3 years ago

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

Effect of high salt concentrations on the stability of immobilized lipases: Dramatic deleterious effects of phosphate anions
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 4M sodium phosphate but 6M NaCl did not inactivate them. Using 2M 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 100mM sodium phosphate produced a significant decrease in enzyme stability; this effect was less pronounced for Lecitase but dramatic for CALB. While 6M 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 preparation.

Publisher URL: www.sciencedirect.com/science

DOI: S1359511317310292

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