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Effect of ionic liquids alkyl chain length on horseradish peroxidase thermal inactivation kinetics and activity recovery after inactivation

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Abstract

The effects of different alkyl chain lengths of ionic liquids 1-ethyl-, 1-butyl- and 1-hexyl-3-methylimidazolium chloride, on the catalytic activity, thermal stability and deactivation kinetics of horseradish peroxidase were studied in the temperature range of 45–85 °C. The presence of 1-ethyl- and 1-butyl-ionic liquids up to 25 % (w/v) did not affect significantly the enzyme activity at 25 °C, whereas the addition of 1-hexyl-solvent resulted in lower activity of enzyme. Typical biphasic deactivation profiles were obtained and adequately fitted by a bi-exponential equation. When increasing ionic liquids concentration up to 25 % (w/v), the second phase of deactivation became more prominent, till leading to apparent first-order kinetics. Occurrence of activity regain, following thermal deactivation was found, reaching up 60–80 % of the initial activity, especially in 1-hexyl-3-methylimidazolium chloride. Activity regain was particularly noticeable in the first phase of deactivation. Temperature sensitivity of the Soret band maxima indicated that the enzyme prepared in buffer or 1-hexyl-3-methylimidazolium chloride had similar conformational changes in the haem region, but no correlations were found with activity decrease.

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References

  • Adams J (1978) The inactivation and regeneration of peroxidase in relation to the high temperature–short time processing of vegetables. Int J Food Sci Technol 13(4):281–297

    Article  CAS  Google Scholar 

  • Alpeeva IS, Niculescu-Nistor M, Leon JC, Csöregi E, Sakharov IY (2005) Palm tree peroxidase-based biosensor with unique characteristics for hydrogen peroxide monitoring. Biosens Bioelectron 21(5):742–748

    Article  CAS  Google Scholar 

  • Carneiro AP, Rodriguez O, Mota FL, Tavares APM, Macedo EA (2009) Kinetic and stability study of the peroxidase inhibition in ionic liquids. Ind Eng Chem Res 48(24):10810–10815

    Article  CAS  Google Scholar 

  • Gholami-Borujeni F, Mahvi AH, Naseri S, Faramarzi MA, Nabizadeh R, Alimohammadi M (2011) Application of immobilized horseradish peroxidase for removal and detoxification of azo dye from aqueous solution. Res J Chem Environ 15(2):217–222

    CAS  Google Scholar 

  • Haifeng L, Yuwen L, Xiaomin C, Zhiyong W, Cunxin W (2008) Effects of sodium phosphate buffer on horseradish peroxidase thermal stability. J Therm Anal Calorim 93(2):569–574

    Article  CAS  Google Scholar 

  • Hei DJ, Clark DS (1993) Estimation of melting curves from enzymatic-activity temperature profiles. Biotechnol Bioeng 42(10):1245–1251

    Article  CAS  Google Scholar 

  • Hernandez-Fernandez FJ, Rios A, Lozano-Blanco LJ, Godinez C (2010) Biocatalytic ester synthesis in ionic liquid media. J Chem Technol Biotechnol 85(11):1423–1435

    CAS  Google Scholar 

  • Hinckley G, Mozhaev VV, Budde C, Khmelnitsky YL (2002) Oxidative enzymes possess catalytic activity in systems with ionic liquids. Biotechnol Lett 24(24):2083–2087

    Article  CAS  Google Scholar 

  • Kaar JL, Jesionowski AM, Berberich JA, Moulton R, Russell AJ (2003) Impact of ionic liquid physical properties on lipase activity and stability. J Am Chem Soc 125(14):4125–4131

    Article  CAS  Google Scholar 

  • Kragl U, Eckstein M, Kaftzik N (2002) Enzyme catalysis in ionic liquids. Curr Opin Biotechnol 13(6):565–571

    Article  CAS  Google Scholar 

  • Krieg R, Halbhuber KJ (2003) Recent advances in catalytic peroxidase histochemistry. Cell Mol Biol 49(4):547–563

    CAS  Google Scholar 

  • Laszlo JA, Compton DL (2002) Comparison of peroxidase activities of hemin, cytochrome c and microperoxidase-11 in molecular solvents and imidazolium-based ionic liquids. J Mol Catal B Enzym 18(1–3):109–120

    Article  CAS  Google Scholar 

  • Li ZL, Liu W, Chen XF, Shang WL (2009) Research on the application of horseradish peroxidase and hydrogen peroxide to the oil removal of oily water. Water Sci Technol 59(9):1751–1758

    Article  CAS  Google Scholar 

  • Machado MF, Saraiva J (2002) Inactivation and reactivation kinetics of horseradish peroxidase in phosphate buffer and buffer–dimethylformamide solutions. J Mol Catal B Enzym 19:451–457

    Article  Google Scholar 

  • Machado MF, Saraiva JM (2005) Thermal stability and activity regain of horseradish peroxidase in aqueous mixtures of imidazolium-based ionic liquids. Biotechnol Lett 27(16):1233–1239

    Article  CAS  Google Scholar 

  • Moniruzzaman M, Nakashima K, Kamiya N, Goto M (2010) Recent advances of enzymatic reactions in ionic liquids. Biochem Eng J 48(3):295–314

    Article  CAS  Google Scholar 

  • Muldoon MJ, Gordon CM, Dunkin IR (2001) Investigations of solvent-solute interactions in room temperature ionic liquids using solvatochromic dyes. J Chem Soc Perkin Trans 2(4):433–435

    Article  Google Scholar 

  • Naushad M, Alothman ZA, Khan AB, Ali M (2012) Effect of ionic liquid on activity, stability, and structure of enzymes: a review. Int J Biol Macromol 51(4):555–560

    Article  CAS  Google Scholar 

  • Rasmussen CB, Henriksen A, Abelskov AK, Jensen RB, Rasmussen SK, Hejgaard J, Welinder KG (1997) Purification, characterization and stability of barley grain peroxidase BP 1, a new type of plant peroxidase. Physiol Plant 100(1):102–110

    Article  CAS  Google Scholar 

  • Rodrigo C, Rodrigo M, Alvarruiz A, Frigola A (1996) Thermal inactivation at high temperatures and regeneration of green asparagus peroxidase. J Food Prot 59(10):1065–1071

    CAS  Google Scholar 

  • Rodriguez O, Cristovao RO, Tavares APM, Macedo EA (2011) Study of the alkyl chain length on laccase stability and enzymatic kinetic with imidazolium ionic liquids. Appl Biochem Biotechnol 164(4):524–533

    Article  CAS  Google Scholar 

  • Ryu K, Dordick JS (1992) How do organic-solvents affect peroxidase structure and function? Biochemistry 31(9):2588–2598

    Article  CAS  Google Scholar 

  • Saraiva J, Oliveira JC, Lemos A, Hendrickx M (1996) Analysis of the kinetic patterns of horseradish peroxidase thermal inactivation in sodium phosphate buffer solutions of different ionic strength. Int J Food Sci Technol 31(3):223–231

    Article  CAS  Google Scholar 

  • van Rantwijk F, Sheldon RA (2007) Biocatalysis in ionic liquids. Chem Rev 107(6):2757–2785

    Article  Google Scholar 

  • van Rantwijk F, Lau RM, Sheldon RA (2003) Biocatalytic transformations in ionic liquids. Trends Biotechnol 21(3):131–138

    Article  Google Scholar 

  • Ventura SPM, Santos LDF, Saraiva JA, Coutinho JAP (2012) Concentration effect of hydrophilic ionic liquids on the enzymatic activity of Candida Antarctica lipase B. World J Microbiol Biotechnol 28(6):2303–2310

    Article  CAS  Google Scholar 

  • Vojinović V, Carvalho R, Lemos F, Cabral J, Fonseca L, Ferreira B (2007) Kinetics of soluble and immobilized horseradish peroxidase-mediated oxidation of phenolic compounds. Biochem Eng J 35(2):126–135

    Article  Google Scholar 

  • Zhao H (2010) Methods for stabilizing and activating enzymes in ionic liquids—a review. J Chem Technol Biotechnol 85(7):891–907

    Article  CAS  Google Scholar 

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Acknowledgments

Thanks are due to Fundação para a Ciência e a Tecnologia (FCT, Portugal), European Union, Quadro de Referência Estratégica Nacional (QREN), Fundo Europeu de Desenvolvimento Regional (FEDER) and COMPETE for funding the QOPNA research unit (Project PEst-C/QUI/UI0062/2013).

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Correspondence to Jorge A. Saraiva.

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Machado, M.F., Queirós, R.P., Santos, M.D. et al. Effect of ionic liquids alkyl chain length on horseradish peroxidase thermal inactivation kinetics and activity recovery after inactivation. World J Microbiol Biotechnol 30, 487–494 (2014). https://doi.org/10.1007/s11274-013-1466-2

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  • DOI: https://doi.org/10.1007/s11274-013-1466-2

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