Applied Biochemistry and Biotechnology

, Volume 164, Issue 5, pp 561–572 | Cite as

Comparison of the Properties of Lipase Immobilized onto Mesoporous Resins by Different Methods

Article

Abstract

Genipin, a natural cross-linking agent, was used for the immobilization of lipase from Candida sp. 99-125 by cross-linking to two kinds of mesoporous resins. Under optimum conditions, the activity recovery of immobilized lipase on resin NKA-9 could reach up to 96.99% when the genipin concentration was 0.5%, and it could reach up to 86.18% for S-8 with a genipin concentration of 0.25%. Compared with using glutaraldehyde as a cross-linking agent, the immobilized lipase using genipin showed better pH and thermal stability, storage stability, and reusability. The residual activity of immobilized lipase using genipin as cross-linker remained more than 60% of its initial activity after six hydrolytic cycles, whereas only about 35% activity remained by using glutaraldehyde as cross-linker.

Keywords

Immobilized lipase Cross-linking Genipin Glutaraldehyde Stability 

Notes

Acknowledgments

This work was supported by the Natural Science Foundation of Hebei Province (B2010000035, B2008000028) and the Natural Science Foundation of Tianjin (08JCYBJC02400).

Supplementary material

12010_2010_9157_MOESM1_ESM.doc (797 kb)
ESM 1 (DOC 797 kb)

References

  1. 1.
    Li, Y., Gao, F., Wei, W., Qu, J. B., Ma, G. H., & Zhou, W. Q. (2010). Journal of Molecular Catalysis. B, Enzymatic, 66(1–2), 182–189.CrossRefGoogle Scholar
  2. 2.
    Hung, T. C., Giridhar, R., Chiou, S. H., & Wu, W. T. (2003). Journal of Molecular Catalysis. B, Enzymatic, 26(1–2), 69–78.CrossRefGoogle Scholar
  3. 3.
    Vaidya, B. K., Ingavle, G. C., Ponrathnam, S., Kulkarni, B. D., & Nene, S. N. (2008). Bioresource Technology, 99(9), 3623–3629.CrossRefGoogle Scholar
  4. 4.
    Mateo, C., Palomo, J. M., Fernandez-Lorente, G., Guisan, J. M., & Fernandez-Lafuente, R. (2007). Enzyme and Microbial Technology, 40(6), 1451–1463.CrossRefGoogle Scholar
  5. 5.
    Lee, C. H., Lin, T. S., & Mou, C. Y. (2009). Nano Today, 4(2), 165–179.CrossRefGoogle Scholar
  6. 6.
    Chen, B., Miller, E. M., Miller, L., Maikner, J. J., & Gross, R. A. (2007). Langmuir, 23(3), 1381–1387.CrossRefGoogle Scholar
  7. 7.
    Sun, J. N., Jiang, Y. J., Zhou, L. Y., & Gao, J. (2010). New Biotechnology, 27(1), 53–58.CrossRefGoogle Scholar
  8. 8.
    Serra, E., Mayoral, A., Sakamoto, Y., Blanco, R. M., & Díaz, I. (2008). Microporous and Mesoporous Materials, 114(1–3), 201–213.CrossRefGoogle Scholar
  9. 9.
    Shamel, M. M., Azaha, R. B., & Al-Zuhair, S. (2005). Artificial Cells. Blood Substitutes and Biotechnology, 33(4), 423–433.CrossRefGoogle Scholar
  10. 10.
    Cunha, A. G., Fernández-Lorente, G., Bevilaqua, J. V., Destain, J., Paiva, L. M. C., Freire, D. M. G., et al. (2008). Applied Biochemistry and Biotechnology, 146(1), 49–56.CrossRefGoogle Scholar
  11. 11.
    Yang, J., Ma, X., Zhang, Z., Chen, B., Li, S., & Wang, G. (2010). Biotechnology Advances, 28(5), 644–650.CrossRefGoogle Scholar
  12. 12.
    Alloue, W. A. M., Destain, J., El Medjoub, T., Ghalfi, H., Kabran, P., & Thonart, P. (2008). Applied Biochemistry and Biotechnology, 150(1), 51–63.CrossRefGoogle Scholar
  13. 13.
    Fernández-Lorente, G., Palomo, J., Mateo, C., Munilla, R., Ortiz, C., Cabrera, Z., et al. (2006). Biomacromolecules, 7(9), 2610–2615.CrossRefGoogle Scholar
  14. 14.
    Migneault, I., Dartiguenave, C., Bertrand, M. J., & Waldron, K. C. (2004). Biotechniques, 37(5), 790–806.Google Scholar
  15. 15.
    Alonso, N., Lopez-Gallego, F., Betancor, L., Hidalgo, A., Mateo, C., Guisan, J. M., et al. (2005). Journal of Molecular Catalysis. B, Enzymatic, 35(1–3), 57–61.CrossRefGoogle Scholar
  16. 16.
    Pauliukaite, R., Ghica, M. E., Fatibello-Filho, O., & Brett, C. M. A. (2009). Analytical Chemistry, 81(13), 5364–5372.CrossRefGoogle Scholar
  17. 17.
    Moehlenbrock, M. J., Toby, T. K., Waheed, A., & Minteer, S. D. (2010). Journal of the American Chemical Society, 132(18), 6288–6289.CrossRefGoogle Scholar
  18. 18.
    Jones, P. O., & Vasudevan, P. T. (2010). Biotechnology Letters, 32(1), 103–106.CrossRefGoogle Scholar
  19. 19.
    Muzzarelli, R. A. A. (2009). Carbohydrate Polymers, 77(1), 1–9.CrossRefGoogle Scholar
  20. 20.
    Mi, F. L., Shyu, S. S., & Peng, C. K. (2005). Journal of Polymer Science. Part A: Polymer Chemistry, 43(10), 1985–2000.CrossRefGoogle Scholar
  21. 21.
    Yao, C. H., Liu, B. S., Hsu, S. H., & Chen, Y. S. (2005). Biomaterials, 26(16), 3065–3074.CrossRefGoogle Scholar
  22. 22.
    Silva, S. S., Motta, A., Rodrigues, M. T., Pinheiro, A. F. M., Gomes, M. E., Mano, J. F., et al. (2008). Biomacromolecules, 9(10), 2764–2774.CrossRefGoogle Scholar
  23. 23.
    Chen, K. Y., Liao, W. J., Kuo, S. M., Tsai, F. J., Chen, Y. S., Huang, C. Y., et al. (2009). Biomacromolecules, 10(6), 1642–1649.CrossRefGoogle Scholar
  24. 24.
    Sung, H. W., Liang, I. L., Chen, C. N., Huang, R. N., & Liang, H. F. (2001). Journal of Biomedical Materials Research. Part A, 55(4), 538–546.CrossRefGoogle Scholar
  25. 25.
    Song, F., Zhang, L. M., Yang, C., & Yan, L. (2009). International Journal of Pharmaceutics, 373(1–2), 41–47.CrossRefGoogle Scholar
  26. 26.
    Taylor, M. M., Bumanlag, L. P., Marmer, W. N., & Brown, E. M. (2009). Journal of the American Leather Chemists Association, 104(3), 79–91.Google Scholar
  27. 27.
    Song, F., & Zhang, L. M. (2009). Industrial and Engineering Chemistry Research, 48(15), 7077–7083.CrossRefGoogle Scholar
  28. 28.
    Koo, H. J., Song, Y. S., Kim, H. J., Lee, Y. H., Hong, S. M., Kim, S. J., et al. (2004). European Journal of Pharmacology, 495(2–3), 201–208.CrossRefGoogle Scholar
  29. 29.
    Fujikawa, S., Nakamura, S., & Koga, K. (1988). Agricultural and Biological Chemistry, 52(3), 869–870.Google Scholar
  30. 30.
    Fujikawa, S., Yokota, T., & Koga, K. (1988). Applied Microbiology and Biotechnology, 28(4), 440–441.CrossRefGoogle Scholar
  31. 31.
    Fujikawa, S., Koga, K., & Yokota, T. (1991). U.S. Patent 4983524.Google Scholar
  32. 32.
    Chiou, S. H., Hung, T. C., Giridhar, R., & Wu, W. T. (2007). Preparative Biochemistry & Biotechnology, 37(3), 265–275.CrossRefGoogle Scholar
  33. 33.
    Bradford, M. M. (1976). Analytical Biochemistry, 72(1–2), 248–254.CrossRefGoogle Scholar
  34. 34.
    Abrami, M., Lei, I., Korica, T., Vitale, L., Saenger, W., & Pigac, J. (1999). Enzyme and Microbial Technology, 25(6), 522–529.CrossRefGoogle Scholar
  35. 35.
    Li, S. F., Chen, J. P., & Wu, W. T. (2007). Journal of Molecular Catalysis. B, Enzymatic, 47(3–4), 117–124.CrossRefGoogle Scholar
  36. 36.
    Bigi, A., Cojazzi, G., Panzavolta, S., Roveri, N., & Rubini, K. (2002). Biomaterials, 23(24), 4827–4832.CrossRefGoogle Scholar
  37. 37.
    Sisson, K., Zhang, C., Farach-Carson, M. C., Chase, D. B., & Rabolt, J. F. (2009). Biomacromolecules, 10(7), 1675–1680.CrossRefGoogle Scholar
  38. 38.
    Trevan, M. D. (1980). Immobilized enzymes: an introduction and applications in biotechnology. New York: Wiley.Google Scholar
  39. 39.
    Altun, G. D., & Cetinus, S. A. (2007). Food Chemistry, 100(3), 964–971.CrossRefGoogle Scholar
  40. 40.
    De Lathouder, K. M., Marques Fló, T., Kapteijn, F., & Moulijn, J. A. (2005). Catalysis Today, 105(3-4), 443–447.CrossRefGoogle Scholar
  41. 41.
    Manyar, H. G., Gianotti, E., Sakamoto, Y., Terasaki, O., Coluccia, S., & Tumbiolo, S. (2008). Journal of Physical Chemistry C, 112(46), 18110–18116.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  • Wenqin Wang
    • 1
  • Yanjun Jiang
    • 1
  • Liya Zhou
    • 1
  • Jing Gao
    • 1
  1. 1.Department of Bioengineering, School of Chemical EngineeringHebei University of TechnologyTianjinChina

Personalised recommendations