title: Stabilization of Candida antarctica Lipase B (CALB) Immobilized on Octyl Agarose by Treatment with Polyethyleneimine (PEI).
abstract: Lipase B from Candida antarctica (CALB) was immobilized on octyl agarose (OC) and physically modified with polyethyleneimine (PEI) in order to confer a strong ion exchange character to the enzyme and thus enable the immobilization of other enzymes on its surface. 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 occurred, making this desorption more difficult. 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 reuse of the support by incubation in 2% ionic detergents. That way, this modified CALB not only has a strong anion exchange nature, while maintaining the activity, but it also shows improved stability under diverse reaction conditions without affecting the reversibility of the immobilization.
authors.affiliation: Departamento de Biocat&#225;lisis, Instituto de Cat&#225;lisis-CSIC, C/Marie Curie 2, Campus UAM-CSIC Cantoblanco, 28049 Madrid, Spain. sara.peirce@unina.it.|Dipartimento di Ingegneria Chimica, dei Materiali e della Produzione Industriale, Universita' degli Studi di Napoli Federico II, 80125 Napoli, Italy. sara.peirce@unina.it.
authors.forename: Sara
authors.initials: S
authors.lastname: Peirce
authors.affiliation: Departamento de Biocat&#225;lisis, Instituto de Cat&#225;lisis-CSIC, C/Marie Curie 2, Campus UAM-CSIC Cantoblanco, 28049 Madrid, Spain. vey_pascacio@live.com.|Unidad de Investigaci&#243;n y Desarrollo en Alimentos, Instituto Tecnol&#243;gico de Veracruz, Calzada Miguel A. de Quevedo 2779, 91897 Veracruz, Mexico. vey_pascacio@live.com.
authors.forename: Veymar G
authors.initials: VG
authors.lastname: Tacias-Pascacio
authors.affiliation: Istituto di Ricerche sulla Combustione-Consiglio Nazionale delle Ricerche, 80125 Napoli, Italy. m.russo@irc.cnr.it.
authors.forename: Maria Elena
authors.initials: ME
authors.lastname: Russo
authors.affiliation: Dipartimento di Ingegneria Chimica, dei Materiali e della Produzione Industriale, Universita' degli Studi di Napoli Federico II, 80125 Napoli, Italy. marzocch@unina.it.
authors.forename: Antonio
authors.initials: A
authors.lastname: Marzocchella
authors.affiliation: Departamento de Biocat&#225;lisis, Instituto de Cat&#225;lisis-CSIC, C/Marie Curie 2, Campus UAM-CSIC Cantoblanco, 28049 Madrid, Spain. juanvirgen@hotmail.com.
authors.forename: José J
authors.initials: JJ
authors.lastname: Virgen-Ortíz
authors.affiliation: Departamento de Biocat&#225;lisis, Instituto de Cat&#225;lisis-CSIC, C/Marie Curie 2, Campus UAM-CSIC Cantoblanco, 28049 Madrid, Spain. rfl@icp.csic.es.
authors.forename: Roberto
authors.initials: R
authors.lastname: Fernandez-Lafuente
mesh_terms: D000327:Adsorption; D002175:Candida / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry*; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D008049:Lipase / Q000737:chemistry* / Q000378:metabolism; D017830:Octoxynol / Q000737:chemistry; D011094:Polyethyleneimine / Q000737:chemistry*; D012685:Sepharose / Q000737:chemistry
chemical_list: D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D017830:Octoxynol; D011094:Polyethyleneimine; D012685:Sepharose; D008049:Lipase; C431349:lipase B, Candida antarctica
keywords: PEI modification; enzyme physical intermolecular crosslinking; enzyme stabilization; interfacial adsorption; reversible immobilization