Science and Technology Production
Article
Authorship
JOSE, CARLA
;
Rita D. Bonetto
;
Luis A. Gambaro
;
María del Pilar Guauque
;
María Laura Foresti
;
María Luján Ferreira
;
Laura E Briand
Date
2011
Publishing House and Editing Place
ELSEVIER SCIENCE BV
Magazine
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,
vol. 71
(pp. 95-107)
ELSEVIER SCIENCE BV
Summary
Information provided by the agent in
SIGEVA
The effect of contacting neat ethanol and an ethanol: H2O mixture on Novozym®435 was investigated at room temperature and 45 °C, during various periods of time of interaction with the alcohol (from 40 min to 8 days) and at different biocatalyst: ethanol ratios. The alcohol dissolves the polymethylmethacrylate (PMMA) that constitutes the support of the Candida antarctica B lipase (CALB) regardless of the conditions investigated and diffuses into the biocatalyst´s beads remaining st...
The effect of contacting neat ethanol and an ethanol: H2O mixture on Novozym®435 was investigated at room temperature and 45 °C, during various periods of time of interaction with the alcohol (from 40 min to 8 days) and at different biocatalyst: ethanol ratios. The alcohol dissolves the polymethylmethacrylate (PMMA) that constitutes the support of the Candida antarctica B lipase (CALB) regardless of the conditions investigated and diffuses into the biocatalyst´s beads remaining strongly adsorbed (the desorption of the alcohol is evidenced only upon heating at 150 °C). The diffusion of the alcohol alters the inner texture of the beads generating channels and increasing the roughness of the polymeric material. Additionally, the ethanol modifies the secondary structure of the enzyme by decreasing the α−helix contributions and increasing the β−sheet structure.
Show more
Show less
Key Words
CALBETHANOLNOVOZYM 435STABILITYBIOCATALYST