Accessing regio- and typo-selectivity of #Yarrowia lipolytica# lipase in its free form and immobilized onto magnetic nanoparticles
2016
Akil E. | Carvalho T. | Baréa B. | Finotelli P. | Lecomte J. | Torres A.G. | Villeneuve P.
The growing interest in lipases is related to its high biotechnological potential. In this work we investigated the regio- and typo-selectivity of extracellular lipase from Yarrowia lipolytica 583 (IMUFRJ 50682) in its free form and immobilized on magnetic nano-sized particles. Results of p-nitrophenyl laurate hydrolysis showed optimal stability of these biocatalysts at pH 6–8 and between 20 and 45 °C. The immobilization of lipase on nano-sized magnetic particles increased thermo and pH stabilities of the enzyme. Both catalysts displayed high hydrolytic activity on triolein and on triacylglycerols in vegetable oils in 5 min. The free lipase showed a strict 1,3-regioselectivity, whereas the immobilized lipase was only slightly 1,3-regioselective, in hydrolysis reactions of triolein and vegetable oils. Both lipases were able to hydrolyze saturated esters, but showed no typo-selectivity for this group. However, the lipases are selective for the hydrolysis of unsaturated esters, especially for 18:2 fatty acids. These results give a better knowledge of this lipase hydrolytic activity, both in the free form and immobilized and widen their potential biotechnological use, especially in the synthesis of structured lipids. (Résumé d'auteur)
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