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Reversible Immobilization of Lipases on Heterofunctional Octyl-Amino Agarose Beads Prevents Enzyme Desorption

Authors:Roberto Fernandez-Lafuente,
Groups of research:Optimization of biocatalysts and bioprocesses
Departamento de Biocatalisis, Instituto de Catálisis-CSIC; C/ Marie Curie 2, Campus UAM-CSIC, 28049 Madrid, Spain; (N.R.); (T.L.A.); (R.B.-C.); (L.F.-L.); (C.S.S.)
2   Escuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga 680002, , Colombia;
3   Departamento de Engenharia Química, Universidade Federal Do Ceará, Campus Do Pici,
CEP 60455-760, Fortaleza, Brazil
4   Escuela de Microbiología, Universidad Industrial de Santander, Bucaramanga,
680002, Colombia;
5   Departamento de Química, Facultad de Ciencias. Universidad del Tolima, Ibagué 546,  Colombia;

†  Current address: Laboratorio de Biotecnología, Instituto Colombiano del Petróleo-Ecopetrol, Piedecuesta, Bucaramanga 680012, Colombia
Two different heterofunctional octyl-amino supports have been prepared using ethylenediamine and hexylendiamine (OCEDA and OCHDA) and utilized to immobilize five lipases (lipases A (CALA) and B (CALB) from Candida antarctica, lipases from Thermomyces lanuginosus (TLL), from Rhizomucor miehei (RML) and from Candida rugosa (CRL) and the phospholipase Lecitase Ultra (LU). Using pH 5 and 50 mM sodium acetate, the immobilizations proceeded via interfacial activation on the octyl layer, after some ionic bridges were established. These supports did not release enzyme when incubated at Triton X-100 concentrations that released all enzyme molecules from the octyl support. The octyl support produced significant enzyme hyperactivation, except for CALB. However, the activities of the immobilized enzymes were usually slightly higher using the new supports than the octyl ones. Thermal and solvent stabilities of LU and TLL were significantly improved compared to the OC counterparts, while in the other enzymes the stability decreased in most cases (depending on the pH value). As a general rule, OCEDA had lower negative effects on the stability of the immobilized enzymes than OCHDA and while in solvent inactivation the enzyme molecules remained attached to the support using the new supports and were released using monofunctional octyl supports, in thermal inactivations this only occurred in certain cases. 

Keywords:heterofunctional supports; octyl supports; interfacial activation of lipases; ion exchange; enzyme hyperactivation; reversible immobilization
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