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RevistaPROCESS BIOCHEMISTRY
Año2017
Volumen56
Páginas117-123
Internacional

EFFECT OF IMMOBILIZATION RATE AND ENZYME CROWDING ON ENZYME STABILITY UNDER DIFFERENT CONDITIONS. THE CASE OF LIPASE FROM Thermomyces lanuginosus IMMOBILIZED ON OCTYL AGAROSE BEADS

Autores:Roberto Fernandez-Lafuente
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos
Hadjer Zaak a,b,c, El-Hocine Siar a,d, Jakub F. Kornecki a, Laura Fernandez-Lopez a, Sara G. Pedrero a, Jose J. Virgen-Ortíz e, Roberto Fernandez-Lafuente a,*
 
a Departamento de Biocatálisis.  Instituto de Catálisis-CSIC, Campus UAM-CSIC Madrid, Spain.
b Food Biotechnology Division, Biotechnology Research Center (CRBt), Algeria
c Applied Microbiology in Environment Laboratory, Science Department, Ibn Khalboun University, Algeria.
d Transformation and Food Product Elaboration Laboratory, Nutrition and Food Technology Institute (INATAA), Algeria.
e CONACYT -  Centro de Investigación en Alimentación y Desarrollo, A.C., Consorcio CIDAM, A.C., Km. 8 Antigua Carretera a Pátzcuaro s/n, C.P. 58341, Morelia, Michoacán, México.



Lipase from Thermomyces lanuginosus (TLL) was immobilized on octyl agarose (OC). Three different TLL-OC biocatalysts were prepared: one lowly loaded using a low enzyme concentration, one fully loaded using a low enzyme concentrations, and a final one using a large excess of enzyme at a higher concentration. The activities after immobilization increased (180%), although diffusion limitations reduced the hyperactivation of the fully loaded preparations (140%). The stabilities of both preparations using low enzyme concentrations were similar under all studied conditions discounting the diffusional limitations of the biocatalyst. However, the biocatalyst prepared using a large concentration of enzyme was less stable that the other preparations at pH 7.0, more stable at pH 5.0 and with a similar stability at pH 9.0. Adding 3 M NaCl, the stability of the fully loaded preparations significantly increased; while the lowly loaded preparation slightly improved enzyme stability. This produced that the biocatalyst prepared under using high enzyme concentration become significantly more stable than the other two TLL preparations. Glycerin increased immobilized TLL stability, in this case all OC-TLL preparations became with similar stabilities. Results show that the TLL concentration during immobilization may greatly affect TLL properties, perhaps due to altering enzyme packing.
Palabras clave:immobilized enzyme distribution; enzyme packing; enzyme stability; octyl agarose; TLL stabilizers; glycerin.
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