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Kinetic characterization ofpenicillium citrinum lipase in AOT/lsooctane-reversed micelles

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Abstract

A lipase from a wild strain ofPenicillium citrinum was encapsulated in AOT/isooctane-reversed micelles, and the kinetic parameters were studied relative to triolein hydrolysis. Lipolytic activity was strongly dependent on the water amount in the system (Wo) and presented a bell-shaped curve for this parameter, with a maximum in the range of Wo 10–15. Optimum conditions for enzyme activity were pH 8.0 and 45‡C. The influence of substrate concentration was also studied. The enzyme showed a Michaelis-Menten behavior and the apparent kinetics constants were calculated as beingV max.app. - 120 U/mg and Kmapp = 49.2 mM.

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Authors and Affiliations

  1. Departamento de Quimica, Universidade Federal do Paraná Curitiba, Parana, Brasil

    N. Krieger

  2. Laboratório de Engenharia Bioquímica, Centro de Engenharia Biológica de Química, Instituto Superior Técnico, 1000, Lisboa, Portugal

    N. Krieger, M. A. Taipa, M. R. Aires-Barros & J. M. S. Cabral

  3. Departamento de Bioquímica, Universidade Federal de Pernambuco/ Laboratório de Imunopatologia Keizo Azami-LIKA, Recife, Pernambuco, Brasil

    E. H. M. Melo & J. L. Lima-Filho

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  1. N. Krieger
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  2. M. A. Taipa
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  3. E. H. M. Melo
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  4. J. L. Lima-Filho
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  5. M. R. Aires-Barros
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  6. J. M. S. Cabral
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Krieger, N., Taipa, M.A., Melo, E.H.M. et al. Kinetic characterization ofpenicillium citrinum lipase in AOT/lsooctane-reversed micelles. Appl Biochem Biotechnol 67, 87–95 (1997). https://doi.org/10.1007/BF02787844

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  • DOI: https://doi.org/10.1007/BF02787844

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