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Accessing regio- and typo-selectivity of Yarrowia lipolytica lipase in its free form and immobilized onto magnetic nanoparticles

Akil E., Carvalho T., Baréa B., Finotelli P., Lecomte J., Torres A.G., Amaral P., Villeneuve P.. 2016. Biochemical Engineering Journal, 109 : p. 101-111.

DOI: 10.1016/j.bej.2015.12.019

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.

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