Immobilization in biotechnology and biorecognition: from macro- to nanoscale systems

[1] Arica, M. Y., & Hasirci, V. (1993). Immobilization of glucose oxidase: a comparison of entrapment and covalent bonding. Journal of Chemical Technology and Biotechnology, 58, 287–292. DOI: 10.1002/jctb.280580313. 10.1002/jctb.280580313Search in Google Scholar

[2] Arica, M. Y., Alaeddinoğlu, N. G., & Hasirci, V. (1998). Immobilization of glucoamylase onto activated pHEMA/EGDMA microspheres: properties and application to a packed-bed reactor. Enzyme and Microbial Technology, 22, 152–157. DOI: 10.1016/s0141-0229(97)00139-7. http://dx.doi.org/10.1016/S0141-0229(97)00139-710.1016/S0141-0229(97)00139-7Search in Google Scholar

[3] Barthelmebs, L., Calas-Blanchard, C., Istamboulie, G., Marty, J. L., & Noguer, T. (2010). Biosensors as analytical tools in food fermentation industry. Bio-farms for nutraceuticals: Advances in experimental medicine and biology, 698, 293–307. DOI: 10.1007/978-1-4419-7347-4 22. http://dx.doi.org/10.1007/978-1-4419-7347-4_2210.1007/978-1-4419-7347-4Search in Google Scholar

[4] Bertók, T., Gemeiner, P., Mikula, M., & Tkac, J. (2012a). An ultrasensitive electrochemical label-free detection of a glycoprotein by a lectin-based biosensor device. Analytical and Bioanalytical Chemistry, submitted for press. Search in Google Scholar

[5] Bertók, T., Šefčovičová, J., Gemeiner, P., & Tkáč J. (2012b). Lectinomics: A tool in clinical diagnostics. Chemické Listy, 106, 20–26. (in Slovak) Search in Google Scholar

[6] Bertók, T., Šefčovičová, J., Gemeiner, P., & Tkáč J. (2012c). Development and current trends in manufacture of nanostructure biosensors. Chemické Listy, 106, 174–181. (in Slovak) Search in Google Scholar

[7] Betancor, L., & Luckarift, H. R. (2008). Bioinspired enzyme encapsulation for biocatalysis. Trends in Biotechnology, 26, 566–572. DOI: 10.1016/j.tibtech.2008.06.009. http://dx.doi.org/10.1016/j.tibtech.2008.06.00910.1016/j.tibtech.2008.06.009Search in Google Scholar PubMed

[8] Bílková, Z., Castagna, A., Zanusso, G., Farinazzo, A., Monaco, S., Damoc, E., Przybylski, M., Beneš, M., Lenfeld, J., Viovy, J. L., & Righetti, P. G. (2005). Immunoaffinity reactors for prion qualitative analysis. Proteomics, 5, 639–647. DOI: 10.1002/pmic.200401016. http://dx.doi.org/10.1002/pmic.20040101610.1002/pmic.200401016Search in Google Scholar PubMed

[9] Brady, D., & Jordaan, J. (2009). Advances in enzyme immobilization. Biotechnology Letters, 31, 1639–1650. DOI: 10.1007/s10529-009-0076-4. http://dx.doi.org/10.1007/s10529-009-0076-410.1007/s10529-009-0076-4Search in Google Scholar PubMed

[10] Bučko, M., Vikartovská, A., Lacík, I., Kolláriková, G., Gemeiner, P., Pätoprstý, V., & Brygin, M. (2005). Immobilization of a whole-cell epoxide-hydrolyzing biocatalyst in sodium alginate-cellulose sulfate-poly(methylene-co-guanidine) capsules using a controlled encapsulation process. Enzyme and Microbial Technology, 36, 118–126. DOI: 10.1016/j.enzmictec.2004.07.006. http://dx.doi.org/10.1016/j.enzmictec.2004.07.00610.1016/j.enzmictec.2004.07.006Search in Google Scholar

[11] Bučko, M., Vikartovská, A., Gemeiner, P., Lacík, I., Kolláriková, G., & Marison, I. W. (2006). Nocardia tartaricans cells immobilized in sodium alginate-cellulose sulfate-poly(methylene-co-guanidine)capsules: mechanical resistance and operational stability. Journal of Chemical Technology and Biotechnology, 81, 500–504. DOI: 10.1002/jctb.1466. http://dx.doi.org/10.1002/jctb.146610.1002/jctb.1466Search in Google Scholar

[12] Bučko, M., Gemeiner, P., Vikartovská, A., Mislovičová, D., Lacík, I., & Tkčá, J. (2010). Coencapsulation of oxygen carriers and glucose oxidase in polyelectrolyte complex capsules for the enhancement of D-gluconic acid and δ-gluconolactone production. Artificial Cells, Blood Substitutes and Biotechnology, 38, 90–98. DOI: 10.3109/10731191003634745. http://dx.doi.org/10.3109/1073119100363474510.3109/10731191003634745Search in Google Scholar PubMed

[13] Bučko, M., Schenkmayerová, A., Gemeiner, P., Vikartovská, A., Mihovilovič, M. D., & Lacík, I. (2011). Continuous testing system for Baeyer-Villiger biooxidation using recombinant Escherichia coli expressing cyclohexanone monooxygenase encapsulated in polyelectrolyte complex capsules. Enzyme and Microbial Technology, 49, 284–288. DOI: 10.1016/j.enzmictec.2011.05.013. http://dx.doi.org/10.1016/j.enzmictec.2011.05.01310.1016/j.enzmictec.2011.05.013Search in Google Scholar PubMed

[14] Chien, L. J., & Lee, C. K. (2008). Biosilicification of dual-fusion enzyme immobilized on magnetic nanoparticle. Biotechnology and Bioengineering, 100, 223–230. DOI: 10.1002/bit.21750. http://dx.doi.org/10.1002/bit.2175010.1002/bit.21750Search in Google Scholar PubMed

[15] Cowan, D. A., & Fernandez-Lafuente, R. (2011). Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization. Enzyme and Microbial Technology, 49, 326–346. DOI: 10.1016/j.enzmictec.2011.06.023. http://dx.doi.org/10.1016/j.enzmictec.2011.06.02310.1016/j.enzmictec.2011.06.023Search in Google Scholar PubMed

[16] Czichocki, G., Dautzenberg, H., Capan, E., & Vorlop, K. D. (2001). New and effective entrapment of polyelectrolyteenzyme-complexes in LentiKats. Biotechnology Letters, 23, 1303–1307. DOI: 10.1023/a:1010569322537. http://dx.doi.org/10.1023/A:101056932253710.1023/A:1010569322537Search in Google Scholar

[17] Danielsson, B., & Mosbach, K. (1988). Enzyme thermistors. In S. P. Colowick, & N. O. Kaplan (Eds.), Methods in enzymology, (Vol. 137, pp. 181–197). San Diego, CA, USA: Academic Press. Search in Google Scholar

[18] Dautzenberg, H. (1997). Polyelectrolyte complex formation in highly aggregating systems. 1. Effect of salt: Polyelectrolyte complex formation in the presence of NaCl. Macromolecules, 30, 7810–7815. DOI: 10.1021/ma970803f. http://dx.doi.org/10.1021/ma970803f10.1021/ma970803fSearch in Google Scholar

[19] Davis, J. J., Tkac, J., Laurenson, S., & Ferrigno, P. K. (2007). Peptide aptamers in label-free protein detection: 1. Characterization of the immobilized scaffold. Analytical Chemistry, 79, 1089–1096. DOI: 10.1021/ac061863z. http://dx.doi.org/10.1021/ac061863z10.1021/ac061863zSearch in Google Scholar PubMed

[20] Davis, J. J., Tkac, J., Humphreys, R., Buxton, A. T., Lee, T. A., & Ferrigno, P. K. (2009). Peptide aptamers in label-free protein detection: 2. Chemical optimization and detection of distinct protein isoforms. Analytical Chemistry, 81, 3314–3320. DOI: 10.1021/ac802513n. http://dx.doi.org/10.1021/ac802513n10.1021/ac802513nSearch in Google Scholar PubMed

[21] de Vos, P., Bučko, M., Gemeiner, P., Navrátil, M., Švitel, J., Faas, M., Strand, B. L., Skjak-Braek, G., Morch, Y. A., Vikartovská, A., Lacík, I., Kolláriková, G., Orive, G., Poncelet, D., Pedraz, J. L., & Ansorge-Schumacher, M. B. (2009). Multiscale requirements for bioencapsulation in medicine and biotechnology. Biomaterials, 30, 2559–2570. DOI: 10.1016/j.biomaterials.2009.01.014. http://dx.doi.org/10.1016/j.biomaterials.2009.01.01410.1016/j.biomaterials.2009.01.014Search in Google Scholar PubMed

[22] Ding, W. A., & Vorlop, K. D. (1995). German Patent DE No. 4327923. Munich, Germany: Deutches Patent- und Markenamt. Search in Google Scholar

[23] Eckermann, A. L., Feld, D. J., Shaw, J. A., & Meade, T. J. (2010). Electrochemistry of redox-active self-assembled monolayers. Coordination Chemistry Reviews, 254, 1769–1802. DOI: 10.1016/j.ccr.2009.12.023. http://dx.doi.org/10.1016/j.ccr.2009.12.02310.1016/j.ccr.2009.12.023Search in Google Scholar PubMed PubMed Central

[24] Fam, D. W. H., Palaniappan, A., Tok, A. I. Y., Liedberg, B., & Moochhala, S. M. (2011). A review on technological aspects influencing commercialization of carbon nanotube sensors. Sensors and Actuators B: Chemical, 157, 1–7. DOI: 10.1016/j.snb.2011.03.040. http://dx.doi.org/10.1016/j.snb.2011.03.04010.1016/j.snb.2011.03.040Search in Google Scholar

[25] Ferapontova, E. E., Shleev, S., Ruzgas, T., Stoica, L., Christenson, A., Tkac, J., Yaropolov, A. I., & Gorton, L. (2005). Direct electrochemistry of proteins and enzymes. In E. Paleček, F. Scheller, & J. Wang (Eds.), Perspectives in bioanalysis: 1 Electrochemistry of nucleic acids and proteins (pp. 517–598). London, UK: Elsevier. Search in Google Scholar

[26] Filip, J., Šefčovičová, J., Tomčík, P., Gemeiner, P., & Tkac, J. (2011). A hyaluronic acid dispersed carbon nanotube electrode used for a mediatorless NADH sensing and biosensing. Talanta, 84, 355–361. DOI: 10.1016/j.talanta.2011.01.004. http://dx.doi.org/10.1016/j.talanta.2011.01.00410.1016/j.talanta.2011.01.004Search in Google Scholar PubMed

[27] Filip, J., Gemeiner, P., Tomčík, P., & Tkáč, J. (2012a). Microbial fuel cells — features and development. Chemické Listy, 106, 158–165. (in Czech) Search in Google Scholar

[28] Filip, J., Šefčovičová, J., Gemeiner, P., & Tkac, J. (2012b). Electrochemistry of bilirubin oxidase and its use in preparation of a low cost enzymatic biofuel cell based on a renewable composite binder chitosan. Electrochimica Acta, submittedfor press. 10.1016/j.electacta.2012.09.054Search in Google Scholar

[29] Garcia-Galan, C., Berenguer-Murcia, Á., Fernandez-Lafuente, R., & Rodrigues, R. C. (2011). Potential of different enzyme immobilization strategies to improve enzyme performance. Advanced Synthesis and Catalysis, 353, 2885–2904. DOI: 10.1002/adsc.201100534. http://dx.doi.org/10.1002/adsc.20110053410.1002/adsc.201100534Search in Google Scholar

[30] Gavrilescu, M., & Chisti, Y. (2005). Biotechnology-a sustainable alternative for chemical industry. Biotechnology Advances, 23, 471–499. DOI: 10.1016/j.biotechadv.2005.03.004. http://dx.doi.org/10.1016/j.biotechadv.2005.03.00410.1016/j.biotechadv.2005.03.004Search in Google Scholar

[31] Gemeiner, P. (1992). Natural carriers for immobilized biosystems. In P. Gemeiner (Ed.), Enzyme engineering. Immobilized biosystems (pp. 15–75, pp. 110–117). Bratislava, Slovakia: Ellis Horwood & Alfa Publishers. Search in Google Scholar

[32] Gemeiner, P., Zemek, J., & Vojtisek, V. (1987). Immobilized enzymes. In P. Gemeiner (Ed.), Enzyme engineering (pp. 126–182). Bratislava, Slovakia: Alfa Publishers. (in Slovak) Search in Google Scholar

[33] Gemeiner, P., Štefuca, V., & Báleš, V. (1993). Biochemical engineering of biocatalysts immobilized on cellulose materials. Enzyme and Microbial Technology, 15, 551–566. DOI: 10.1016/0141-0229(93)90017-v. http://dx.doi.org/10.1016/0141-0229(93)90017-V10.1016/0141-0229(93)90017-VSearch in Google Scholar

[34] Gemeiner, P., Rexová-Benková, Ł., Švec, F., & Norrlöw, O. (1994). Natural and synthetic carriers suitable for immobilization of viable cells, active organelles and molecules. In I. A. Veliky, & R. J. C. McLean (Eds.), Immobilized biosystems: Theory and practical applications (pp. 1–128). London, UK: Chapman & Hall. Search in Google Scholar

[35] Gemeiner, P., Dočolomanská, P., Vikartovská, A., & Štefuca, V. (1998). Amplification of flow micro-calorimetry signal by means of multiple bioaffinity layering of lectin and glycoenzyme. Biotechnology and Applied Biochemistry, 28, 155–162. DOI: 10.1111/j.1470-8744.1998.tb00525.x. Search in Google Scholar

[36] Gemeiner, P., Mislovičová, D., Tkáč, J., Švitel, J., Pätoprstý, V., Hrabárová, E., Kogan, G., & Kožár, T. (2009). Lectinomics: II. A highway to biomedical/clinical diagnostics. Biotechnology Advances, 27, 1–15. DOI: 10.1016/j.biotechadv.2008.07.003. 10.1016/j.biotechadv.2008.07.003Search in Google Scholar PubMed

[37] Gröger, H., Capan, E., Barthuber, A., & Vorlop, K. D. (2001). Asymetric synthesis of an (R)-cyanohydrin using enzymes entrapped in lens-shaped gels. Organic Letters, 3, 1969–1972. DOI: 10.1021/ol015920g. http://dx.doi.org/10.1021/ol015920g10.1021/ol015920gSearch in Google Scholar PubMed

[38] Grosová, Z., Rosenberg, M., Rebroš, M., Šipocz, M., & Sedláčková, B. (2008). Entrapment of β-galactosidase in polyvinylalcohol hydrogel. Biotechnology Letters, 30, 763–767. DOI: 10.1007/s10529-007-9606-0. http://dx.doi.org/10.1007/s10529-007-9606-010.1007/s10529-007-9606-0Search in Google Scholar PubMed

[39] Hernandez, K., & Fernandez-Lafuente, R. (2011). Control of protein immobilization: Coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance. Enzyme and Microbial Technology, 48, 107–122. DOI: 10.1016/j.enzmictec.2010.10.003. http://dx.doi.org/10.1016/j.enzmictec.2010.10.00310.1016/j.enzmictec.2010.10.003Search in Google Scholar PubMed

[40] Homola, J. (2008). Surface plasmon resonance sensors for detection of chemical and biological species. Chemical Reviews, 108, 462–493. DOI: 10.1021/cr068107d. http://dx.doi.org/10.1021/cr068107d10.1021/cr068107dSearch in Google Scholar PubMed

[41] Hucík, M., Bučko, M., Gemeiner, P., Štefuca, V., Vikartovská, A., Mihovilovič, M. D., Rudroff, F., Iqbal, N., Chorvát, D., Jr., & Lacík, I. (2010). Encapsulation of recombinant E. coli expressing cyclopentanone monooxygenase in polyelectrolyte complex capsules for Baeyer-Villiger biooxidation of 8-oxabicyclo[3.2.1]oct-6-en-3-one. Biotechnology Letters, 32, 675–680. DOI: 10.1007/s10529-010-0203-2. http://dx.doi.org/10.1007/s10529-010-0203-210.1007/s10529-010-0203-2Search in Google Scholar PubMed

[42] Iijima, S. (1991). Helical microtubules of graphitic carbon. Nature, 354, 56–58. DOI: 10.1038/354056a0. http://dx.doi.org/10.1038/354056a010.1038/354056a0Search in Google Scholar

[43] Kalimuthu, P., Tkac, J., Kappler, U., Davis, J. J., & Bernhardt, P. V. (2010). Highly sensitive and stable electrochemical sulfite biosensor incorporating a bacterial sulfite dehydrogenase. Analytical Chemistry, 82, 7374–7379. DOI: 10.1021/ac101493y. http://dx.doi.org/10.1021/ac101493y10.1021/ac101493ySearch in Google Scholar PubMed

[44] Katrlík, J., Mastihuba, V., Voštiar, I., Šefčovičová, J., Štefuca, V., & Gemeiner, P. (2006). Amperometric biosensors based on two different enzyme systems and their use for glycerol determination in samples from biotechnological fermentation process. Analytica Chimica Acta, 566, 11–18. DOI: 10.1016/j.aca.2006.02.063. http://dx.doi.org/10.1016/j.aca.2006.02.06310.1016/j.aca.2006.02.063Search in Google Scholar

[45] Katrlík, J., Voštiar, I., Šefčovičová, J., Tkáč, J., Mastihuba, V., Valach, M., Štefuca, V., & Gemeiner, P. (2007). A novel microbial biosensor based on cells of Gluconobacter oxydans for the selective determination of 1,3-propanediol in the presence of glycerol and its application to bioprocess monitoring. Analytical and Bioanalytical Chemistry, 388, 287–295. DOI: 10.1007/s00216-007-1211-5. http://dx.doi.org/10.1007/s00216-007-1211-510.1007/s00216-007-1211-5Search in Google Scholar PubMed

[46] Katrlík, J., Švitel, J., Gemeiner, P., Kožár, T., & Tkac, J. (2010). Glycan and lectin microarrays for glycomics and medicinal applications. Medicinal Research Reviews, 30, 394–418. DOI: 10.1002/med.20195. 10.1002/med.20195Search in Google Scholar PubMed

[47] Katrlík, J., Škrabana, R., Mislovičová, D., & Gemeiner, P. (2011). Binding of D-mannose-containing glycoproteins to D-mannose-specific lectins studied by surface plasmon resonance. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 382, 198–202. DOI: 10.1016/j.colsurfa.2011.01.020. http://dx.doi.org/10.1016/j.colsurfa.2011.01.02010.1016/j.colsurfa.2011.01.020Search in Google Scholar

[48] Kim, J., Grate, J. W., & Wang, P. (2008). Nanobiocatalysis and its potential applications. Trends in Biotechnology, 26, 639–646. DOI: 10.1016/j.tibtech.2008.07.009. http://dx.doi.org/10.1016/j.tibtech.2008.07.00910.1016/j.tibtech.2008.07.009Search in Google Scholar PubMed

[49] Korecká, L., Bílková, Z., Holčápek, M., Královsky, J., Beneš, M., Lenfeld, J., Minc, N., Cecal, R., Viovy, J. L., & Przybylski, M. (2004). Utilization of newly developed immobilized enzyme reactors for preparation and study of immunoglobulin G fragments. Journal of Chromatography B, 808, 15–24. DOI: 10.1016/j.jchromb.2004.04.035. http://dx.doi.org/10.1016/j.jchromb.2004.04.03510.1016/j.jchromb.2004.04.035Search in Google Scholar PubMed

[50] Kurillova, Ł., Gemeiner, P., Vikartovska, A., Mikova, H., Rosenberg, M., & Ilavsky, M. (2000). Calcium pectate gel beads for cell entrapment. 6. Morphology of stabilized and hardened calcium pectate gel beads with cells for immobilized biotechnology. Journal of Microencapsulation, 17, 279–296. DOI: 10.1080/026520400288265. http://dx.doi.org/10.1080/02652040028826510.1080/026520400288265Search in Google Scholar PubMed

[51] Lacík, I. (2004). Polyelectrolyte complexes for microcapsule formation: In V. Nedović, & R. Willaert (Eds.), Focus on biotechnology, Fundamentals of cell immobilisation biotechnology (pp. 103–120). Dordrecht, The Netherlands: Kluwer Academic Publishers. Search in Google Scholar

[52] Lacík, I. (2006). Polymer chemistry in diabetes treatment by encapsulated islets of Langerhans: Review to 2006. Australian Journal of Chemistry, 59, 508–524. DOI: 10.1071/ch06197. http://dx.doi.org/10.1071/CH0619710.1071/CH06197Search in Google Scholar

[53] Laurent, N., Haddoub, R., & Flitsch, S. L. (2008). Enzyme catalysts on solid surfaces. Trends in Biotechnology, 26, 328–337. DOI: 10.1016/j.tibtech.2008.03.003. http://dx.doi.org/10.1016/j.tibtech.2008.03.00310.1016/j.tibtech.2008.03.003Search in Google Scholar

[54] Lozinsky, V. I., & Plieva, F. M. (1998). Poly(vinyl alcohol) cryogels employed as matrices for cell immobilization. 3. Overview of recent research and developments. Enzyme and Microbial Technology, 23, 227–242. DOI: 10.1016/s0141-0229(98)00036-2. http://dx.doi.org/10.1016/S0141-0229(98)00036-210.1016/S0141-0229(98)00036-2Search in Google Scholar

[55] Maksymovych, P., Voznyy, O., Dougherty, D. B., Sorescu, D. C., & Yates, J. T., Jr. (2010). Gold adatom as a key structural component in self-assembled monolayers of organosulfur molecules on Au(111). Progress in Surface Science, 85, 206–240. DOI: 10.1016/j.progsurf.2010.05.001. http://dx.doi.org/10.1016/j.progsurf.2010.05.00110.1016/j.progsurf.2010.05.001Search in Google Scholar

[56] Malík, F. (2006). Study of dynamic behavior of systems with immobilized biocatalyst. PhD. thesis, Slovak University of Technology, Bratislava, Slovakia. Search in Google Scholar

[57] Malík, F., & Štefuca, V. (2002). Acetylcholine esterase — dynamic behaviour with flow calorimetry. Chemical Papers, 56, 406–411. Search in Google Scholar

[58] Malík, F., Štefuca, V., & Báleš, V. (2004). Investigation of kinetics of immobilized liver esterase by flow calorimetry. Journal of Molecular Catalysis B — Enzymatic, 29, 81–87. DOI: 10.1016/j.molcatb.2003.12.016. http://dx.doi.org/10.1016/j.molcatb.2003.12.01610.1016/j.molcatb.2003.12.016Search in Google Scholar

[59] Masárová, J., Mislovičová, D., Mendichi, R., Švitel, J., Gemeiner, P., & Danielsson, B. (2004). Mannan-penicillin G acylase neoglycoproteins and their potential applications in biotechnology. Biotechnology and Applied Biochemistry, 39, 285–291. DOI: 10.1042/ba20030169. http://dx.doi.org/10.1042/BA2003016910.1042/BA20030169Search in Google Scholar

[60] Mislovičová, D., Masárová, J., Švitel, J., & Gemeiner, P. (2002a). Influence of mannan epitopes in glycoproteins-Concanavalin A interaction. Comparison of natural and synthetic glycosylated proteins. International Journal of Biological Macromolecules, 30, 251–258. DOI: 10.1016/s0141-8130(02)00035-1. 10.1016/S0141-8130(02)00035-1Search in Google Scholar

[61] Mislovicová, D., Masárová, J., Svitel, J., Mendichi, R., Soltés, L., Gemeiner, P., & Danielsson, B. (2002b). Neoglycoconjugates of mannan with bovine serum albumin and their interaction with lectin concanavalin A. Bioconjugate Chemistry, 13, 136–142. http://dx.doi.org/10.1021/bc015517u10.1021/bc015517uSearch in Google Scholar PubMed

[62] Mislovičová, D., Masárová, J., Vikartovská, A., Gemeiner, P., & Michalková, E. (2004). Biospecific immobilization of mannan-penicillin G acylase neoglycoenzyme on Concanavalin A-bead cellulose. Journal of Biotechnolology, 110, 11–19. DOI: 10.1016/j.jbiotec.2004.01.006. http://dx.doi.org/10.1016/j.jbiotec.2004.01.00610.1016/j.jbiotec.2004.01.006Search in Google Scholar PubMed

[63] Mislovičová, D., Masárová, J., Hostinová, E., Gašperík, J., & Gemeiner, P. (2006). Modulation of biorecognition of glucoamylases with Concanavalin A by glycosylation via recombinant expression. International Journal of Biological Macromolecules, 39, 286–290. DOI: 10.1016/j.ijbiomac.2006.04.005. http://dx.doi.org/10.1016/j.ijbiomac.2006.04.00510.1016/j.ijbiomac.2006.04.005Search in Google Scholar PubMed

[64] Mislovičová, D., Michálková, E., & Vikartovská, A. (2007). Immobilized glucose oxidase on different supports for biotransformation removal of glucose from oligosaccharide mixtures. Process Biochemistry, 42, 704–709. DOI: 10.1016/j.procbio.2006.11.001. http://dx.doi.org/10.1016/j.procbio.2006.11.00110.1016/j.procbio.2006.11.001Search in Google Scholar

[65] Mislovičová, D., Gemeiner, P., Kozarova, A. & Kožár, T. (2009a). Lectinomics I. Relevance of exogenous plant lectins in biomedical diagnostics. Biologia, 64, 1–19. DOI: 10.2478/s11756-009-0029-3. http://dx.doi.org/10.2478/s11756-009-0029-310.2478/s11756-009-0029-3Search in Google Scholar

[66] Mislovičová, D., Turjan, J., Vikartovská, A., & Pätoprstý, V. (2009b). Removal of D-glucose from a mixture with D-mannose using immobilized glucose oxidase. Journal of Molecular Catalysis B: Enzymatic, 60, 45–49. DOI: 10.1016/j.molcatb.2009.03.009. http://dx.doi.org/10.1016/j.molcatb.2009.03.00910.1016/j.molcatb.2009.03.009Search in Google Scholar

[67] Mislovičová, D., Pätoprstý, V., & Vikartovská, A. (2010). Enzymatic oxidation and separation of various saccharides with immobilized glucose oxidase. Applied Biochemistry and Biotechnology, 162, 1669–1677. DOI: 10.1007/s12010-010-8948-6. http://dx.doi.org/10.1007/s12010-010-8948-610.1007/s12010-010-8948-6Search in Google Scholar

[68] Mislovičová, D., Katrlík, J., Paulovičová, E., Gemeiner, P., & Tkac, J. (2012). Comparison of three distinct ELLA protocols for determination of apparent affinity constants between Con A and glycoproteins. Colloids and Surfaces B: Biointerfaces, 94, 163–169. DOI: 10.1016/j.colsurfb.2012.01.036. http://dx.doi.org/10.1016/j.colsurfb.2012.01.03610.1016/j.colsurfb.2012.01.036Search in Google Scholar

[69] Mosbach, K., & Danielsson, B. (1974). An enzyme thermistor. Biochimica et Biophysica Acta (BBA) — Enzymology, 364, 140–145. DOI: 10.1016/0005-2744(74)90141-7. http://dx.doi.org/10.1016/0005-2744(74)90141-710.1016/0005-2744(74)90141-7Search in Google Scholar

[70] Nahálka, J. (2008). Physiological aggregation of maltodextrin phosphorylase from Pyrococcus furiosus and its application in a process of batch starch degradation to α-D-glucose-1-phosphate. Journal of Industrial Microbiology & Biotechnology, 35, 219–223. DOI: 10.1007/s10295-007-0287-4. http://dx.doi.org/10.1007/s10295-007-0287-410.1007/s10295-007-0287-4Search in Google Scholar PubMed

[71] Nahálka, J., Wu, B., Shao, J., Gemeiner, P., & Wang, P. G. (2004). Production of cytidine 5′-monophospho-N-acetyl-β-D-neuraminic acid (CMP-sialic acid) using enzymes or whole cells entrapped in calcium pectate-silica-gel beads. Biotechnology and Applied Biochemistry, 40, 101–106. DOI: 10.1042/ba20030159. http://dx.doi.org/10.1042/BA2003015910.1042/BA20030159Search in Google Scholar PubMed

[72] Nahálka, J., Gemeiner, P., Bučko, M., & Wang, P. G. (2006). Bioenergy beads: A tool for regeneration of ATP/NTP in biocatalytic synthesis. Artificial Cells, Blood Substitutes and Biotechnology, 34, 515–521. DOI: 10.1080/10731190600862886. http://dx.doi.org/10.1080/1073119060086288610.1080/10731190600862886Search in Google Scholar PubMed

[73] Nahalka, J., & Nidetzky, B. (2007). Fusion to a pull-down domain: a novel approach of producing Trigonopsis variabilis D-amino acid oxidase as insoluble enzyme aggregates. Biotechnology and Bioengineering, 97, 454–461. DOI: 10.1002/bit.21244. http://dx.doi.org/10.1002/bit.2124410.1002/bit.21244Search in Google Scholar PubMed

[74] Nahálka, J., Vikartovská, A., & Hrabárová, E. (2008). A crosslinked inclusion body process for sialic acid synthesis. Journal of Biotechnolology, 134, 146–153. DOI: 10.1016/j.jbiotec.2008.01.014. http://dx.doi.org/10.1016/j.jbiotec.2008.01.01410.1016/j.jbiotec.2008.01.014Search in Google Scholar PubMed

[75] Nahálka, J., Mislovičová, D., & Kavcová, H. (2009). Targeting lectin activity into inclusion bodies for the characterisation of glycoproteins. Molecular BioSystems, 5, 819–821. DOI: 10.1039/b900526a. http://dx.doi.org/10.1039/b900526a10.1039/b900526aSearch in Google Scholar

[76] Nahálka, J., & Pätoprstý, V. (2009). Enzymatic synthesis of sialylation substrates powered by a novel polyphosphate kinase (PPK3). Organic & Biomolecular Chemistry, 7, 1778–1780. DOI: 10.1039/b822549b. http://dx.doi.org/10.1039/b822549b10.1039/b822549bSearch in Google Scholar

[77] Nahálková, J., Švitel, J., Gemeiner, P., Danielsson, B., Pribulová, B., & Petruš, L. (2002). Affinity analysis of lectin interaction with immobilized C- and O-glycosides studied by surface plasmon resonance assay. Journal of Biochemical and Biophysical Methods, 52, 11–18. DOI: 10.1016/s0165-022x(02)00016-7. http://dx.doi.org/10.1016/S0165-022X(02)00016-710.1016/S0165-022X(02)00016-7Search in Google Scholar

[78] Navrátil, M., Tkčá, J., Švitel, J., Danielsson, B., & Šturdík, E. (2001). Monitoring of the bioconversion of glycerol to dihydroxyacetone with immobilized Gluconobacter oxydans cell using thermometric flow injection analysis. Process Biochemistry, 36, 1045–1052. DOI: 10.1016/s0032-9592(00)00298-3. http://dx.doi.org/10.1016/S0032-9592(00)00298-310.1016/S0032-9592(00)00298-3Search in Google Scholar

[79] Navrátil, M., Gemeiner, P., Klein, J., Šturdík, E., Malovíková, A., Nahálka, J., Vikartovská, A., Dömény, Z., & Šmogrovičová, D. (2002). Properties of hydrogel materials used for entrapment of microbial cells in production of fermented beverages. Artifical Cells, Blood Substitutes and Immobilization Biotechnology, 30, 199–218. DOI: 10.1081/bio-120004340. http://dx.doi.org/10.1081/BIO-12000434010.1081/BIO-120004340Search in Google Scholar

[80] Ortner, V., Kaspar, C., Halter, C., Töllner, L., Mykhaylyk, O., Walzer, J., Günzburg, W. H., Dangerfield, J. A., Hohenadl, C., & Czerny, T. (2012) Magnetic field-controlled gene expression in encapsulated cells. Journal of Controlled Release, 158, 424–432. DOI: 10.1016/j.jconrel.2011.12.006. http://dx.doi.org/10.1016/j.jconrel.2011.12.00610.1016/j.jconrel.2011.12.006Search in Google Scholar

[81] Prüsse, U., Bilancetti, L., Bučko, M., Bugarski, B., Bukowski, J., Gemeiner, P., Lewińska, D., Manojlovic, V., Massart, B., Nastruzzi, C., Nedovic, V., Poncelet, D., Siebenhaar, S., Tobler, L., Tosi, A., Vikartovská, A., & Vorlop, K. D. (2008). Comparison of different technologies for alginate beads production. Chemical Papers, 62, 364–374. DOI: 10.2478/s11696-008-0035-x. http://dx.doi.org/10.2478/s11696-008-0035-x10.2478/s11696-008-0035-xSearch in Google Scholar

[82] Pumera, M. (2011). Graphene in biosensing. Materials Today, 14, 308–315. DOI: 10.1016/s1369-7021(11)70160-2. http://dx.doi.org/10.1016/S1369-7021(11)70160-210.1016/S1369-7021(11)70160-2Search in Google Scholar

[83] Rebroš, M., Rosenberg, M., Stloukal, R., & Krištofíková, Ł. (2005). High efficiency ethanol fermentation by entrapment of Zymomonas mobilis into LentiKats®. Letters in Applied Microbiology, 41, 412–416. DOI: 10.1111/j.1472-765x.2005.01770.x. http://dx.doi.org/10.1111/j.1472-765X.2005.01770.x10.1111/j.1472-765X.2005.01770.xSearch in Google Scholar PubMed

[84] Rebroš, M., Rosenberg, M., Mlichová, Z., Krištofíková, Ł., & Paluch, M. (2006). A simple entrapment of glucoamylase into LentiKats® as an efficient catalyst for maltodextrin hydrolysis. Enzyme and Microbial Technology, 39, 800–804. DOI: 10.1016/j.enzmictec.2006.01.001. http://dx.doi.org/10.1016/j.enzmictec.2006.01.00110.1016/j.enzmictec.2006.01.001Search in Google Scholar

[85] Rebroš, M., Rosenberg, M., Mlichová, Z., & Krištofíková, Ł. (2007). Hydrolysis of sucrose by invertase entrapped in polyvinyl alcohol hydrogel capsules. Food Chemistry, 102, 784–787. DOI: 10.1016/j.foodchem.2006.06.020. http://dx.doi.org/10.1016/j.foodchem.2006.06.02010.1016/j.foodchem.2006.06.020Search in Google Scholar

[86] Rich, R. L., & Myszka, D. G. (2010). Grading the commercial optical biosensor literature-Class of 2008: ‘The Mighty Binders’. Journal of Molecular Recognition, 23, 1–64. DOI: 10.1002/jmr.1004. http://dx.doi.org/10.1002/jmr.100410.1002/jmr.1004Search in Google Scholar

[87] Rodrigues, R. C., Berenguer-Murcia, á., & Fernandez-Lafuente, R. (2011). Coupling chemical modification and immobilization to improve the catalytic performance of enzymes. Advanced Synthesis and Catalysis, 353, 2216–2238. DOI: 10.1002/adsc.201100163. http://dx.doi.org/10.1002/adsc.20110016310.1002/adsc.201100163Search in Google Scholar

[88] Rosenberg, M., Rebroš, M., Krištofíková, L., & Malatová, K. (2005). High temperature lactic acid production by Bacillus coagulans immobilized in LentiKats. Biotechnology Letters, 27, 1943–1947. DOI: 10.1007/s10529-005-3907-y. http://dx.doi.org/10.1007/s10529-005-3907-y10.1007/s10529-005-3907-ySearch in Google Scholar

[89] Rotková, J., Šuláková, R., Korecká, L., Zdražilová, P., Jandová, M., Lenfeld, J., Horák, D., & Bílková, Z. (2009). Laccase immobilized on magnetic carriers for biotechnology applications. Journal of Magnetism and Magnetic Materials, 321, 1335–1340. DOI: 10.1016/j.jmmm.2009.02.034. http://dx.doi.org/10.1016/j.jmmm.2009.02.03410.1016/j.jmmm.2009.02.034Search in Google Scholar

[90] Schenkmayerová, A., Bučko, M., Gemeiner, P., Chorvát, D., & Lacík, I. (2012). Viability of free and encapsulated Escherichia coli overexpressing cyclopentanone monooxygenase monitored during model Baeyer-Villiger biooxidation by confocal laser scanning microscopy. Biotechnology Letters, 34, 309–314. DOI: 10.1007/s10529-011-0765-7. http://dx.doi.org/10.1007/s10529-011-0765-710.1007/s10529-011-0765-7Search in Google Scholar

[91] Scouten, W. H., Luong, J. H. T., & Brown, R. S. (1995). Enzyme or protein immobilization techniques for applications in biosensor design. Trends in Biotechnology, 13, 178–185. DOI: 10.1016/s0167-7799(00)88935-0. http://dx.doi.org/10.1016/S0167-7799(00)88935-010.1016/S0167-7799(00)88935-0Search in Google Scholar

[92] Šefčovičová, J., Katrlík, J., Štefuca, V., Mastihuba, V., Voštiar, I., Greif, G., Bučko, M., Tkac, J., & Gemeiner, P. (2008). A filtration probe-free on-line monitoring of glycerol during fermentation by a biosensor device. Enzyme and Microbial Technology, 42, 434–439. DOI: 10.1016/j.enzmictec.2008.01.006. http://dx.doi.org/10.1016/j.enzmictec.2008.01.00610.1016/j.enzmictec.2008.01.006Search in Google Scholar

[93] Šefčovičová, J., Vikartovská, A., Pätoprstý, V., Magdolen, P., Katrlík, J., Tkac, J., & Gemeiner, P. (2009). Off-line FIA monitoring of D-sorbitol consumption during L-sorbose production using a sorbitol biosensor. Analytica Chimica Acta, 644, 68–71. DOI: 10.1016/j.aca.2009.04.012. http://dx.doi.org/10.1016/j.aca.2009.04.01210.1016/j.aca.2009.04.012Search in Google Scholar PubMed

[94] Šefčovičová, J., Filip, J., Gemeiner, P., Vikartovská, A., Pätoprstý, V., & Tkac, J. (2011a). High performance microbial 3-D bionanocomposite as a bioanode for a mediated biosensor device. Electrochemistry Communications, 13, 966–968. DOI: 10.1016/j.elecom.2011.06.013. http://dx.doi.org/10.1016/j.elecom.2011.06.01310.1016/j.elecom.2011.06.013Search in Google Scholar

[95] Šefčovičová, J., Filip, J., Tomčík, P., Gemeiner, P., Bučko, M., Magdolen, P., & Tkac, J. (2011b). A biopolymer-based carbon nanotube interface integrated with a redox shuttle and a D-sorbitol dehydrogenase for robust monitoring of D-sorbitol. Microchimica Acta, 175, 21–30. DOI: 10.1007/s00604-011-0641-0. http://dx.doi.org/10.1007/s00604-011-0641-010.1007/s00604-011-0641-0Search in Google Scholar

[96] Šefčovičová, J., Filip, J., Mastihuba, V., Gemeiner, P., & Tkac, J. (2012). Analysis of ethanol in fermentation samples by a robust nanocomposite-based microbial biosensor. Biotechnology Letters, 34, 1033–1039. DOI: 10.1007/s10529-012-0875-x. http://dx.doi.org/10.1007/s10529-012-0875-x10.1007/s10529-012-0875-xSearch in Google Scholar

[97] Sheldon, R. A. (2011). Characteristic features and biotechnological applications of cross-linked enzyme aggregates (CLEAs). Applied Microbiology and Biotechnology, 92, 467–477. DOI: 10.1007/s00253-011-3554-2. http://dx.doi.org/10.1007/s00253-011-3554-210.1007/s00253-011-3554-2Search in Google Scholar

[98] Skerra, A. (2007). Alternative non-antibody scaffolds for molecular recognition. Current Opinion in Biotechnology, 18, 295–304. DOI: 10.1016/j.copbio.2007.04.010. http://dx.doi.org/10.1016/j.copbio.2007.04.01010.1016/j.copbio.2007.04.010Search in Google Scholar

[99] Štefuca, V., Gemeiner, P., Kurillová, Ł., Dautzenberg, H., Polakovič, M., & Báleš, V. (1991). Polyelectrolyte complex capsules as a material for enzyme immobilization. Applied Biochemistry and Biotechnology, 30, 313–324. DOI: 10.1007/bf02922035. http://dx.doi.org/10.1007/BF0292203510.1007/BF02922035Search in Google Scholar

[100] Štefuca, V., & Gemeiner, P. (1999). Investigation of catalytic properties of immobilized enzymes and cells by flow microcalorimetry. Thermal Biosensors, Bioactivity, Bioaffinitty. Advances in Biochemical Engineering — Biotechnology, 64, 69–99. DOI: 10.1007/3-540-49811-7 3. http://dx.doi.org/10.1007/3-540-49811-7_310.1007/3-540-49811-7Search in Google Scholar

[101] Štefuca, V., Čipáková, I., & Gemeiner, P. (2001). Investigation of immobilized glucoamylase kinetics by flow calorimetry. Thermochimica Acta, 378, 79–85. DOI: 10.1016/s0040-6031(01)00589-5. http://dx.doi.org/10.1016/S0040-6031(01)00589-510.1016/S0040-6031(01)00589-5Search in Google Scholar

[102] Štefuca, V., Voštiar, I., Šefčovičová, J., Katrlík, J., Mastihuba, V., Greifová, M., & Gemeiner, P. (2006). Development of enzyme flow calorimeter system for monitoring of microbial glycerol conversion. Applied Microbiology and Biotechnology, 72, 1170–1175. DOI: 10.1007/s00253-006-0420-8. http://dx.doi.org/10.1007/s00253-006-0420-810.1007/s00253-006-0420-8Search in Google Scholar

[103] Švitel, J., Dzgoev, A., Ramanathan, K., & Danielsson, B. (2000). Surface plasmon resonance based pesticide assay on a renewable biosensing surface using the reversible concanavalin A monosaccharide interaction. Biosensors and Bioelectronics, 15, 411–415. DOI: 10.1016/s0956-5663(00)00099-3. http://dx.doi.org/10.1016/S0956-5663(00)00099-310.1016/S0956-5663(00)00099-3Search in Google Scholar

[104] Švitel, J., Tkčá, J., Voštiar, I., Navrátil, M., Štefuca, V., Bučko, M., & Gemeiner, P. (2006). Gluconobacter in biosensors: applications of whole cells and enzymes isolated from gluconobacter and acetobacter to biosensor construction. Biotechnology Letters, 28, 2003–2010. DOI: 10.1007/s10529-006-9195-3. http://dx.doi.org/10.1007/s10529-006-9195-310.1007/s10529-006-9195-3Search in Google Scholar PubMed

[105] Svitel, J., Tkac, J., Vostiar, I., Navratil, M., & Gemeiner, P. (2009). Microbial biosensors and biofuel cells based on acetobacter and gluconobacter cells. In R. Comeaux, & P. Novotny (Eds.), Biosensors: Properties, materials and applications (pp. 247–264). New York, NY, USA: Nova Science Publishers. Search in Google Scholar

[106] Thümmler, K., Fisher, S., Feldner, A., Weber, V., Ettenauer, M., Loth, F., & Falkenhagen, D. (2011). Preparation and characterization of cellulose microspheres. Cellulose, 18, 135–142. DOI: 10.1007/s10570-010-9465-z. http://dx.doi.org/10.1007/s10570-010-9465-z10.1007/s10570-010-9465-zSearch in Google Scholar

[107] Tkčá, J., Gemeiner, P., Švitel, J., Benikovsky, T., Šturdík, E., Vala, V., Petruš, L., & Hrabárová, E. (2000). Determination of total sugars in lignocellulose hydrolysate by a mediated Gluconobacter oxydans biosensor. Analytica Chimica Acta, 420, 1–7. DOI: 10.1016/s0003-2670(00)01001-1. http://dx.doi.org/10.1016/S0003-2670(00)01001-110.1016/S0003-2670(00)01001-1Search in Google Scholar

[108] Tkčá, J., Navrátil, M., Šturdík, E., & Gemeiner, P. (2001a). Monitoring of dihydroxyacetone production during oxidation of glycerol by immobilized Gluconobacter oxydans cells with an enzyme biosensor. Enzyme and Microbial Technology, 28, 383–388. DOI: 10.1016/s0141-0229(00)00328-8. http://dx.doi.org/10.1016/S0141-0229(00)00328-810.1016/S0141-0229(00)00328-8Search in Google Scholar

[109] Tkčá, J., Voštiar, I., Šturdík, E., Gemeiner, P., Mastihuba, V., & Annus, J. (2001b). Fructose biosensor based on D-fructose dehydrogenase immobilised on a ferrocene-embedded cellulose acetate membrane. Analytica Chimica Acta, 439, 39–46. DOI: 10.1016/s0003-2670(01)01021-2. http://dx.doi.org/10.1016/S0003-2670(01)01021-210.1016/S0003-2670(01)01021-2Search in Google Scholar

[110] Tkčá, J., Voštiar, I., Gemeiner, P., & Šturdík, E. (2002a). Stabilization of ferrocene leakage by physical retention in a cellulose acetate membrane. The fructose biosensor. Bioelectrochemistry, 55, 149–151. DOI: 10.1016/s1567-5394(01)00130-x. http://dx.doi.org/10.1016/S1567-5394(01)00130-X10.1016/S1567-5394(01)00130-XSearch in Google Scholar

[111] Tkac, J., Vostiar, I., Gemeiner, P., & Sturdik, E. (2002b). Monitoring of ethanol during fermentation using a microbial biosensor with enhanced selectivity. Bioelectrochemistry, 56, 127–129. DOI: 10.1016/s1567-5394(02)00054-3. http://dx.doi.org/10.1016/S1567-5394(02)00054-310.1016/S1567-5394(02)00054-3Search in Google Scholar

[112] Tkac, J., Vostiar, I., Gorton, L., Gemeiner, P., & Sturdik, E. (2003). Improved selectivity of microbial biosensor using membrane coating. Application to the analysis of ethanol during fermentation. Biosensors and Bioelectronics, 18, 1125–1134. DOI: 10.1016/s0956-5663(02)00244-0. 10.1016/S0956-5663(02)00244-0Search in Google Scholar

[113] Tkčá, J., Štefuca, V., & Gemeiner, P. (2005). Biosensors with immobilised microbial cells using amperometric and thermal detection principles. In V. Nedović, & R. Willaert (Eds.), Applications of cell immobilisation biotechnology: Focus on biotechnology (pp. 549–566). Dordrecht, The Netherlands: Springer. Search in Google Scholar

[114] Tkac, J., & Ruzgas, T. (2006). Dispersion of single walled carbon nanotubes. Comparison of different dispersing strategies for preparation of modified electrodes toward hydrogen peroxide detection. Electrochemistry Communications, 8, 899–903. DOI: 10.1016/j.elecom.2006.03.028. 10.1016/j.elecom.2006.03.028Search in Google Scholar

[115] Tkac, J., Whittaker, J. W., & Ruzgas, T. (2007). The use of single walled carbon nanotubes dispersed in a chitosan matrix for preparation of a galactose biosensor. Biosensors and Bioelectronics, 22, 1820–1824. DOI: 10.1016/j.bios.2006.08.014. http://dx.doi.org/10.1016/j.bios.2006.08.01410.1016/j.bios.2006.08.014Search in Google Scholar PubMed

[116] Tkac, J., & Davis, J. J. (2008). An optimised electrode pre-treatment for SAM formation on polycrystalline gold. Journal of Electroanalytical Chemistry, 621, 117–120. DOI: 10.1016/j.jelechem.2008.04.010. http://dx.doi.org/10.1016/j.jelechem.2008.04.01010.1016/j.jelechem.2008.04.010Search in Google Scholar

[117] Tkac, J., & Davis, J. J. (2009). Label-free field effect protein sensing. In J. J. Davis (Ed.), Engineering the bioelectronic interface: Applications to analyte biosensing and protein detection (pp. 193–224). Cambridge, UK: Royal Society of Chemistry. Search in Google Scholar

[118] Tkac, J., Svitel, J., Vostiar, I., Navratil, M., & Gemeiner, P. (2009). Membrane-bound dehydrogenases from Gluconobacter sp.: Interfacial electrochemistry and direct bioelectrocatalysis. Bioelectrochemistry, 76, 53–62. DOI: 10.1016/j.bioelechem.2009.02.013. http://dx.doi.org/10.1016/j.bioelechem.2009.02.01310.1016/j.bioelechem.2009.02.013Search in Google Scholar

[119] Uhlich, T., Ulbricht, M., & Tomaschewski, G. (1996). Immobilization of enzymes in photochemically cross-linked polyvinyl alcohol. Enzyme and Microbial Technology, 19, 124–131. DOI: 10.1016/0141-0229(95)00190-5. http://dx.doi.org/10.1016/0141-0229(95)00190-510.1016/0141-0229(95)00190-5Search in Google Scholar

[120] Upadhyayula, V. K. K., & Gadhamshetty, V. (2010). Appreciating the role of carbon nanotube composites in preventing biofouling and promoting biofilms on material surfaces in environmental engineering: A review. Biotechnology Advances, 28, 802–816. DOI: 10.1016/j.biotechadv.2010.06.006. http://dx.doi.org/10.1016/j.biotechadv.2010.06.00610.1016/j.biotechadv.2010.06.006Search in Google Scholar

[121] Vaithilingam, V., & Tuch, B. E. (2011). Islet transplantation and encapsulation: an update on recent developments. The Review of Diabetic Studies, 8, 63–79. DOI: 10.1900/rds.2011.8.51. http://dx.doi.org/10.1900/RDS.2011.8.5110.1900/RDS.2011.8.51Search in Google Scholar

[122] Valach, M., Katrlík, J., Šturdík, E., & Gemeiner, P. (2009). Ethanol Gluconobacter biosensor designed for flow injection analysis: Application in ethanol fermentation off-line monitoring. Sensors and Actuators B: Chemical, 138, 581–586. DOI: 10.1016/j.snb.2009.02.017. http://dx.doi.org/10.1016/j.snb.2009.02.01710.1016/j.snb.2009.02.017Search in Google Scholar

[123] Vikartovská, A., Bučko, M., Gemeiner, P., Nahálka, J., Pätoprstý, V., & Hrabárová, E. (2004). Flow calorimetry-A useful tool for determination of immobilized cis-epoxysuccinate hydrolase activity from Nocardia tartaricans. Artifical Cells, Blood Substitutes and Biotechnology, 32, 77–89. DOI: 10.1081/BIO-120028670. http://dx.doi.org/10.1081/BIO-12002867010.1081/BIO-120028670Search in Google Scholar

[124] Vikartovská, A., Bučko, M., Mislovičová, D., Pätoprstý, V., Lacík, I., & Gemeiner, P. (2007). Improvement of the stability of glucose oxidase via encapsulation in sodium alginate-cellulose sulfate-poly(methylene-co-guanidine) capsules. Enzyme and Microbial Technology, 41, 748–755. DOI: 10.1016/j.enzmictec.2007.06.010. http://dx.doi.org/10.1016/j.enzmictec.2007.06.01010.1016/j.enzmictec.2007.06.010Search in Google Scholar

[125] Volkert, B., Wolf, B., Fischer, S., Li, N., & Lou, C. (2009). Application of modified bead cellulose as a carrier of active ingredients. Macromolecular Symposia, 280, 130–135. DOI: 10.1002/masy.200950615. http://dx.doi.org/10.1002/masy.20095061510.1002/masy.200950615Search in Google Scholar

[126] Vostiar, I., Tkac, J., Sturdik, E., & Gemeiner, P. (2002). Amperometric urea biosensor based on urease and electropolymerized toluidine blue dye as a pH-sensitive redox probe. Bioelectrochemistry, 56, 113–115. DOI: 10.1016/s1567-5394(02)00042-7. http://dx.doi.org/10.1016/S1567-5394(02)00042-710.1016/S1567-5394(02)00042-7Search in Google Scholar

[127] Vostiar, I., Tkac, J., & Mandenius, C. F. (2003). Monitoring of the heat-shock response in Escherichia coli using an optical biosensor. Analytical Biochemistry, 322, 156–163. DOI: 10.1016/j.ab.2003.07.019. http://dx.doi.org/10.1016/j.ab.2003.07.01910.1016/j.ab.2003.07.019Search in Google Scholar PubMed

[128] Vostiar, I., Tkac, J., & Mandenius, C. F. (2004). Off-line monitoring of bacterial stress response during recombinant protein production using an optical biosensor. Journal of Biotechnology, 111, 191–201. DOI: 10.1016/j.jbiotec.2004.04.007. http://dx.doi.org/10.1016/j.jbiotec.2004.04.00710.1016/j.jbiotec.2004.04.007Search in Google Scholar PubMed

[129] Vostiar, I., Tkac, J., & Mandenius, C. F. (2005). Intracellular monitoring of superoxide dismutase expression in an Escherichia coli fed-batch cultivation using on-line disruption with at-line surface plasmon resonance detection. Analytical Biochemistry, 342, 152–159. DOI: 10.1016/j.ab.2005.03.055. http://dx.doi.org/10.1016/j.ab.2005.03.05510.1016/j.ab.2005.03.055Search in Google Scholar PubMed

[130] Wang, P. (2006). Nanoscale biocatalyst systems. Current Opinion in Biotechnology, 17, 574–579. DOI: 10.1016/j.copbio.2006.10.009. http://dx.doi.org/10.1016/j.copbio.2006.10.00910.1016/j.copbio.2006.10.009Search in Google Scholar PubMed

[131] Wang, P. (2009). Multi-scale features in recent development of enzymic biocatalyst systems. Applied Biochemistry and Biotechnology, 152, 343–352. DOI: 10.1007/s12010-008-8243-y. http://dx.doi.org/10.1007/s12010-008-8243-y10.1007/s12010-008-8243-ySearch in Google Scholar PubMed

[132] Wang, Y., Li, Z., Wang, J., Li, J., & Lin, Y. (2011). Graphene and graphene oxide: biofunctionalization and applications in biotechnology. Trends in Biotechnology, 29, 205–212. DOI: 10.1016/j.tibtech.2011.01.008. http://dx.doi.org/10.1016/j.tibtech.2011.01.00810.1016/j.tibtech.2011.01.008Search in Google Scholar PubMed PubMed Central

[133] Weber, V., Ettenauer, M., Linsberger, I., Loth, F., Thümmler, K., Feldner, A., Fischer, S., & Falkenhagen, D. (2010). Funcionalization and application of cellulose microparticles as adsorbents in extracorporeal blood purification. Macromolecular Symposia, 294, 90–95. DOI: 10.1002/masy.200900042. http://dx.doi.org/10.1002/masy.20090004210.1002/masy.200900042Search in Google Scholar

[134] Wilson, L., Illanes, A., Pessela, B. C. C., Abian, O., Fernández-Lafuente, R., & Guisán, J. M. (2004). Encapsulation of crosslinked penicillin G acylase aggregates in lentikats: Evaluation of a novel biocatalyst in organic media. Biotechnology and Bioengineering, 86, 558–562. DOI: 10.1002/bit.20107. http://dx.doi.org/10.1002/bit.2010710.1002/bit.20107Search in Google Scholar PubMed

[135] Wittlich, P., Capan, E., Schlieker, M., Vorlop, K. D., & Jahnz, U. (2004). Entrapment in LentiKats®. In V. Nedović, & R. Willaert (Eds.), Fundamentals of cell immobilisation biotechnology: Focus on biotechnology (pp. 53–63). Dordrecht, The Netherlands: Kluwer Academic Publishers. Search in Google Scholar

[136] Woodman, R., Yeh, J. T. H., Laurenson, S., & Ferrigno, P. K. (2005). Design and validation of a neutral protein scaffold for the presentation of peptide aptamers. Journal of Molecular Biology, 352, 1118–1133. DOI: 10.1016/j.jmb.2005.08.001. http://dx.doi.org/10.1016/j.jmb.2005.08.00110.1016/j.jmb.2005.08.001Search in Google Scholar PubMed

[137] Yeo, L. Y., Chang, H. C., Chan, P. P. Y., & Friend, J. R. (2011). Microfluidic devices for bioapplications. Small, 7, 12–48. DOI: 10.1002/smll.201000946. http://dx.doi.org/10.1002/smll.20100094610.1002/smll.201000946Search in Google Scholar PubMed