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Characterization and Utilization of Candida rugosa Lipase Immobilized on Controlled Pore Silica

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Twentieth Symposium on Biotechnology for Fuels and Chemicals

Abstract

Candida rugosa lipase was immobilized by covalent binding on controlled pore silica (CPS) using glutaraldehyde as cross-linking agent under aqueous and nonaqueous conditions. The immobilized C. rugosa was more active when the coupling procedure was performed in the presence of a nonpolar solvent, hexane. Similar optima pH (7.5–8.0) was found for both free and immobilized lipase. The optimum temperature for the immobilized lipase was about 10°C higher than that for the free lipase. The thermal stability of the CPS lipase was also greater than the original lipase preparation. Studies on the operational stability of CPS lipase revealed good potential for recycling under aqueous (olive-oil hydrolysis) and nonaqueous (butyl butyrate synthesis) conditions.

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Correspondence to Heizir F. De Castro .

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Soares, C.M.F., De Castro, H.F., De Moraes, F.F., Zanin, G.M. (1999). Characterization and Utilization of Candida rugosa Lipase Immobilized on Controlled Pore Silica. In: Davison, B.H., Finkelstein, M. (eds) Twentieth Symposium on Biotechnology for Fuels and Chemicals. Applied Biochemistry and Biotechnology. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-4612-1604-9_68

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  • DOI: https://doi.org/10.1007/978-1-4612-1604-9_68

  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-4612-7214-4

  • Online ISBN: 978-1-4612-1604-9

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