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Effect of high salt concentrations on the stability of immobilized lipases: Dramatic deleterious effects of phosphate anions

Autores:Roberto Fernandez-Lafuente
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos
Hadjer Zaak⁠a⁠, ⁠b⁠, ⁠c, Laura Fernandez-Lopez⁠a, Susana Velasco-Lozano⁠d, Maria Teresa Alcaraz-Fructuoso⁠a⁠, ⁠b⁠, ⁠c⁠, ⁠d⁠, ⁠e,
Mohamed Sassi⁠c⁠, ⁠⁎⁎, Fernando Lopez-Gallego⁠d⁠, ⁠e, Roberto Fernandez-Lafuente⁠a⁠, ⁠⁎
a Departamento de Biocatálisis, 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 Heterogenous Biocatalysis laboratory, CIC Biomagune, Paseo Miramon 182, 20014, San Sebastian, Spain
e IKERBASQUE, Basque Foundation for Science, Bilbao, Spain
We have analyzed the effects of the buffer nature on the stability of immobilized lipases. Commercial phospholipase
Lecitase Ultra (LU), lipase B from Candida antarctica (CALB) and lipase from Thermomyces lanuginosus (TLL)
have been immobilized on octyl-glyoxyl agarose beads. The enzymes were readily inactivated using 4 M sodium
phosphate but 6 M NaCl did not inactivate them. Using 2 M of sodium phosphate, the inactivation of the 3 immobilized
enzymes still was very significant even at 25 °C but at lower rate than with higher phosphate concentration.
Thermal stress inactivations of the immobilized enzymes revealed that even 100 mM sodium phosphate
produced a significant decrease in enzyme stability; this effect was less pronounced for Lecitase but dramatic for
CALB. While 6 M NaCl presented slightly positive (LU) or negative (TLL) effects on their thermal stabilities of,
CALB was thermally stabilized under the same conditions. Results were very different using free enymes. Fluorescence
spectroscopy revealed dramatic structural rearrangements of the immobilized enzymes in the presence
of high phosphate concentration. From these results, the use of sodium phosphate does not seem to be recommended
for studies on thermal stability of lipases, although this should be verified for each enzyme and immobilized

Palabras clave:Lipase stability, Phosphate inactivation of lipases, Buffers for lipases, Ionic strength and enzyme stability, Lipases immobilized in heterofunctional supports
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