Effects Of Different Self-assembled Monolayers On Enzyme Immobilization Procedures In Peroxidase-based Biosensor Development

dc.creatorMendes R.K.
dc.creatorCarvalhal R.F.
dc.creatorKubota L.T.
dc.date2008
dc.date2015-06-30T19:17:12Z
dc.date2015-11-26T14:41:25Z
dc.date2015-06-30T19:17:12Z
dc.date2015-11-26T14:41:25Z
dc.date.accessioned2018-03-28T21:48:18Z
dc.date.available2018-03-28T21:48:18Z
dc.identifier
dc.identifierJournal Of Electroanalytical Chemistry. , v. 612, n. 2, p. 164 - 172, 2008.
dc.identifier220728
dc.identifier10.1016/j.jelechem.2007.09.033
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-37349023918&partnerID=40&md5=0a35b38533513f9b824b2d09aec285d2
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/105585
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/105585
dc.identifier2-s2.0-37349023918
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1250826
dc.descriptionDifferent immobilization procedures for horseradish peroxidase (HRP) were investigated using, as support matrices, self-assembled monolayers (SAM) formed on gold electrodes. The influences of these immobilization processes in the biosensor performance were also evaluated. For this, monolayers were prepared from thiols with different structures, carbon chain sizes and terminal groups. It was shown that the thiol carbon chain size influences especially in monolayer coverage and, consequently, in the biomolecule immobilization efficiency. From the studies carried out for SAM characterization on the electrode surface it was verified that thiols with shorter chains (n < 9) tend to form monolayers with a considerable amount of defects on the gold surface that lead to a lower coverage. However, thiols with a longer carbon chain present a higher coverage degree, which are not suited as substrate to the development of electrochemical biosensors, because they passivate the transduction interface, making difficult the electron transfer and, consequently, reducing electrode sensitivity. In relation to the enzyme immobilization on gold electrodes, it was verified, using different techniques, that monolayers that possess -NH2 terminal groups provided the best results, probably due to the use of glutaraldeyde as ligand during the immobilization process. Analyzing biosensor performances for hydrogen peroxide, it was verified that SAM formed by cysteamine is the most adequate for HRP immobilization, because it provides better efficiency for enzyme immobilization associated to high sensitivity for H2O2. © 2007 Elsevier B.V. All rights reserved.
dc.description612
dc.description2
dc.description164
dc.description172
dc.descriptionSuarez, G., Jackson, R.J., Spoors, J.A., McNeil, C.J., (2007) Anal. Chem., 79, pp. 1961-1969
dc.descriptionPyun, J.C., Kim, S.D., Chung, J.W., (2005) Anal. Biochem., 347, pp. 227-233
dc.descriptionJi, X.P., Jin, B.K., Jin, J.Y., Nakamura, T., (2006) J. Electroanal. Chem., 590, pp. 173-180
dc.descriptionPhong, P.H., Yamamoto, M., Kakiuchi, T., (2006) Sci. Technol. Adv. Mater., 7, pp. 552-557
dc.descriptionSchweiss, R., Werner, C., Knoll, W., (2003) J. Electroanal. Chem., 540, pp. 145-151
dc.descriptionVollhardt, D., (2005) Adv. Colloid Interface Sci., 116, pp. 63-80
dc.descriptionBain, C.D., Whitesides, G.M., (1989) Langmuir, 5, pp. 1370-1378
dc.descriptionTang, H., Zhang, W., Geng, P., Wang, Q., Jin, L., Wu, Z., Lou, M., (2006) Anal. Chim. Acta, 562, pp. 190-196
dc.descriptionVidal, J.C., Esteban, S., Gil, J., Castillo, J.R., (2006) Talanta, 68, pp. 791-799
dc.descriptionSong, Y.H., Wang, L., Ren, C.B., Zhu, G.Y., Li, Z., (2006) Sens. Actuators B, 114, pp. 1001-1006
dc.descriptionLimbutt, W., Kanatharana, P., Matisson, B., Asawatreratanakul, P., Thavarungkul, P., (2006) Anal. Chim. Acta, 561, pp. 55-61
dc.descriptionLi, A., Yang, F., Ma, Y., Yang, X., (2007) Biosens. Bioelectron., 22, pp. 1716-1722
dc.descriptionMoré, S.D., Hudecek, J., Urisu, T., (2003) Surf. Sci., 532-535, pp. 993-998
dc.descriptionCosnier, S., Molins, C., Mousty, C., Galland, B., Lepellec, A., (2006) Mater. Sci. Eng. C, 26, pp. 436-441
dc.descriptionAndrieux, C.P., Limoges, B., Savéant, J.-M., Yazidi, D., (2006) Langmuir, 22, pp. 10807-10815
dc.descriptionLimoges, B., Savéant, J.-M., Yazidi, D., (2003) J. Am. Chem. Soc., 125, pp. 9192-9203
dc.descriptionBourdillon, C., Demaille, C., Moiroux, J., Savéant, J.-M., (1999) J. Am. Chem. Soc., 121, pp. 2401-2408
dc.descriptionBourdillon, C., Demaille, C., Moiroux, J., Savéant, J.-M., (1999) J. Phys. Chem. B, 103, pp. 8532-8537
dc.descriptionBourdillon, C., Demaille, C., Moiroux, J., Savéant, J.-M., (1994) J. Am. Chem. Soc., 116, pp. 10328-10329
dc.descriptionEggins, B.R., (2004) Chemical Sensors and Biosensors, , John Wiley and Sons, England
dc.descriptionRuzgas, T., Csöregi, E., Emnéus, J., Gorton, L., Marko-Varga, G., (1996) Anal. Chim. Acta, 330, pp. 123-138
dc.descriptionFreire, R.S., Pessoa, C.A., Kubota, L.T., (2003) Quim. Nova, 26, pp. 381-389
dc.descriptionImabayashi, S., Iida, M., Hobara, D., Feng, Z.Q., Niki, K., Kakiuchi, T., (1997) J. Electroanal. Chem., 428, pp. 33-38
dc.descriptionCarvalhal, R.F., Freire, R.S., Kubota, L.T., (2005) Electroanalysis, 17, pp. 1251-1259
dc.descriptionLove, J.C., Estroff, L.A., Kriebel, J.K., Nuzzo, R.G., Whitesides, G.M., (2005) Chem. Rev., 105, pp. 1103-1170
dc.descriptionDijksma, M., Kamp, B., Hoogvliet, J.C., van Bennekom, W.P., (2000) Langmuir, 16, pp. 3852-3857
dc.descriptionSmith, R.K., Lewis, P.A., Weiss, P.S., (2004) Prog. Surf. Sci., 75, pp. 1-68
dc.descriptionCosta, P., Vasconcellos, M., Pilli, R., (2003) Substâncias Carboniladas e Derivados, , Artmed, Brazil
dc.descriptionSchreiber, F., (2000) Prog. Surf. Sci., 65, pp. 151-256
dc.descriptionMendes, R.K., Freire, R.S., Fonseca, C.P., Nves, S., Kubota, L.T., (2004) J. Braz. Chem. Soc., 15, pp. 849-855
dc.descriptionSrivastava, P., Chapman, W.G., Laibinis, P.E., (2005) Langmuir, 21, pp. 12171-12178
dc.descriptionUlman, A., (1996) Chem. Rev., 96, pp. 1533-1554
dc.descriptionChaki, N.K., Vijayamohanan, K., (2002) Biosens. Bioelectron., 17, pp. 1-12
dc.descriptionGooding, J.J., Erokhin, P., Losic, D., Yang, W., Policarpo, V., Liu, J., Ho, F.M., Hibbert, D.B., (2001) Anal. Sci., 17, pp. 3-9
dc.descriptionDing, S.J., Chang, B.W., Wu, C.C., Lai, M.F., Chang, H.C., (2005) Electrochim. Acta, 50, pp. 3660-3666
dc.descriptionCarvalho, R.M., Rath, S., Kubota, L.T., (2003) Quim. Nova, 26, pp. 97-104
dc.descriptionDamos, F.S., Mendes, R.K., Kubota, L.T., (2004) Quim. Nova, 27, pp. 970-979
dc.descriptionStenberg, E., Persson, B., Roos, H., Urbaniczky, C., (1991) Coll. Interface Sci., 1473, pp. 513-526
dc.languageen
dc.publisher
dc.relationJournal of Electroanalytical Chemistry
dc.rightsfechado
dc.sourceScopus
dc.titleEffects Of Different Self-assembled Monolayers On Enzyme Immobilization Procedures In Peroxidase-based Biosensor Development
dc.typeArtículos de revistas


Este ítem pertenece a la siguiente institución