Activated Carbon as Support for Lipase Immobilization

Authors

  • Mohd Basyaruddin Abdul Rahman Centre for Research in Enzyme and Microbial Technology, Faculty of Science and Environmental Studies, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia
  • Mahiran Basri Centre for Research in Enzyme and Microbial Technology, Faculty of Science and Environmental Studies, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia
  • Mohd Zobir Hussein Centre for Research in Enzyme and Microbial Technology, Faculty of Science and Environmental Studies, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia
  • Raja Nor Zaliha Raja Abdul Rahman Centre for Research in Enzyme and Microbial Technology, Faculty of Science and Environmental Studies, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia
  • Yau Kim Yan Centre for Research in Enzyme and Microbial Technology, Faculty of Science and Environmental Studies, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia
  • Abu Bakar Salleh Centre for Research in Enzyme and Microbial Technology, Faculty of Science and Environmental Studies, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia

DOI:

https://doi.org/10.18321/ectj298

Abstract

Lipase from Candida rugosa was immobilized onto four different types of activated carbon; KI/2030,
KI/3040, KI/5060 and KI/6070. The immobilized lipase was used in the esterification of oleic acid and 1-
butanol in hexane. The effects of difference pore sizes, surface area, reaction temperature, thermostability of the immobilized lipases, storage stability in organic solvent and leaching studies were investigated. Among the four samples, KI/6070 gave the highest activities and stability in all the parameters investigated. Immobilized lipases generally exhibit activities higher than the native lipase for the parameters studied, with optimum temperature of 40 °C. Immobilized lipases are more stable than native lipase in hexane at room temperature up to 12 days. Leaching study proved that the immobilization of lipase using physical adsorption is cheap and easy. This method was found to be suitable for the attachment of enzyme on the support.

References

(1). Gergova, K., J Chem Tech Biotechnol 56:77 (1993).

(2). Bandosz, T.J., Jagiello, J. and Contescu, C., Carbon 31(7):1193 (1993).

(3). Bosley, J., Biochem Soc Transactions 25:174 (1997).

(4). Taylor, R.F., Industrial applications of immobilized proteins. Protein Immobilization. Marcel Dekker, New York , 1991, 339.

(5). Bradford, M.M., Anal. Biochem. 72: 248 (1976).

(6). Ampon, K., J Chem Biotechnol Bioeng 55:185 (1992).

(7). Ruckenstein, E. and Wang, X., Biotechnol Bioeng 42:821 (1992).

(8). Basri, M., Ampon, K., Razak, C.N.A., Salleh, A.B., Yoong, W.S. and Yunus, W.M.Z., J. Chem Tech Biotechnol 66:169(1996).

(9). Fagain, C.O., Manipulating protein stability in Stabilizing Proteins Functions, Heidelberg, Berlin, Springer, New York, 1997, 67.

(10). Gorman, L.A. and Dordick, J.S., Bioeng 39:392 (1992).

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Published

2003-04-15

How to Cite

Abdul Rahman, M. B., Basri, M., Hussein, M. Z., Raja Abdul Rahman, R. N. Z., Yan, Y. K., & Salleh, A. B. (2003). Activated Carbon as Support for Lipase Immobilization. Eurasian Chemico-Technological Journal, 5(2), 115–119. https://doi.org/10.18321/ectj298

Issue

Vol. 5 No. 2 (2003)

Section

Articles

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