You can use the filter on the left to narrow the results
Previous
Type
All Books Papers
Title
Author
Keywords
ISBN
DOI Access
CSIC digital access
Search
Details
PublicationMolecules
Year2016
Volume21
Pages751
International

Stabilization of CALB Immobilized on Octyl Agarose by Treatment with PEI

Authors:Roberto Fernandez-Lafuente
Groups of research:Optimización de biocatalizadores y bioprocesos enzimáticos

Sara Peirce 1,2, Veymar G. Tacias-Pascacio 1,3, Maria Elena Russo 4, Antonio Marzocchella 2, José J. Virgen-Ortíz 1,* and Roberto Fernandez-Lafuente 1,*

1   Departamento de Biocatálisis. Instituto de Catálisis-CSIC, Campus UAM-CSIC Madrid, Spain; sara.peirce@unina.it

2   Dipartimento di Ingegneria Chimica, dei Materiali e della Produzione Industriale. Universita' degli Studi di Napoli Federico II, Italy; marzocch@unina.it

3   Unidad de Investigación y Desarrollo en Alimentos. Instituto Tecnológico de Veracruz, Calzada Miguel A. de Quevedo 2779, 91897 Veracruz, Mexico; vey_pascacio@live.com

4   Istituto di Ricerche sulla Combustione– Consiglio Nazionale delle Ricerche, Napoli, Italy; m.russo@irc.cnr.it

Abstract: Lipase B from Candida antarctica (CALB) was immobilized on octyl agarose (OC) and physically modified with PEI in order to confer a strong ion exchanger to the enzyme and that way, enable the immobilization of other enzymes over it. The enzyme activity was fully maintained during the coating and the thermal stability was marginally improved. The enzyme release from the support by incubation in the non-ionic detergent Triton X-100 was more difficult after the PEI-coating suggesting that some intermolecular physical crosslinking had been achieved making more difficult this desorption.  Thermal stability was marginally improved, but the stability of the OCCALB-PEI was significantly better than that of OCCALB during inactivation in mixtures of aqueous buffer and organic cosolvents. SDS-PAGE analysis of the inactivated biocatalyst showed the OCCALB released some enzyme to the medium during inactivation, and this was partially prevented by coating with PEI. This effect was obtained without preventing the possibility of re-use of the support by incubation in 2% ionic detergents. That way, this modified CALB not only has a strong anion exchange nature, keeping the activity, but also improves its stability under diverse reaction conditions without losing the reversibility of the immobilization.

 

Keywords:Enzyme stabilization, reversible immobilization, interfacial adsorption, PEI modification, enzyme physical intermolecular crosslinking
logo de CSIC