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PublicationEnzyme and Microbial Technology
Year2017
Volume98
Pages18-25
International

EFFECT OF PROTEIN LOAD ON STABILITY OF IMMOBILIZED ENZYMES

Authors:Roberto Fernandez-Lafuente
Groups of research:Optimización de biocatalizadores y bioprocesos enzimáticos
Laura Fernandez-Lopez+, Sara G. Pedrero+, Nerea Lopez-Carrobles, Beatriz C. Gorines, Jose J. Virgen-Ortíz*a, Roberto Fernandez-Lafuente*
 
Departamento de biocatálisis.  Instituto de Catálisis-CSIC, Campus UAM-CSIC Madrid, Spain.
 
a CONACYT -  Centro de Investigación en Alimentación y Desarrollo, A.C., Centro de Innovación y Desarrollo Agroalimentario de Michoacán, A.C., Km. 8 Antigua Carretera a Pátzcuaro s/n, C.P. 58341, Morelia, Michoacán, México.


 Different lipases have been immobilized on octyl agarose beads at 1 mg/g and at maximum loading, via physical interfacial activation versus the octyl layer on the support. The stability of the preparations was analyzed.  Most biocatalysts had the expected result: the apparent stability increased using the highly loaded preparations, due to the diffusional limitations that reduced the initial observed activity. However, lipase B from Candida antarctica (CALB) was significantly more stable using the lowly loaded preparation than the maximum loaded one. This negative effect of the enzyme crowding on enzyme stability was found in inactivations at pH 5, 7 or 9, but not in inactivations in the presence of organic solvents. The immobilization using ethanol to reduce the immobilization rate had not effect on the stability of the lowly loaded preparation, while the highly loaded enzyme biocatalysts increased their stabilities, becoming very similar to that of the lowly loaded preparation. Results suggested that CALB molecules immobilized on octyl agarose may be closely packed together due to the high immobilization rate and this produced some negative interactions between immobilized enzyme molecules during enzyme thermal inactivation. Slowing-down the immobilization rate may be a solution for this unexpected problem.

Keywords:enzyme stability, control of immobilization rate, immobilized enzyme interactions, enzyme crowding, octyl agarose
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