Stabilization of horseradish peroxidase by covalent conjugation with dextran aldehyde against temperature and pH changes

• Authors: Melda Altikatoglu , Candan Arioz , Yeliz Basaran , Huriye Kuzu
• Languages of publication: EN

Abstracts

EN

Stabilization of Horseradish Peroxidase (HRP; EC 1.11.1.7) against temperature and pH via the formation of the conjugates obtained by multipoint covalent bonding of dextran aldehyde (DA) to the enzyme were studied. Hence, three different molar weighted dextrans (17.5 kD, 75 kD, 188 kD) were covalently bonded to purified enzyme with different molar ratios (nHRP/nDA 20/1, 10/1, 1/1, 1/5, 1/10, 1/15, 1/20). The thermal stabilities of the obtained conjugates were evaluated with the activities determined at different temperatures (25, 30, 35, 40, 50, 60, 70, 80°C) applying 60 minutes incubation time. Conjugates formed were characterized by gel-permeation chromatography (GPC) and fluorescence techniques. The conjugate synthesized using dextran 75 kDa with nHRP/nDA 1/10 molar ratio showed better thermal stability than other conjugates and purified enzyme at pH 7. This conjugate also has wider activity pH range than purified enzyme. In addition, mentioned conjugate at pH 7 had very long storage lifetime compared to purified enzyme at +4°C and room temperature; which is considered a favorable feature for usage in practice. [...]

Keywords

EN

Enzyme stabilization; Covalent conjugate; Horseradish peroxidase; Dextran; GPC

• Publisher: De Gruyter Open
• Journal: Open Chemistry
• Year: 2009
• Volume: 7
• Issue: 3
• Pages: 423-428

Dates

published

1 - 9 - 2009

online

21 - 6 - 2009

Contributors

author

Melda Altikatoglu

• Faculty of Arts and Sciences, Department of Chemistry, Yildiz Technical University, Davutpasa Campus, 34210, Esenler, Istanbul, Turkey

author

Candan Arioz

• Faculty of Chemical and Metallurgical Engineering, Department of Bioengineering, Yildiz Technical University, Davutpasa Campus, 34210, Esenler, Istanbul, Turkey

author

Yeliz Basaran

• Faculty of Chemical and Metallurgical Engineering, Department of Bioengineering, Yildiz Technical University, Davutpasa Campus, 34210, Esenler, Istanbul, Turkey

author

Huriye Kuzu

• Faculty of Chemical and Metallurgical Engineering, Department of Bioengineering, Yildiz Technical University, Davutpasa Campus, 34210, Esenler, Istanbul, Turkey

References

• [1] C. Ó’Fágáain, Enzym. Microb. Technol. 33, 137 (2003) http://dx.doi.org/10.1016/S0141-0229(03)00160-1[Crossref]
• [2] S.S. Despande, Enzyme immunoassays: from concept to product development (Chapman and Hall, New York, 1996) 149
• [3] S. Kumar, C-J. Tsai, R. Nussinov, Protein Eng. 13, 179 (2000) http://dx.doi.org/10.1093/protein/13.3.179[Crossref]
• [4] M.A. Longo, D. Combes, J. Chem. Biotechnol. 74, 25 (1999) http://dx.doi.org/10.1002/(SICI)1097-4660(199901)74:1<25::AID-JCTB978>3.0.CO;2-B[Crossref]
• [5] K. Chattopadhyay, S. Mazumdar, Biochemistry 39, 263 (2001) http://dx.doi.org/10.1021/bi990729o[Crossref]
• [6] M. Sola-Penna, J.R. Meyer-Fernandes, Arch. Biochem. Biophys. 360, 10 (1998) http://dx.doi.org/10.1006/abbi.1998.0906[Crossref]
• [7] J.Z. Liu, H.Y. Song, L.P. Weng, L.N. Ji, J. Mol. Catal. B: Enzym. 18, 225 (2002) http://dx.doi.org/10.1016/S1381-1177(02)00100-5[Crossref]
• [8] R. Wimmer, M. Olsson, M.T.N. Petersen, R. Hatti-Kaul, S.B. Petersen, N. Muller, J. Biotechnol. 55, 85 (1997) http://dx.doi.org/10.1016/S0168-1656(97)00061-8[Crossref]
• [9] L. Betancor, F. López-Gallego, A. Hidalgo, N. Alonso-Morales, M. Fuentes, R. Fernández-Lafuente, J.M. Guisán, J. Biotechnol. 110, 201 (2004) http://dx.doi.org/10.1016/j.jbiotec.2004.02.003[Crossref]
• [10] C. Kühlmeyer, J. Klein, Enzym. Microb. Technol. 32, 99 (2003) http://dx.doi.org/10.1016/S0141-0229(02)00243-0[Crossref]
• [11] V. Arasaratnam, I.Y. Galaev, B. Mattiason, Enzym. Microb. Technol. 27, 254 (2000) http://dx.doi.org/10.1016/S0141-0229(00)00195-2[Crossref]
• [12] V. Sanz, S. de Marcos, J.R. Castillo, J. Galban, J. Am. Chem. Soc. 127, 1038 (2005) http://dx.doi.org/10.1021/ja046830k[Crossref]
• [13] N.C Veitch, C. Nigel, Phytochemistry 65, 249 (2004) http://dx.doi.org/10.1016/j.phytochem.2003.10.022[Crossref]
• [14] I.J. Castellanos, R. Crespo, K. Griebenow, J. Control Release. 88, 135 (2003) http://dx.doi.org/10.1016/S0168-3659(02)00488-1[Crossref]
• [15] Y. Murakami, R. Hoshi, A. Hirata, J. Mol. Catal. B: Enzym. 22, 79 (2003) http://dx.doi.org/10.1016/S1381-1177(03)00009-2[Crossref]
• [16] M.A.M.E. Vertommen, V.A Nierstrasz, M. van der Veer, M.M.C.G Warmoeskerken, J. Biotechnol. 120, 376 (2005) http://dx.doi.org/10.1016/j.jbiotec.2005.06.015[Crossref]
• [17] Y. Murakami, A. Hirata, J. Biotechnol. Bioeng. 88, 441 (1999)
• [18] A.M. O’Brien, C. O’Fágáin, P.F. Nielsen, K. Welinder, Biotechnol. Bioeng. 76, 277 (2001) http://dx.doi.org/10.1002/bit.1194[Crossref]
• [19] A. Abian, O. Wilson, L. Mateo, C, Fernández-Lorento, G. Palomo, J.M. Fernández-Lafuente, J.M. Gusian, D. Re, A. Tam, M. Damianti, J. Mol. Catal. B: Enzym. 19–20, 295 (2002) http://dx.doi.org/10.1016/S1381-1177(02)00180-7[Crossref]
• [20] C. Mateo, O. Abian, R. Fernandez-Lafuente, J.M. Guisan, Enzyme Microb. Technol. 26, 509 (2000) http://dx.doi.org/10.1016/S0141-0229(99)00188-X[Crossref]
• [21] A.S. Dilgimen, Z. Mustafaeva, M. Demchenko, T. Kaneko, Y. Osada, M. Mustafaev, Biomaterials 22, 2383 (2001) http://dx.doi.org/10.1016/S0142-9612(00)00425-7[Crossref]
• [22] A. Başalp, E. Bermek, B. Çırakoğlu, V. Çoka, M.I. Mustafaev, A.S. Saraç, Hybridoma 15, 233 (1996) http://dx.doi.org/10.1089/hyb.1996.15.233[Crossref]
• [23] P. Christakopoulos, E. Kourentzi, D.G. Hatzinikolaou, M. Claeyssens, D. Kekos, B.J. Macris, Carbohydr. Res. 314, 95 (1998) http://dx.doi.org/10.1016/S0008-6215(98)00284-5[Crossref]
• [24] F-Y. Jeng, S-C. Lin, Proc. Biochem. 41, 1566 (2006) http://dx.doi.org/10.1016/j.procbio.2006.02.021[Crossref]
• [25] R.M. De la Casa, J.M. Guisán, J.M. Sánchez-Montero, J.V. Sinisterra, Enzym. Microb. Technol. 30, 30 (2002) http://dx.doi.org/10.1016/S0141-0229(01)00446-X[Crossref]
• [26] X. Hong, W. Guo, H. Yuan, J. Li, Y. Liu, L. Ma, Y. Bai, T. Li, J. Magn. Mater. 269, 95 (2004) http://dx.doi.org/10.1016/S0304-8853(03)00566-3[Crossref]
• [27] I.P. Gladysheva, N.A. Moroz, A.I. Papisova, N.I. Larionova, Biochemistry 66, 474 (2001)
• [28] M. Fuentes, L.R. Segura, O. Abian, L. Betancor, A. Hidalgo, C. Mateo, R. Fernández-Lafuente, J.M. Guisán, Proteomics. 4, 2602 (2004) http://dx.doi.org/10.1002/pmic.200300766[Crossref]
• [29] S.M.A.G. Ulson de Souza, E.F.A.A. Ulson de Souza, J. Hazard. Mater. 147, 1073 (2007) http://dx.doi.org/10.1016/j.jhazmat.2007.06.003[Crossref]
• [30] G-Y. Kim, K-B. Lee, S-H. Cho, J. Shim, S-H. Moon, J. Hazard. Mater. B 126, 183 (2005) http://dx.doi.org/10.1016/j.jhazmat.2005.06.023[Crossref]
• [31] D.G. Pina, A.V. Shnyrova, F. Gavilanes, A. Rodríguez, F. Leal, M.G. Roig, I.Y. Sakharov, G.G. Zhada, E. Villar, V.L. Shnyrov, Eur. J. Biochem. 268, 120 (2001) http://dx.doi.org/10.1046/j.1432-1033.2001.01855.x[Crossref]
• [32] A.S.L. Carvalho, M.T. Neves-Petersen, S.B. Petersen, M.R. Aires-Barros, E. Pinho e Melo, Biochim. Biophys. Acta 1747, 99 (2004)
• [33] M. Tanaka, A. Morimoto, K. Ishimori, I. Morishima, Pure and Appl. Chem. 70, 911 (1998) http://dx.doi.org/10.1351/pac199870040911[Crossref]
• [34] S. Mumtaz, B.K. Bachhavat, Biochim. Biophys. Acta 1117(2), 174 (1992)
• [35] M.G. Brattain, M.E. Marks, T.G. Pretlow, Anal. Biochem. 72, 346 (1976) http://dx.doi.org/10.1016/0003-2697(76)90540-6[Crossref]
• [36] A. Guerra, A. Ferraz, Enzyme Microb. Technol. 28, 308 (2000) http://dx.doi.org/10.1016/S0141-0229(00)00350-1[Crossref]
• [37] D. Mislovičvá, J. Masárová, M. Bučko, P. Gemenier, Enzyme Microb. Technol. 39, 579 (2006) http://dx.doi.org/10.1016/j.enzmictec.2005.11.012[Crossref]
• [38] H-Y. Song, J-H. Yao, J-Z. Liu, S-J. Zhou, Y-H. Xiong, L-N. Ji, Enzyme Microb. Technol. 36, 605 (2005) http://dx.doi.org/10.1016/j.enzmictec.2004.12.018[Crossref]

Identifiers

DOI

10.2478/s11532-009-0041-z