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Stability of a Fusarium solani pisi recombinant cutinase in phosphatidylcholine reversed micelles

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Summary

A Fusarium solani pisi recombinant cutinase solubilized in phosphatidylcholine/isooctane reversed micelles was used to catalyse the esterification reaction of butyric acid with 2-butanol at pH 10.7. The influence of temperature, Wo and substrates on lipase stability was evaluated. The enzyme displays a better stability, with a half-life over 125 days, at a temperature of 22°C and for a low water content (WO= 6.5). Butyric acid increased the cutinase deactivation (t1/2=0.56h), while 2-butanol led to a similar half-life (t1/2=14h) as without substrate.

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Pinto-Sousa, A.M., Cabral, J.M.S. & Aires-Barros, M.R. Stability of a Fusarium solani pisi recombinant cutinase in phosphatidylcholine reversed micelles. Biotechnol Lett 18, 583–586 (1996). https://doi.org/10.1007/BF00140207

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  • DOI: https://doi.org/10.1007/BF00140207

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