756
Petrov AP, Volodkin DV, Sukhorukov GB (2005) Protein-calcium carbonate coprecipitation: a tool for protein encapsulation. Biotechnol Prog 21(3):918–925
Parakhonskiy BV, Yashchenok AM, Konrad M, Skirtach AG (2014) Colloidal micro- and nano-particles as templates for polyelectrolyte multilayer capsules. Adv Colloid Interf Sci 207:253–264
Parakhonskiy BV, Haase A, Antolini R (2012) Sub-micrometer vaterite containers: synthesis, substance loading, and release. Angew Chem Int Ed 51(5):1195–1197
Parakhonskiy B, Zyuzin MV, Yashchenok A, Carregal-Romero S, Rejman J, Möhwald H, Parak WJ, Skirtach AG (2015) The influence of the size and aspect ratio of anisotropic, porous CaCO3 particles on their uptake by cells. J Nanobiotechnol 13(1):53
Harimech PK, Hartmann R, Rejman J, del_Pino P, Rivera_Gil P, Parak WJ (2015) Encapsulated enzymes with integrated fluorescence-control of enzymatic activity. J Mater Chem B 3(14):2801–2807
Volodkin DV, Petrov AI, Prevot M, Sukhorukov GB (2004) Matrix polyelectrolyte microcapsules: new system for macromolecule encapsulation. Langmuir 20(8):3398–3406
Skirtach A, Yashchenok A, Möhwald H (2011) Encapsulation, release and applications of LbL polyelectrolyte multilayer capsules. Chem Commun 47(48):12736–12746
Donath E, Sukhorukov GB, Caruso F, Davis SA, Möhwald H (1998) Novel hollow polymer shells by colloid-templated assembly of polyelectrolytes. Angew Chem Int Ed 37(16):2202–2205
Milkova V, Radeva T (2013) Effect of ionic strength and molecular weight on electrical properties and thickness of polyelectrolyte bi-layers. Colloids Surf A Physicochem Eng Asp 424:52–58
Schönhoff M, Ball V, Bausch AR, Dejugnat C, Delorme N, Glinel K, Klitzing RV, Steitz R (2007) Hydration and internal properties of polyelectrolyte multilayers. Colloids Surf A Physicochem Eng Asp 303(1–2):14–29
Steitz R, Leiner V, Siebrecht R, Klitzing R (2000) Influence of the ionic strength on the structure of polyelectrolyte films at the solid/liquid interface. Colloids Surf A Physicochem Eng Asp 163(1):63–70
Karamitros CS, Yashchenok AM, Möhwald H, Skirtach AG, Konrad M (2013) Preserving catalytic activity and enhancing biochemical stability of the therapeutic enzyme asparaginase by biocompatible multi layered polyelectrolyte microcapsules. Biomacromolecules 14(12):4398–4406
Mahajan RV, Kumar V, Rajendran V, Saran S, Ghosh PC, Saxena RK (2014) Purification and characterization of a novel and robust L-asparaginase having low-glutaminase activity from bacillus licheniformis: in vitro evaluation of anti-cancerous properties. PLoS One 9(6):e99037
Volodkin DV, Larionova NI, Sukhorukov GB (2004) Protein encapsulation via porous CaCO3 microparticles templating. Biomacromolecules 5(5):1962–1972
Svenskaya YI, Fattah H, Inozemtseva OA, Ivanova AG, Shtykov SN, Gorin DA, Parakhonskiy BV (2018) Key parameters for size- and shape-controlled synthesis of vaterite particles. Cryst Growth Des 18(1):331–337
Beck R, Andreassen J-P (2010) Spherulitic growth of calcium carbonate. Cryst Growth Des 10(7):2934–2947
Ochs M, Carregal-Romero S, Rejman J, Braeckmans K, De Smedt SC, Parak WJ (2012) Light-addressable capsules as caged compound matrix for controlled triggering of cytosolic reactions. Angew Chem Int Ed 52(2):695–699
Trushina DB, Bukreeva TV, Antipina MN (2016) Size-controlled synthesis of vaterite calcium carbonate by the mixing method: aiming for nanosized method. Cryst Growth Des 16(3):1311–1319.40
Krzyzanek V, Sporenberg N, Keller U, Guddorf J, Reichelt R, Schönhoff M (2011) Polyelectrolyte multilayer capsules: nanostructure and visualisation of nanopores in the wall. Soft Matter 7(15):7034–7041
Acknowledgments
MVZ acknowledges the President’s Scholarship SP-1576.2018.4 and the Russian Science Foundation for funding (Grant N 19-75-00039).
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Zyuzin, M.V., Ramos-Cabrer, P., Carregal-Romero, S. (2020). Encapsulation of Enzymes in Porous Capsules via Particle Templating. In: Guisan, J., Bolivar, J., López-Gallego, F., Rocha-Martín, J. (eds) Immobilization of Enzymes and Cells. Methods in Molecular Biology, vol 2100. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0215-7_15
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DOI: https://doi.org/10.1007/978-1-0716-0215-7_15
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