Aminated single-walled carbon nanotubes as carrier for covalent immobilization of phenylalanine ammonia-lyase

Periodica Polytechnica Chemical Engineering

Volumn 61, Issue 1, 2017, Pages 59-66

  Bartha Vári, Judith Hajnal ^a   Bencze, László Csaba ^a   Bell, Evelin ^b   Poppe, László ^a,b,c   Katona, Gabriel ^a   Irimie, Florin Dan ^a   Paizs, Csaba ^a   Toşa, Monica Ioana ^a  

^a BABE BOLYAI UNIVERSITY   (Romania)

^b BUDAPEST UNIVERSITY OF TECHNOLOGY AND ECONOMICS   (Hungary)

^c SynBiocat Ltd   (Hungary)

Author keywords

Aminated SwCNT; Continuous flow system; Covalent immobilization; PAL

Indexed keywords

AMMONIA; BIOCATALYSTS; CHEMICAL REACTORS; IONIC LIQUIDS; PACKED BEDS; PROPIONIC ACID; SATURATED FATTY ACIDS; SINGLE-WALLED CARBON NANOTUBES (SWCN); YARN;

AMINATED SWCNT; CATALYTIC PROPERTIES; CONTINUOUS-FLOW SYSTEM; COVALENT IMMOBILIZATION; COVALENT LINKAGE; FUNCTIONALIZED; KINETIC RESOLUTION; NANO-STRUCTURED; PHENYLALANINE AMMONIA-LYASE; SINGLE-WALLED CARBON;

AMINO ACIDS;

EID: 85010726009     PISSN: 03245853     EISSN: 15873765     Source Type: Journal    
DOI: 10.3311/PPch.10417     Document Type: Article

References (33)

1. Wohlgemuth, R. “Biocatalysis—key to sustainable industrial chemistry.” Current Opinion in Biotechnology. 21, pp. 713–724. 2010. https://doi.org/10.1016/j.copbio.2010.09.016
2. Hanefeld, U., Gardossi, L., Magner, E. “Understanding enzyme immobilisation.” Chemical Society Reviews. 38, pp. 453–468. 2009. https://doi.org/10.1039/B711564B
3. Cantone, S., Ferrario, V., Corici, L., Ebert, C., Fattor, D., Spizzo, P., Gardossi, L. “Efficient immobilisation of industrial biocatalysts: criteria and constraints for the selection of organic polymeric carriers and immobilisation methods.” Chemical Society Reviews. 42, pp. 6262–6276, 2013. https://doi.org/10.1039/c3cs35464d
4. Rodrigues, R. C., Ortiz, C., Berenguer-Murcia, A., Torres, R., Fernandez-Lafuente, R. “Modifying enzyme activity and selectivity by immobilization.” Chemical Society Reviews. 42, pp. 6290-6307. 2013. https://doi.org/10.1039/c2cs35231a
5. Sheldon, R. A., van Pelt, S. “Enzyme immobilisation in biocatalysis: why, what and how.” Chemical Society Reviews. 42, pp. 6223–6235. 2013. https://doi.org/10.1039/C3CS60075K
6. Franssen, M. C. R., Steunenberg, P., Scott, E. L., Zuilhofac, H., Sanders, J. P. M. “Immobilised enzymes in biorenewables production.” Chemical Society Reviews. 42, pp. 6491–6533. 2013. https://doi.org/10.1039/c3cs00004d
7. Adlercreutz, P. “Immobilisation and application of lipases in organic me­dia.” Chemical Society Reviews. 42, pp. 6406–6436. 2013. https://doi.org/10.1039/C3CS35446F
8. Banerjee, S., Hemraj-Benny, T., Wong, S. S. “Covalent surface chemistry of single-walled carbon nanotubes.” Advanced Materials. 17, pp. 17–29. 2005. https://doi.org/10.1002/adma.200401340
9. Bandaru, P. R. “Electrical Properties and Applications of Carbon Nanotube Structures.” Journal of Nanoscience and Nanotechnology. 7, pp. 1–29. 2007. https://doi.org/10.1166/jnn.2007.307
10. Gustavsson, P., Hedmer, M., Rissler, J. “Carbon nanotubes – Exposure, toxicology and protective measures in the work environment.” (Kunskapsöversikt; Vol. Rapport 2011:1) Lund University, Lund, Sweeden, 2013. lup.lub.lu.se/record/2295102/file/2300375.pdf
11. Rummeli, M. H., Ayala, P., Pichler, T. “Carbon Nanotubes and Related Structures: Production and Formation.” In: Carbon Nanotubes and Related Structures. (Guldi, D. M., Martín, N. (eds.)) Chapter 1, Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany, 2010. https://doi.org/10.1002/9783527629930.ch1
12. Lee, H. K., Lee, J. K., Kim, M. J., Lee, J. C. “Immobilization of Lipase on Single Walled Carbon Nanotubes in Ionic Liquid.” Bulletin of the Korean Chemical Society. 31, pp. 650–652. 2010. https://doi.org/10.5012/bkcs.2010.31.03.650
13. Pavlidis, I. V., Vorhaben, T., Tsoufis, T., Rudolf, T. P., Bornscheuer, U. T., Gournis, D., Stamatis, H. “Development of effective nanobiocatalytic systems through the immobilization of hydrolases on functionalized carbon-based nanomaterials.” Bioresource Technology. 115, pp. 164–171. 2012. https://doi.org/10.1016/j.biortech.2011.11.007
14. Poppe, L., Paizs, C., Kovács, K., Irimie, F. D., Vértessy, B. G. “Preparation of Unnatural Amino Acids with Ammonia-Lyases and 2,3-Aminomutases.” Methods in Molecular Biology. 794, pp. 3–19. 2012. https://doi.org/10.1007/978-1-61779-331-8_1
15. Hamilton, B. K., Hsiao, H. Y., Swann, W. E., Anderson, D. M., Delent, J. J. “Manufacture of L-amino acids with bioreactors.” Trends in Biotechnology. 3, pp. 64–68. 1985. https://doi.org/10.1016/0167-7799(85)90079-4
16. de Lange, B., Hyett, D. J., Maas, P. J. D., Mink, D., van Assema, F. B. J., Sereinig, N., de Vries, A. H. M., de Vries, J. G. “Asymmetric Synthesis of (S)-2-Indoline-carboxylic Acid by Combining Biocatalysis and Homogeneous Catalysis.” ChemCatChem. 3, pp. 289–292. 2011. https://doi.org/10.1002/cctc.201000435
17. Wang, L., Gamez, A., Archer, H., Abola, E. E., Sarkissian, C. N., Fitzpatrick, P., Wendt, D., Zhang, Y., Vellard, M., Bliesath, J., Bell, S. M., Lemontt, J. F., Scriver, C. R., Stevens, R. C. “Structural and Biochemical Characterization of the Therapeutic Anabaena variabilis Phenylalanine Ammonia Lyase.” Journal of Molecular Biology. 38, pp. 335–623. 2008. https://doi.org/10.1016/j.jmb.2008.05.025
18. Babich, O. O., Pokrovsky, V. S., Anisimova, N. Y., Sokolov, N. N., Prosekov, A. Y. “Recombinant L-phenylalanine ammonia lyase from Rhodosporidium toruloides as a potential anticancer agent.” Biotechnology and Applied Biochemistry. 60, pp. 316–322. 2013. https://doi.org/10.1002/bab.1089
19. Bartha-Vári, J.H., Tosa, M. I., Irimie, F. D., Weiser, D., Boros, Z., Vértessy, B. G., Paizs, C., Poppe, L. “Immobilization of phenylalanine ammonia-lyase on single-walled carbon nanotubes for stereoselective biotransformation in batch and continuous-flow modes.” ChemCatChem, 7, pp. 1122–1128. 2015. https://doi.org/10.1002/cctc.201402894
20. Weiser, D., Bencze, L.C., Bánóczi, G., Ender, F., Kiss, R., Kókai, E., Szilágyi, A., Vértessy, B.G., Farkas, O., Paizs, C., Poppe, L. “Phenylalanine Ammonia-Lyase-Catalyzed Deamination of an Acyclic Amino Acid: Enzyme Mechanistic Studies Aided by a Novel Microreactor Filled with Magnetic Nanoparticles.” ChemBioChem. 16, pp. 2283–2288. 2015. https://doi.org/10.1002/cbic.201500444
21. Ender, F., Weiser, D., Nagy, B., Bencze, L. C., Paizs, C., Palovics, P., Poppe, L. “Microfluidic multiple cell chip reactor filled with enzyme-coated magnetic nanoparticles – An efficient and flexible novel tool for enzyme catalyzed biotransformations.” Journal of Flow Chemistry. 6(1), pp. 43–52. 2016. https://doi.org/10.1556/1846.2015.00036
22. Wohlgemuth, R., Plazl, I., Žnidaršič-Plazl, P., Gernaey, K., Woodley, J. “Microscale technology and biocatalytic processes: Opportunities and chal­lenges for synthesis.” Trends in Biotechnology. 33(5), pp. 302–314. 2015. https://doi.org/10.1016/j.tibtech.2015.02.010
23. Bajić, M., Plazl, I., Stloukal, R., Žnidaršič-Plazl, P. “Development of a miniaturized packed bed reactor with ω-transaminase immobilized in LentiKats.” Process Biochemistry. 52, pp. 63–72. 2017. https://doi.org/10.1016/j.procbio.2016.09.021
24. Paizs, C., Katona, A., Rétey, J. “The Interaction of Heteroaryl-Acrylates and Alanines with Phenylalanine Ammonia-Lyase from Parsley.” Chemistry-A European Journal. 12, pp. 2739–2744. 2006. https://doi.org/10.1002/chem.200501034
25. Paizs, C., Katona, A., Rétey, J. “Chemoenzymatic One-Pot Synthesis of Enantiopure L-Arylalanines from Arylaldehydes.” European Journal of Organic Chemistry. 5, pp. 1113–1116, 2006. https://doi.org/10.1002/ejoc.200500902
26. Mirzarakhmetova, D. T., Dekhkonov, D. B., Rakhimov, M. M., Abdurazakova, S. Kh., Akhmedova, Z. R. “The Properties of Invertase, Covalently Immobilized at Activated Carbon.” Applied Biochemistry and Microbiology. 3, pp. 258–261. 2009. https://doi.org/10.1134/S000368380903003X
27. −catalyzed hydrolysis of the amide bond.” International Journal of Chemical Kinetics. 41(9), pp. 599–611. 2009. https://doi.org/10.1002/kin.20435
28. Sergeeva, M. V., Mozhaev, V. V., Rich, J. O., Khmelnitsky, Y. L. “Lipase-catalyzed transamidation of non-activated amides in organic solvent.” Biotechnology Letters. 22(17), pp. 1419–1422. 2000. https://doi.org/10.1023/A:1005621117392
29. Kovács, K., Bánóczi, G., Varga, A., Szabó, I., Holczinger, A., Hornyánszky, G., Zagyva, I., Paizs, C., Vértessy, B. G., Poppe, L. “Expression and Properties of the Highly Alkalophilic Phenylalanine Ammonia-Lyase of Thermophilic Rubrobacter xylanophilus.” PLoS ONE. 9(1), e85943, 2014. https://doi.org/10.1371/journal.pone.0085943
30. Csajági, C., Szatzker, G., Tőke, E. R., Ürge, L., Darvas, F., Poppe, L., “Enantiomer selective acylation of racemic alcohols by lipases in continu­ous-flow bioreactors.” Tetrahedron: Asymmetry. 19(2), pp. 237–246. 2008. https://doi.org/10.1016/j.tetasy.2008.01.002
31. Mateo, C., Abian, O., Fernandez-Lafuente, R., Guisan, J. M. “Increase in conformational stability of enzymes immobilized on epoxy-activated supports by favoring additional multipoint covalent attachment.” Enzyme and Microbial Technology. 26(7), pp. 509–515. 2000. https://doi.org/10.1016/S0141-0229(99)00188-X
32. Mateo, C., Grazu, V., Palomo, J. M., Lopez-Gallego, F., Fernandez-Lafuente, R., Guisan J. M. “Immobilization of enzymes on heterofunctional epoxy supports.” Nature Protocols. 2, pp. 1022–1033. 2007. https://doi.org/10.1038/nprot.2007.133
33. Valikhani, D., Bolivar, J. M., Pfeiffer, M., Nidetzky, B. “Multivalency Effects on the Immobilization of Sucrose Phosphorylase in Flow Microchannels and Their Use in the Development of a High-Performance Biocatalytic Microreactor.” ChemCatChem. 2016. https://doi.org/10.1002/cctc.201601019