Stability of a Fusarium solani pisi recombinant cutinase in phosphatidylcholine reversed micelles
1996
Pinto-Sousa, A.M. | Cabral, J.M.S. | Aires-Barros, M.R.
A Fusarium solani pisi recombinant cutinase solubilized in phosphatidylcholine/isooctane reverse 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 better stability, with a half-life over 125 days, at a temperature of 22 degrees 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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