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Immobilization of Candida antarctica lipase B on the surface of modified sol–gel matrix

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Abstract

The use of modified sol–gel matrix to immobilize the enzyme Candida antartica lipase B (CALB) was investigated. Free hydroxyl groups on the matrix surface were exploited to covalently immobilize the enzyme. Based from the results, incorporating hydrophobic sol–gel precursor (ethyltrimethoxysilane) enhanced enzyme activity. An enzyme activity of 192.02 U/g beads with 80.88 % attachment was obtained. At alkaline pH, immobilization yield of enzyme increased. The attachment of enzyme on the surface of the matrix was confirmed by scanning electron microscope images. Covalently immobilized CALB on sol–gel supports has higher thermal stability with 2.7 times higher half-life compared to soluble enzymes at 60 °C. This enzyme immobilization system retains the enzyme residual activity even for repetitive use. Hence, the immobilization approach developed recommends its further application.

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References

  1. Yu HW, Chen H, Wang X, Yang YY, Ching CB (2006) Cross-linked enzyme aggregates (CLEAs) with controlled particles: application to Candida rugosa lipase. J Mol Catal B Enzym 43:124–127

    Article  Google Scholar 

  2. Cao L (2003) Carrier-bound immobilized enzymes: principles, applications and design, Wiley-VCH Verlag, Weinheim 2005. 32: 801–811

  3. Pirozzi D, Fanelli E, Aronne A, Pernice P, Mingione A (2009) Lipase entrapment in a zirconia matrix: sol–gel synthesis and catalytic properties. J Mol Catal B Enzym 59:116–120

    Article  Google Scholar 

  4. Reetz MT, Jaeger KE (2003) Overexpression, immobilization and biotechnological application of Psedomonas lipases. Chem Phys Lipids 93:3–14

    Article  Google Scholar 

  5. Pierre AC (2004) The sol–gel encapsulation of biocatalysts. Biocat Biotrans 22(3):145–170

    Article  Google Scholar 

  6. Wu AC, Wang PY, Chen KJ, Tsai SW (2012) Lipase-catalyzed regioselective hydrolysis of 3(5)-methylpyrazole-N-carboxylates in water-saturated organic solvents. J Mol Catal B Enzym 74:41–47

    Article  Google Scholar 

  7. Sutili FK, Ruela HS, Leite SGF, de Miranda LS, Leal ICR, de Souza ROMA (2013) Lipase-catalyzed esterification of steric hindered fructose derivative by continuous flow and batch conditions. J Mol Catal B Enzym 85–86:37–42

    Article  Google Scholar 

  8. Narwal SK, Gupta R (2013) Biodiesel production by transesterification using immobilized lipase. Biotechnol Lett 35:479–490

    Article  Google Scholar 

  9. Anderson EM, Larsson KM, Kirk O (1998) One biocatalyst—many applications: the use of Candida antarctica B-lipase in organic synthesis. Biocatal Biotransform 16:181–204

    Google Scholar 

  10. Laszlo JA, Evans KO (2007) Influence of self-assembled monolayer surface chemistry on Candida antarctica lipase B adsorption and specific activity. J Mol Catal B Enzym 48:84–89

    Article  Google Scholar 

  11. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254

    Article  Google Scholar 

  12. Reetz MT, Zonta A, Simpelkamp J (1995) Efficient heterogeneous biocatalysts by entrapment of lipases in hydrophobic sol–gel materials. Angew Chem Int Ed Engl 34:301–303

    Article  Google Scholar 

  13. Reetz MT, Zonta A, Simpelkamp J (1996) Efficient immoblization of lipases by entrapment in hydrophobic sol-gel materials. Biotechnol Bioeng 49:527–534

    Article  Google Scholar 

  14. Lee KW, Min K, Park K, Yoo YJ (2010) Development of an amphiphilic matrix for immobilization of Candida antartica lipase B for biodiesel production. Biotechnol Bioproc Eng 15:603–607

    Article  Google Scholar 

  15. Rodrigues DS, Mendes AA, Adriano WS, Gonçalves LRB, Giordano RLC (2008) Multipoint covalent immobilization of microbial lipase on chitosan and agarose activated by different methods. J Mol Catal B Enzym 51:100–109

    Article  Google Scholar 

  16. Silva JA, Macedo GP, Rodrigues DS, Giordano RLC, Goncalves LRB (2012) Immobilization of Candida antarctica lipase B by covalent attachment on chitosan-based hydrogels using different support activation strategies. Biochem Eng J 60:16–24

    Article  Google Scholar 

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Authors and Affiliations

  1. School of Chemical and Biological Engineering, Seoul National University, Seoul, 151-742, Korea

    Camila Flor J. Yagonia & Young Je Yoo

  2. Department of Biological and Chemical Engineering, Hongik University, Sejong, 399-701, Korea

    Kyungmoon Park

  3. Bio-Max Institute, Seoul National University, Seoul, 151-742, Korea

    Young Je Yoo

Authors
  1. Camila Flor J. Yagonia
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  2. Kyungmoon Park
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  3. Young Je Yoo
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Correspondence to Young Je Yoo.

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Yagonia, C.F.J., Park, K. & Yoo, Y.J. Immobilization of Candida antarctica lipase B on the surface of modified sol–gel matrix. J Sol-Gel Sci Technol 69, 564–570 (2014). https://doi.org/10.1007/s10971-013-3257-5

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  • DOI: https://doi.org/10.1007/s10971-013-3257-5

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