STABILITY OF A FUSARIUM-SOLANI PISI RECOMBINANT CUTINASE IN PHOSPHATIDYLCHOLINE REVERSED MICELLES

Authors
PINTOSOUSA AM CABRAL JMS AIRESBARROS MR
Citation
Am. Pintosousa et al., STABILITY OF A FUSARIUM-SOLANI PISI RECOMBINANT CUTINASE IN PHOSPHATIDYLCHOLINE REVERSED MICELLES, Biotechnology letters, 18(5), 1996, pp. 583-586
Citations number
6
Categorie Soggetti
Biothechnology & Applied Migrobiology
Journal title
Biotechnology letters → ACNP
ISSN journal
01415492
Volume
18
Issue
5
Year of publication
1996
Pages
583 - 586
Database
ISI
SICI code
0141-5492(1996)18:5<583:SOAFPR>2.0.ZU;2-D
Abstract
A Fusarium solani pisi recombinant cutinase solubilized in phosphatidy lcholine/isooctane reversed micellas was used to catalyse the esterifi cation reaction of butyric acid with 2-butanol at pH 10.7. The influen ce of temperature, Wo and substrates on lipase stability was evaluated . The enzyme displays a better stability, with a half-life over 125 da ys, at a temperature of 22 degrees C and for a low water content (W-O= 6.5). Butyric acid increased the cutinase deactivation (t(1/2)=0.56h), while 2-butanol led to a similar half-life (t(1/2)=14h) as without su bstrate.