Stability of aFusarium solani pisirecombinant cutinase in phosphatidylcholine reversed micelles

✍ Scribed by A. M. Pinto-Sousa; J. M. S. Cabral; M. R. Aires-Barros

• Book ID: 104638491
• Publisher: Springer Netherlands
• Year: 1996
• Tongue: English
• Weight: 233 KB
• Volume: 18
• Category: Article
• ISSN: 0141-5492
• DOI: 10.1007/bf00140207

✦ Synopsis

A Fuwriurn solani pisi recombinant cutinase solubilizd in phosphatidyIcholine/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 temperahUe of 22'C and for a low water content (W,= 6.5). Butyric acid increased the cutinase deactivation (t1/2=0.56h), while 2-butanol led to a similar halflife (t1/2=14h) as without substrate.