Enzymatic reactions in confined environments

Nature Nanotechnology

Volumn 11, Issue 5, 2016, Pages 409-420

  Küchler, Andreas ^a   Yoshimoto, Makoto ^b   Luginbühl, Sandra ^a   Mavelli, Fabio ^c   Walde, Peter ^a  

^a ETH ZURICH   (Switzerland)

^b YAMAGUCHI UNIVERSITY   (Japan)

^c UNIVERSITY OF BARI   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEX NETWORKS; ENZYMATIC FUEL CELLS; ENZYMES; FUEL CELLS;

ADVANCED APPLICATIONS; BIOLOGICAL CELLS; CASCADE REACTIONS; CONFINED ENVIRONMENT; ENZYMATIC REACTION; IMMOBILIZED ENZYME; IN-VITRO; MACROMOLECULAR NETWORKS;

SURFACE REACTIONS;

ENZYME; IMMOBILIZED ENZYME;

ARTICLE; BACTERIOPHAGE; CATALYSIS; ENCAPSULATION; ENVIRONMENT; ENZYME IMMOBILIZATION; ENZYME MECHANISM; NONHUMAN; PRIORITY JOURNAL; SURFACE PROPERTY; BIOENERGY; CELL MEMBRANE; CHEMISTRY; ENZYME ACTIVE SITE; METABOLISM; NANOTECHNOLOGY; PROCEDURES; SOLUBILITY;

BIOELECTRIC ENERGY SOURCES; CATALYTIC DOMAIN; CELL MEMBRANE; ENZYMES; ENZYMES, IMMOBILIZED; NANOTECHNOLOGY; SOLUBILITY;

EID: 84966622062     PISSN: 17483387     EISSN: 17483395     Source Type: Journal    
DOI: 10.1038/nnano.2016.54     Document Type: Article

References (129)

1. Grunwald, P. Biocatalysis: Biochemical Fundamentals and Applications (Imperial College Press, 2009
2. Purich, D. L. Enzyme Kinetics: Catalysis and Control (Elsevier, 2010
3. Nagel, Z. D., & Klinman, J. P. A 21st century revisionist?s view at a turning point in enzymology. Nature Chem. Biol. 5, 543-550 (2009
4. Ellis, R. J. Macromolecular crowding: obvious but underappreciated. Trends Biochem. Sci. 26, 597-604 (2001
5. Alberts, B., et al. Molecular Biology of the Cell 6th edn (Garland Science, 2015
6. Conrado, R. J., Varner, J. D., & DeLisa, M. P. Engineering the spatial organization of metabolic enzymes: mimicking nature?s synergy. Curr. Opin. Biotechnol. 19, 492-499 (2008
7. Kunkel, J., & Asuri, P. Function, structure, and stability of enzymes confined in agarose gels. PLoS ONE 9, e86785 (2014
8. Schoffelen, S., & Van Hest, J. C. M. Chemical approaches for the construction of multi-enzyme reaction systems. Curr. Opin. Struct. Biol. 23, 613-621 (2013
9. Jia, F., Narasimhan, B., & Mallapragada, S. Materials-based strategies for multi-enzyme immobilization and co-localization: a review. Biotechnol. Bioeng. 111, 209-222 (2013
10. Van Oers, M. C. M., Rutjes, F. P. J. T., & Van Hest, J. C. M. Cascade reactions in nanoreactors. Curr. Opin. Biotechnol. 28, 10-16 (2014
11. Mateo, C., Palomo, J. M., Fernandez-Lorente, G., Guisan, J. M., & Fernandez-Lafuente, R. Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzyme Microb. Technol. 40, 1451-1463 (2007
12. Hanefeld, U., Gardossi, L., & Magner, E. Understanding enzyme immobilisation. Chem. Soc. Rev. 38, 453-468 (2009
13. Zhang, Y.-H. P. Substrate channeling and enzyme complexes for biotechnological applications. Biotechnol. Adv. 29, 715-725 (2011
14. Sheldon, R. A., & Van Pelt, S. Enzyme immobilisation in biocatalysis: why, what and how. Chem. Soc. Rev. 42, 6223-6235 (2013
15. Nelson, C. J., Li, L., & Millar, H. A. Quantitative analysis of protein turnover in plants. Proteomics 14, 579-592 (2014
16. Rodrigues, R. C., Berenguer-Murcia, Á., & Fernandez-Lafuente, R. Coupling chemical modification and immobilization to improve the catalytic performance of enzymes. Adv. Synth. Catal. 353, 2216-2238 (2011
17. Davis, B. G., & Boyer, V. Biocatalysis and enzymes in organic synthesis. Nat. Prod. Rep. 18, 618-640 (2001
18. Kobayashi, S., & Makino, A. Enzymatic polymer synthesis: an opportunity for green polymer chemistry. Chem. Rev. 109, 5288-5353 (2009
19. Busto, E., Gotor-Fernández, V., & Gotor, V. Hydrolases: catalytically promiscuous enzymes for non-conventional reactions in organic synthesis. Chem. Soc. Rev. 39, 4504-4523 (2010
20. Hollmann, F., Arends, I. W. C. E., Buehler, K., Schallmey, A., & Bühler, B. Enzyme-mediated oxidations for the chemist. Green Chem. 13, 226-265 (2011
21. Reetz, M. F. Biocatalysis in organic chemistry and biotechnology: past, present, and future. J. Am. Chem. Soc. 135, 12480-12496 (2013
22. Kazenwadel, F., Franzreb, M., & Rapp, B. E. Synthetic enzyme supercomplexes: co-immobilization of enzyme cascades. Anal. Methods 7, 4030-4037 (2015
23. Agapakis, C. M., Boyle, P. M., & Silver, P. A. Natural strategies for the spatial optimization of metabolism in synthetic biology. Nature Chem. Biol. 8, 527-535 (2012
24. Ghomashchi, F., Yu, B.-Z., Berg, O., Jain, M. K., & Gelb, M. H. Interfacial catalysis by phospholipase A2: substrate specificity in vesicles. Biochemistry 30, 7318-7329 (1991
25. Sanchez, S. A., Bagatolli, L. A., Gratton, E., & Hazlett, T. L. A two-photon view of an enzyme at work: Crotalus atrox venom PLA2 interaction with single-lipid and mixed-lipid giant unilamellar vesicles. Biophys. J. 82, 2232-2243 (2002
26. Tabaei, S. R., Rabe, M., Zetterberg, H., Zhdanov, V. P., & Höök, F. Single lipid vesicle assay for characterizing single-enzyme kinetics of phospholipid hydrolysis in a complex biological fluid. J. Am. Chem. Soc. 135, 14151-14158 (2013
27. Martinek, K., Levashov, A. V., Klyachko, N. L., Khmelnistki, Y. L., & Berezin, I. V. Micellar enzymology. Eur. J. Biochem. 155, 453-468 (1986
28. Luisi, P. L., Giomini, M., Pileni, M. P., & Robinson, B. H. Reverse micelles as hosts for proteins and small molecules. Biochim. Biophys. Acta 947, 209-246 (1988
29. Carvalho, C. M. L., & Cabral, J. M. S. Reverse micelles as reaction media for lipases. Biochimie 82, 1063-1085 (2000
30. Grandbois, M., Clausen-Schaumann, H., & Gaub, H. Atomic force microscope imaging of phospholipid bilayer degradation by phospholipase A2. Biophys. J. 74, 2398-2404 (1998
31. Dutta, D., Pulsipher, A., & Yousaf, M. N. PI3 kinase enzymology on fluid lipid bilayers. Analyst 139, 5127-5133 (2014
32. Fornera, S., et al. Sequential immobilization of enzymes in microfluidic channels for cascade reactions. ChemPlusChem 77, 98-101 (2012
33. Küchler, A., Bleich, J. N., Sebastian, B., Dittrich, P. S., & Walde, P. Stable and simple immobilization of proteinase K inside glass tubes and microfluidic channels. ACS Appl. Mater. Interfaces 7, 25970-25980 (2015
34. Yu, J., Zhang, Y., & Liu, S. Enzymatic reactivity of glucose oxidase confined in nanochannels. Biosens. Bioelectron. 55, 307-312 (2014
35. Johnson, B. J., Algar, W. R., Malanoski, A. P., Ancona, M. G., & Medintz, I. L. Understanding enzymatic acceleration at nanoparticle interfaces: approaches and challenges. Nano Today 9, 102-131 (2014
36. Vashist, S. K., Lam, E., Hrapovic, S., Male, K. B., & Luong, J. H. T. Immobilization of antibodies and enzymes on 3 aminopropyltriethoxysilane-functionalized bioanalytical platforms for biosensors and diagnostics. Chem. Rev. 114, 11083-11130 (2014
37. Palazzo, G., Colafemmina, G., Guzzoni Iudice, C., & Mallardi, A. Three immobilized enzymes acting in series in layer by layer assemblies: exploiting the trehalase-glucose oxidase-horseradish peroxidase cascade reactions for the optical determination of trehalose. Sensor. Actuat. B 202, 217-223 (2014
38. Fornera, S., Bauer, T., Schlüter, A. D., & Walde, P. Simple enzyme immobilization inside glass tubes for enzymatic cascade reactions. J. Mater. Chem. 22, 502-511 (2012
39. Küchler, A., Adamcik, J., Mezzenga, R., Schlüter, A. D., & Walde, P. Enzyme immobilization on silicate glass through simple adsorption of dendronized polymer-enzyme conjugates for localized enzymatic cascade reactions. RSC Adv. 5, 44530-44544 (2015
40. Linko, V., Eerikäinen, M., & Kostiainen, M. A. A modular DNA origami-based enzyme cascade nanoreactor. Chem. Commun. 51, 5351-5354 (2015
41. Castellana, M., et al. Enzyme clustering accelerates processing of intermediates through metabolic channeling. Nature Biotechnol. 32, 1011-1018 (2014
42. Fu, J., Liu, M., Liu, Y., Woodbury, N. W., & Yan, H. Interenzyme substrate diffusion for an enzyme cascade organized on spatially addressable DNA nanostructures. J. Am. Chem. Soc. 134, 5516-5519 (2012
43. Wu, F., & Minteer, S. Krebs cycle metabolon: structural evidence of substrate channeling revealed by cross-linking and mass spectrometry. Angew. Chem. Int. Ed. 54, 1851-1854 (2015
44. Dueber, J. E., et al. Synthetic protein scaffolds provide modular control over metabolic flux. Nature Biotechnol. 27, 753-759 (2009
45. Gustafsson, H., Küchler, A., Holmberg, K., & Walde, P. Co-immobilization of enzymes with the help of a dendronized polymer and mesoporous silica nanoparticles. J. Mater. Chem. B 3, 6174-6184 (2015
46. Kang, W., et al. Cascade biocatalysis by multienzyme-nanoparticle assemblies. Bioconjugate Chem. 25, 1387-1394 (2014
47. You, C.-C., Agasti, S. S., De, M., Knapp, M. J., & Rotello, V. M. Modulation of the catalytic behavior of α-chymotrypsin at monolayer-protected nanoparticle surfaces. J. Am. Chem. Soc. 128, 14612-14618 (2006
48. Kim, J., Jia, H., & Wang, P. Challenges in biocatalysis for enzyme-based biofuel cells. Biotechnol. Adv. 24, 296-308 (2006
49. Willner, I., Yan, Y.-M., Willner, B., & Tel-Vered, R. Integrated enzyme-based biofuel cells: a review. Fuel Cells 9, 7-24 (2009
50. Osman, M. H., Shah, A. A., & Walsh, F. C. Recent progress and continuing challenges in bio-fuel cells. Part I: enzymatic cells. Biosens. Bioelectron. 26, 3087-3102 (2011
51. Leech, D., Kavanagh, P., & Schuhmann, W. Enzymatic fuel cells: recent progress. Electrochim. Acta 84, 223-234 (2012
52. Kim, Y. H., Campbell, E., Yu, J., Minteer, S. D., & Banta, S. Complete oxidation of methanol in biobattery devices using a hydrogel created from three modified dehydrogenases. Angew. Chem. 125, 1477-1480 (2013
53. de Poulpiquet, A., Ciaccafava, A., & Lojou, A. New trends in enzyme immobilization at nanostructured interfaces for efficient electrocatalysis in biofuel cells. Electrochim. Acta 126, 104-114 (2014
54. Luz, R. A. S., Pereira, A. R., de Souza, J. C. P., Sales, F. C. P. F., & Crespilho, F. N. Enzyme biofuel cells: thermodynamics, kinetics and challenges in applicability. ChemElectroChem 1, 1751-1777 (2014
55. Heller, A., & Feldman, B. Electrochemical glucose sensors and their applications in diabetes management. Chem. Rev. 108, 2482-2505 (2008
56. Tsujimura, S., Murata, K., & Akatsuka, W. Exceptionally high glucose current on a hierarchically structured porous carbon electrode with ?wired? flavin adenine dinucleotide-dependent glucose dehydrogenase. J. Am. Chem. Soc. 136, 14432-14437 (2014
57. Ohara, T. J., Rajagopalan, R., & Heller, A. Glucose electrodes based on cross-linked [Os(bpy)2CI]+/2+ complexed poly(1-vinylimidazole) films. Anal. Chem. 65, 3512-3517 (1993
58. Junker, K., et al. Mechanistic aspects of the horseradish peroxidase-catalysed polymerisation of aniline in the presence of AOT vesicles as templates. RSC Adv. 2, 6478-6495 (2012
59. Walde, P., Umakoshi, H., Stano, P., & Mavelli, F. Emergent properties arising from the assembly of amphiphiles. Artificial vesicle membranes as reaction promoters and regulators. Chem. Commun. 50, 10177-10197 (2014
60. Chen, A. H., & Silver, P. A. Designing biological compartmentalization. Trends Cell Biol. 22, 662-670 (2012
61. Satori, C. P., et al. Bioanalysis of eukaryotic organelles. Chem. Rev. 113, 2733-2811 (2013
62. Chowdhury, C., Sinha, S., Chun, S., Yeates, T. O., & Bobik, T. A. Diverse bacterial microcompartment organelles. Microbiol. Mol. Biol. Rev. 78, 438-468 (2014
63. Yeates, T. O., Kerfeld, C. A., Heinhorst, S., Cannon, G. C., & Shively, J. M. Protein-based organelles in bacteria: carboxysomes and related microcompartments. Nature Rev. Microbiol. 6, 681-691 (2008
64. Lee, H., DeLoache, W. C., & Dueber, J. E. Spatial organization of enzymes for metabolic engineering. Metabol. Eng. 14, 242-251 (2012
65. Cannon, G. C., Heinhorst, S., & Kerfeld, C. A. Carboxysomal carbonic anhydrases: structure and role in microbial CO2 fixation. Biochim. Biophys. Acta 1804, 382-392 (2010
66. Kerfeld, C. A., Heinhorst, S., & Cannon, G. C. Bacterial microcompartments. Annu. Rev. Microbiol. 64, 391-408 (2010
67. Heinhorst, S., et al. Characterization of the carboxysomal carbonic anhydrase CsoSCA from Halothiobacillus neapolitanus. J. Bacteriol. 188, 8087-8094 (2006
68. Walde, P., & Ichikawa, S. Enzymes inside lipid vesicles: preparation, reactivity and applications. Biomol. Eng. 18, 143-177 (2001
69. Walde, P., Cosentino, K., Engel, H., & Stano, P. Giant vesicles: preparations and applications. ChemBioChem 11, 848-865 (2010
70. Theberge, A. B., et al. Microdroplets in microfluidics: an evolving platform for discoveries in chemistry and biology. Angew. Chem. Int. Ed. 49, 5846-5868 (2010
71. Christensen, S. M., Bolinger, P.-Y., Hatzakis, N. S., Mortensen, M. W., & Stamou, D. Mixing subattolitre volumes in a quantitative and highly parallel manner with soft matter nanofluidics. Nature Nanotech. 7, 51-55 (2012
72. Miyake, Y. Enzymatic reaction in water-in-oil microemulsions. Colloid. Surf. A 109, 255-262 (1996
73. Ruckenstein, E., & Karpe, P. Enzymatic super- and subactivity in nonionic reverse micelles. J. Phys. Chem. 95, 4869-4882 (1991
74. Walde, P., & Marzetta, B. Bilayer permeability-based substrate selectivity of an enzyme in liposomes. Biotechnol. Bioeng. 57, 216-219 (1998
75. Yoshimoto, M., Okamoto, M., Ujihashi, K., & Okita, T. Selective oxidation of d-Amino acids catalyzed by oligolamellar liposomes intercalated with d-Amino acid oxidase. Langmuir 30, 6180-6186 (2014
76. Chowdhury, C., et al. Selective molecular transport through the protein shell of a bacterial microcompartment organelle. Proc. Natl Acad. Sci. USA 112, 2990-2995 (2015
77. Glasgow, J. E., Asensio, M. A., Jakobson, C. M., Francis, M. B., & Tullman-Ercek, D. Influence of electrostatics on small molecule flux through a protein nanoreactor. ACS Synth. Biol. 4, 1011-1019 (2015
78. Weitz, M., et al. Diversity in the dynamical behaviour of a compartmentalized programmable biochemical oscillator. Nature Chem. 6, 295-302 (2014
79. Karig, D. K., Jung, S.-Y., Srijanto, B., Collier, C. P., & Simpson, M. L. Probing cell-free gene expression noise in femtoliter volumes. ACS Synth. Biol. 2, 497-505 (2013
80. Sintra, T. E., Ventura, S. P. M., & Coutinho, J. A. P. Superactivity induced by micellar systems as the key for boosting the yield of enzymatic reactions. J. Mol. Catal. B 107, 140-151 (2014
81. Moyano, F., Falcone, R. D., Mejuto, J. C., Silber, J. J., & Correa, N. M. Cationic reverse micelles create water with super hydrogen-bond-donor capacity for enzymatic catalysis: hydrolysis of 2-naphthyl acetate by α-chymotrypsin. Chem. Eur. J. 16, 8887-8893 (2010
82. Biswas, R., et al. Spectroscopic studies of catanionic reverse microemulsion: correlation with the superactivity of horseradish peroxidase enzyme in a restricted environment. J. Phys. Chem. B 112, 6620-6628 (2008
83. Moniruzzaman, M., Kamiya, N., & Goto, M. Biocatalysis in water-in-ionic liquid microemulsions: a case study with horseradish peroxidase. Langmuir 25, 977-982 (2009
84. Pereira de Souza, T., Stano, P., & Luisi, P. L. The minimal size of liposome-based model cells brings about a remarkably enhanced entrapment and protein synthesis. ChemBioChem 10, 1056-1063 (2009
85. Nourian, Z., Roelofsen, W., & Danelon, C. Triggered gene expression in fed-vesicle microreactors with a multifunctional membrane. Angew. Chem. Int. Ed. 51, 3114-3118 (2012
86. Nishimura, K., Tsuru, S., Suzuki, H., & Yomo, T. Stochasticity in gene expression in a cell-sized compartment. ACS Synth. Biol. 4, 566-576 (2015
87. Mavelli, F., & Stano, P. Experiments and numerical modelling on the capture and concentration of transcription-Translation machinery inside vesicles. Artif. Life 21, 1-19 (2015
88. Petrovics, I., et al. Antagonism of paraoxon intoxication by recombinant phosphotriesterase encapsulated within sterically stabilized liposomes. Toxicol. Appl. Pharmacol. 156, 56-63 (1999
89. Torchilin, V. Recent advances with liposomes as pharmaceutical carriers. Nature Rev. Drug. Discov. 4, 145-160 (2005
90. Yoshimoto, M., et al. Novel immobilized liposomal glucose oxidase system using the channel protein OmpF and catalase. Biotechnol. Bioeng. 90, 231-238 (2005
91. Peters, R. J. R. W., et al. Cascade reactions in multicompartmentalized polymersomes. Angew. Chem. Int. Ed. 53, 146-150 (2014
92. Louzao, I., & Van Hest, J. C. M. Permeability effects on the efficiency of antioxidant nanoreactors. Biomacromolecules 14, 2364-2372 (2013
93. Patterson, D. P., Schwarz, B., Waters, R. S., Gedeon, T., & Douglas, T. Encapsulation of an enzyme cascade within the bacteriophage P22 virus-like particle. ACS Chem. Biol. 9, 359-365 (2014
94. Chen, R., et al. Biomolecular scaffolds for enhanced signaling and catalytic efficiency. Curr. Opin. Biotechnol. 28, 59-68 (2014
95. Patterson, D. P., Prevelige, P. E., & Douglas, T. Nanoreactors by programmed enzyme encapsulation inside the capsid of the bacteriophage P22. ACS Nano 6, 5000-5009 (2012
96. Bobik, T. A., Lehman, B. P., & Yeates, T. O. Bacterial microcompartments: widespread prokaryotic organelles for isolation and optimization of metabolic pathways. Mol. Microbiol. 98, 193-207 (2015
97. Ariga, K., et al. Enzyme nanoarchitectonics: organization and device application. Chem. Soc. Rev. 42, 6322-6345 (2013
98. Rasmussen, M., Abdellaoui, S., & Minteer, S. D. Enzymatic biofuel cells: 30 years of critical advancements. Biosens. Bioelectron. 76, 91-102 (2016
99. Marguet, M., Bonduelle, C., & Lecommandoux, S. Multicompartmentalized polymeric systems: towards biomimetic cellular structure and function. Chem. Soc. Rev. 42, 512-529 (2013
100. Tanner, P., Balasubramanian, V., & Palivan, C G. Aiding nature?s organelles: artificial peroxisomes play their role. Nano Lett. 13, 2875-2883 (2013
101. Kim, E. Y., & Tullman-Ercek, D. Engineering nanoscale protein compartments for synthetic organelles. Curr. Opin. Biotechnol. 24, 627-632 (2013
102. Hansen, M. M. K., et al. Macromolecular crowding creates heterogeneous environments of gene expression in picolitre droplets. Nature Nanotech. 11, 191-197 (2016
103. Stano, P., & Luisi, P. L. Achievements and open questions in the self-reproduction of vesicles and synthetic minimal cells. Chem. Commun. 46, 3639-3653 (2010
104. Ishitsuka, Y., Okumus, B., Arslan, S., Chen, K. H., & Ha, T. Temperature-independent porous nanocontainers for single-molecule fluorescence studies. Anal. Chem. 82, 9694-9701 (2010
105. Christensen, A. L., Lohr, C., Christensen, S. M., & Stamou, D. Single vesicle biochips for ultra-miniaturized nanoscale fluidics and single molecule bioscience. Lab Chip 13, 3613-3625 (2013
106. Piwonski, H. M., Goomanovsky, M., Bensimon, D., Horovitz, A., & Haran, G. Allosteric inhibition of individual enzyme molecules trapped in lipid vesicles. Proc. Natl Acad. Sci. USA 109, E1437-E1443 (2012
107. Pavlidis, I. V., Patila, M., Bornscheuer, U. T., Gournis, D., & Stamatis, H. Graphene-based nanobiocatalytic systems: recent advances and future prospects. Trends Biotechnol. 32, 312-320 (2014
108. Fang, W., & Ji, P. Enzymes immobilized on carbon nanotubes. Biotechnol. Adv. 29, 889-895 (2011
109. Magner, E. Immobilisation of enzymes on mesoporous silicate materials. Chem. Soc. Rev. 42, 6213-6266 (2013
110. Nandiyanto, A. B. D., Kim, S.-G., Iskandar, F., & Okuyama, K. Synthesis of spherical mesoporous silica nanoparticles with nanometer-size controllable pores and outer diameters. Micropor. Mesopor. Mater. 120, 447-453 (2009
111. Jia, H., Zhu, G., & Wang, P. Catalytic behaviors of enzymes attached to nanoparticles: the effect of particle mobility. Biotechnol. Bioeng. 84, 406-414 (2003
112. Yoshimoto, M., Sakamoto, H., & Shirakami, H. Covalent conjugation of tetrameric bovine liver catalase to liposome membranes for stabilization of the enzyme tertiary and quaternary structures. Colloid. Surf. B 69, 281-287 (2009
113. Huang, X., Li, M., & Mann, S. Membrane-mediated cascade reactions by enzyme-polymer proteinosomes. Chem. Commun. 50, 6278-6280 (2014
114. Park, M., Sun, Q., Liu, F., DeLisa, M., & Chen, W. Positional assembly of enzymes on bacterial outer membrane vesicles for cascade reactions. PLoS ONE 9, e97103 (2014
115. Liu, F., Banta, S., & Chen, W. Functional assembly of a multi-enzyme methanol oxidation cascade on a surface-displayed trifunctional scaffold for enhanced NADH production. Chem. Commun. 49, 3766-3768 (2013
116. Meredith, M. T., & Minteer, S. D. Biofuel cells: enhanced enzymatic bioelectrocatalysis. Annu. Rev. Anal. Chem. 5, 157-179 (2012
117. Orlich, B., & Schomäcker, R. Enzyme catalysis in reverse micelles. Adv. Biochem. Eng. Biotechnol. 75, 185-208 (2002
118. Liu, Y., Jung, S.-Y., & Collier, C. P. Shear-driven redistribution of surfactant affects enzyme activity in well-mixed femtoliter droplets. Anal. Chem. 81, 4922-4928 (2009
119. Nardin, C., Widmer, J., Winterhalter, M., & Meier, W. Amphiphilic block copolymer nanocontainers as bioreactors. Eur. Phys. J. E 4, 403-410 (2001
120. Chen, Q., Schönherr, H., & Vancso, G. J. Block-copolymer vesicles as nanoreactors for enzymatic reactions. Small 5, 1436-1445 (2009
121. Vriezema, D. M., et al. Positional assembly of enzymes in polymersome nanoreactors for cascade reactions. Angew. Chem. 119, 7522-7526 (2007
122. Hansen, J. S., Elbing, K., Thompson, J. R., Malmstadt, N., & Lindkvist-Petersson, K. Glucose transport machinery reconstituted in cell models. Chem. Commun. 51, 2316-2319 (2015
123. Comellas-Aragonès, M., et al. A virus-based single-enzyme nanoreactor. Nature Nanotech. 2, 635-639 (2007
124. Price, A. D., Zelikin, A. N., Wang, Y., & Caruso, F. Triggered enzymatic degradation of DNA within selectively permeable polymer capsule microreactors. Angew. Chem. Int. Ed. 48, 329-332 (2009
125. Kreft, O., Prevot, M., Möhwald, H., & Sukhorukov, G. B. Shell-in-shell microcapsules: a novel tool for integrated, spatially confined enzymatic reactions. Angew. Chem. Int. Ed. 46, 5605-5608 (2007
126. Sakr, O. S., & Borchard, G. Encapsulation of enzymes in layer-by-layer (LbL) structures: latest advances and applications. Biomacromolecules 14, 2117-2135 (2013
127. Hosta-Rigau, L., York-Duran, M. J., Zhang, Y., Goldie, K. N., & Städler, B. Confined multiple enzymatic (cascade) reactions within poly(dopamine)-based capsosomes. ACS Appl. Mater. Interfaces 6, 12771-12779 (2014
128. Gorris, H. H., & Walt, D. R. Mechanistic aspects of horseradish peroxidase elucidated through single-molecule studies. J. Am. Chem. Soc. 131, 6277-6282 (2009
129. Liebherr, R. B., & Gorris, H. H. Enzyme molecules in solitary confinement. Molecules 19, 14417-14445 (2014