Biocatalytic Activity of Glucose Oxidase Immobilized on Functionalized Supports for Enzymatic Biosensors

Marco Elisio Marques; Alexandra Ancelmo Piscitelli Mansur; Herman Sander Mansur

doi:10.4028/www.scientific.net/MSF.805.77

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HomeMaterials Science ForumMaterials Science Forum Vol. 805Biocatalytic Activity of Glucose Oxidase...

Biocatalytic Activity of Glucose Oxidase Immobilized on Functionalized Supports for Enzymatic Biosensors

Abstract:

The present study reports on a novel approach for the development of enzymatic biosensor systems using chemically functionalized supports. Silica glass slides were surface-modified by reacting with organosilanes at room temperature and a glucose oxidase (GOx) enzyme layer was covalently immobilized using the bi-functional linker glutaraldehyde (GA). The activities of enzymes in solution and immobilized on hydroxyl-, amine-and thiol-modified glass surfaces were tested by sensing β-D-glucose with the horseradish peroxidase (HRP) mediated oxidation of 3,3’,5,5’-tetramethylbenzidime hydrochloride (TMB) by H₂O₂ based on biochemical reactions. The results indicated that the intensity and overall kinetics of the enzymatic catalysis were dependent on solid support chemical functionality with the amine-modified support providing the highest enzymatic catalytic activity.

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Periodical:

Materials Science Forum (Volume 805)

Pages:

77-82

DOI:

https://doi.org/10.4028/www.scientific.net/MSF.805.77

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Online since:

September 2014

Authors:

Marco Elisio Marques*, Alexandra Ancelmo Piscitelli Mansur, Herman Sander Mansur

Keywords:

Bioconjugate, Biosensor, Enzyme, Nanostructure, Surface Modification

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References

[1] P. Si, P. Kannan, L. Guo, H. Son, D.H. Kim: Biosens. Bioelectron. Vol. 26 (2011), p.3845.

Google Scholar

[2] H.S. Mansur, Z.I.P. Lobato, R.L. Oréfice, W.L. Vasconcelos, L.J.C. Machado: Biomacromolecules Vol. 1 (2000), p.789.

Google Scholar

[3] H.S. Mansur, L.J.C. Machado, W.L. Vasconcelos, Z.I. P Lobato: Spectroscopy Vol. 16 (2002), p.351.

Google Scholar

[4] A.A.P. Mansur, O.L. do Nascimento, W.L. Vasconcelos, H.S. Mansur: Mater. Res. Vol. 11 (2008), p.293.

Google Scholar

[5] H.S. Mansur, R.L. Oréfice, W.L. Vasconcelos, Z.I.P. Lobato, L.J.C. Machado: J. Mater. Sci. Mater. M. Vol. 16 (2005), p.333.

Google Scholar

[6] A. Mansur, H. Mansur, J. González: Sensors Vol. 11 (2011), p.9951.

Google Scholar

[7] Z. Guo, R.A. Guilfoyle, A.J. Thiel, R. Wang, L.M. Smith: Nucleic Acids Res. Vol. 22 (1994), p.5456.

Google Scholar

[8] P.D. Josephy, T. Eling, R. Mason: J. Biol. Chem. Vol. 257 (1982), p.3669.

Google Scholar

[9] J.M. Bolivar, F. Cava, C. Mateo, J. Rocha-Martin, J.M. Guisán, J. Berenguer, R. Fernandez-Lafuente: Appl. Microbiol. Biotechnol. Vol. 80 (2008), p.49.

DOI: 10.1007/s00253-008-1521-3

Google Scholar

[10] S.G. Rhee, T.S. Chang, W. Jeong, D. Kang: Mol. Cells Vol. 29 (2010), p.539.

Google Scholar

[11] H. Ukeda, M. Ohira, A.K. Sarker, M. Sawamura: Food Res. Int. Vol. 31 (1998), p.297.

Google Scholar

[12] P. Pandey, S.P. Singh, S.K. Arya, V. Gupta, M. Datta, S. Singh, B.D. Malhotra: Langmuir Vol. 23 (2007), p.3333.

Google Scholar

[13] L. Svobodová, M. Šnejárková, T. Hianik: Anal. Bioanal. Chem. Vol. 373 (2002), p.735.

Google Scholar

[14] G. Ozyilmaz, S.S. Tukel, O. Alptekin: J. Mol. Catal. Enzym. Vol. 35 (2005), p.154.

Google Scholar

[15] J.S. Redinha, A.M.O. Brett, J.L. C Pereira, M.A. da Silva, M.H. Gil; Bioelectrochem. Bioenerg. Vol. 22 (1989), p.379.

Google Scholar