Summary
Lipase fromC. cylindracea was covalently immobilised to a number of surface-treated ceramic supports (3–10 mg. (g dry wt support)−1). At room temperature, the immobilised lipase could convert R,S-citronellol and butyric acid to citronellyl butyrate at rates in the range 7–51 μmol. (mg lipase.min)−1. The lipase maintained 90–100% of its initial activity over a period of 150 days.
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References
Adams, J.M., Ash, L.A., Brown, A.J., James, R., Kell, D.B., Salter, G.J. & Walter, R.P. (1988),Int. Biotechnol. Lab. 6(3), 22–27.
Brockerhoff, H. & Jensen, R.G. (1974).Lipolytic enzymes, New York: Academic Press.
Cambou, B. & Klibanov, A.M. (1984)J. Am. Chem. Soc. 106, 2687–2692
Kawmoto, T., Sonomoto, K. & Tanaka, A. (1987)Biocatalysis 1, 137–145
Klibanov, A.M. & Cambou, B. (1987)Meth. Enzymol. 136, 117–137.
Nishio, T., Takahashi, K., Yoshimoto, Y., Kodera, Y., Saito, Y. & Inada, Y.M. (1987).Biotechnol. Lett. 9(3), 187–190.
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Walter, R.P., Kell, D.B., Morris, J.G. et al. Immobilisation ofCandida cylindracea lipase on a new range of ceramic supports. Biotechnol Tech 3, 345–348 (1989). https://doi.org/10.1007/BF01875634
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DOI: https://doi.org/10.1007/BF01875634