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RevistaPROCESS BIOCHEMISTRY
Año2017
Volumen61
Páginas95-101
Internacional

COIMMOBILIZATION OF ENZYMES IN BILAYERS USING PEI AS A GLUE TO REUSE THE MOST STABLE ENZYME: PREVENTING PEI RELEASE DURING INACTIVATED ENZYME DESORPTION.

Autores:V.C: Corberan, Roberto Fernandez-Lafuente
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos, Catalizadores y procesos de oxidación selectiva (CPOS)
Hadjer Zaaka,b,c, Jakub F. Korneckia, El-Hocine Siara,d, Laura Fernandez-Lopeza, V. Cortés Corberána,  Mohamed Sassi*,c, Roberto Fernandez-Lafuentea,*
 
a Instituto de Catálisis y Petroleoquímica (ICP), CSIC, Campus UAM-CSIC, Madrid, Spain.
b Food Biotechnology Division, Biotechnology Research Center (CRBt), Constantine, Algeria
c Faculty of Nature and Life Sciences, Ibn Khalboun University, Tiaret, Algeria.
d Transformation and Food Product Elaboration Laboratory, Nutrition and Food Technology Institute (INATAA),  Algeria.
 
Coimmobilization of enzymes using polyethylenimine (PEI) as glue permits to reuse the most stable enzyme, immobilized on the support, after its incubation at high ionic strength to desorb the other enzyme, immobilized via ion exchange. However, this produced PEI desorption.  Now, we solve this problem via covalent immobilization of the PEI on the immobilized first and more stable enzyme and the glyoxyl support. The phospholipase Lecitase ultra (LU) and the lipase from Thermomyces lanuginosus (TLL) have been immobilized in octyl (OC) and OC-glyoxyl (OC-GLX) agarose beads, coated with PEI and used to immobilize β-galactosidase from Aspergillus oryze. The treatment of immobilized lipases with glutaraldehyde and the use of glyoxyl-octyl allowed preventing PEI release, even in the presence of  6 M NaCl.  As covalently immobilized LU and TLL were more stable than β-galactosidase, 3 cycles of β-galactosidase adsorption, thermal inactivation, desorption by incubation in 6 M NaCl and reloading of a fresh batch of galactosidase batch were performed. During these treatments, LU retained around 90% of the activity, and TLL more than 80%, and the PEI bound to these biocatalysts was maintained. This new strategy probed to be useful to allowing reusing the most stable enzyme without any further treatment.
 
Palabras clave:PEI, ion exchange, Operational Stability, enzyme desorption, Enzyme coimmobilization, enzyme reuse
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