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PublicationJournal of Molecular Catalysis B: Enzymatic
Year2016
Volume128
Pages10-18
International

REVERSIBLE IMMOBILIZATION OF LIPASES ON OCTYL-GLUTAMIC AGAROSE BEADS: A MIXED ADSORPTION THAT REINFORCES ENZYME IMMOBILIZATION

Authors:José Cleiton Sousa dos Santos, Roberto Fernandez-Lafuente
Groups of research:Optimization of biocatalysts and bioprocesses
Nazzoly Ruedaa,b, Cleiton S. dos Santosa,c, Maria Daniela Rodrigueza,d, Tiago L. Albuquerquea,c, Oveimar Barbosae, Rodrigo Torresb,f, Claudia Ortizg,*, Roberto Fernandez-Lafuentea*
a Departamento de Biocatálisis. Instituto de Catálisis-CSIC, Campus UAM-CSIC Madrid. Spain.
b Escuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga, Colombia.
c Departamento de Engenharia Química, Universidade Federal Do Ceará, Campus Do Pici, CEP 60455-760, Fortaleza, CE, Brazil.
d Laboratorio de Biotecnología Molecular. Instituto de Biotecnología Misiones "María Ebe Reca". (FCEQyN – UnaM). Posadas, Argentina.
e Departamento de Química, Facultad de Ciencias. Universidad del Tolima, Ibagué, Colombia
f Current address: Laboratorio de Biotecnología, Instituto Colombiano del Petróleo-Ecopetrol, Piedecuesta, Bucaramanga, Colombia.
g Escuela de Microbiología, Universidad Industrial de Santander, Bucaramanga, Colombia


Abstract

A new octyl-glutamic(OCGLU)  heterofunctional agarose bead has been prepared. It has been compared to octyl-agarose (OC) in their performance to immobilize 5 different lipases, those from Candida antarctica (A (CALA) and B (CALB)), from Thermomyces lanuginosus (TLL), from Rhizomucor miehei (RML) and from Candida rugosa (CRL) and a phospholipase (Lecitase ultra, LU). The immobilization rate was very similar using both supports, and the increase of activity versus p-nitrophenyl butyrate were also very similar. The effects on enzyme stability of the immobilization on OCGLU compared to the conventional OC was quite diverse, in some cases reducing the enzyme stability while in other examples the enzyme stability improved more than hundredfold. Curiously, the highest stabilizations were found under pH conditions where the free enzyme could not be adsorbed on a support just bearing glutamic groups on its surface, suggesting that the mechanism of stabilization may be a quite complex one that should consider the hydrophilization of the support surface, the cationic and anionic groups of glutamic, the likely partition of organic solvents from the support surface, positive and negative enzyme-support interactions, etc. Even though the lipases adsorption was very strong, the support could be regenerated and reused by incubation in ionic detergents.
Keywords:Enzyme stabilization, heterofunctional supports, lipase interfacial activation, ion exchange, reversible immobilization, prevention of enzyme leakage.
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