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RevistaRSC Advances
Año2015
Volumen5
Páginas83868-83875
Internacional

STABILIZING EFFECTS OF CATIONS ON LIPASES DEPEND ON THE IMMOBILIZATION PROTOCOL

Autores:José Cleiton Sousa dos Santos, Roberto Fernandez-Lafuente
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos
Laura Fernandez-Lopeza,+, Rocio Bartolome-Cabreroa,+, Maria Daniela Rodrigueza,b, Cleiton S. Dos Santosa,c,  Nazzoly Ruedaa,d;* and Roberto Fernandez-Lafuentea*
 
a Departamento de Biocatálisis. Instituto de Catálisis-CSIC, Campus UAM-CSIC Madrid. Spain.
b  Laboratorio de Biotecnología Molecular. Instituto de Biotecnología Misiones "María Ebe Reca". (FCEQyN – UnaM). Posadas, Argentina.
c Departamento de Engenharia Química, Universidade Federal Do Ceará, Campus Do Pici, CEP 60455-760, Fortaleza, CE, Brazil.
d Escuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga, Colombia.

Abstract
The effect of an additive on enzyme stability use to be considered an intrinsic feature of the lipase. However, in this paper we have found that the effect of additive on enzyme stability is depended on the immobilization protocol. After assaying the effects of diverse chloride salts with different cations on different lipases activity, no relevant effect was detected. Free enzymes or the covalently immobilized enzymes are not stabilized by these cations for any of the studied lipases.  However, Mn2+ and Ca2+ (at a concentration of 5 mM) are able to greatly stabilize the lipases from Rhizomucor miehei (RML) and Candida rugosa (CRL) when they are present during the inactivation, but only if the enzymes are immobilized on octyl-agarose (stabilization factor ranging from 20 to 50).  The effect was only detected using more than 2.5 mM of the cations, and reached the maximum value at 5 mM, suggesting a saturation mechanism of action. The stabilization seemed to be based on a specific mechanism, and required to have the recognition sites saturated by the cations. Mg2+ has no effect on enzyme stability for both enzymes, but it is able to suppress the stabilization promoted by the other two cations using CRL; while it has no effect on the cation stabilization when using RML.
This is the first report of a cation induced enzyme stabilization effect that depends on the lipase immobilization protocol.
Palabras clave:interfacial activation, octyl-agarose, Lipase stabilization, additives, cations
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