Abstract

VALENZUELA-JARAMILLO, IVON-ESHER;  and  MENDOZA-MEZA, DARY;. Lipase of Pachira speciosa seeds immobilized in chitosan beads: a recyclable bio-catalytic system. Rev.Bio.Agro [online]. 2022, vol.20, n.1, pp.179-193.  Epub Dec 30, 2021. ISSN 1692-3561.  https://doi.org/10.18684/bsaa.v20.n1.2022.1890.

Plant lipases are highly versatile biocatalysts due to their chemo-selectivity, enantio-selectivity, and region-selectivity. The purpose was to obtain a recyclable biocatalyst from Pachira speciosa seed lipases, applicable to lipid bioconversion. A partially purified lipase was obtained from P. speciosa seed extracts, by gel filtration chromatography on Sephadex G-100; the specific lipase activity (LAS) was determined by free fatty acid titration. A Box-Behnken response surface design was applied to establish conditions that maximize lipase immobilization to three supports: chitosan beads (Ch), calcium alginate beads coated with chitosan (Alg-Ch), and chitosan-Fe(OH)3 magnetic beads (Ch-Fe). The highest LAS of the free enzyme was 8,23 ± 0,23 nKat/mg of protein at 40 °C and pH 9. The immobilization percentage and LAs (nKat/mg of beads) of each biocatalyst was EQ = 90,6 % and 3,74 ± 0,3 nKat/mg; Alg-Q = 88,5 % and 3,62 ± 0,1 nKat/mg; EQ-Fe = 76,4 % and 2,88 ± 0,1 nKat/mg. The most stable biocatalyst was the lipase immobilized in Ch, with 85 % retention of LAS until the third catalytic cycle. Future studies will be focused on establishing the kinetic parameters of the biocatalyst.

Keywords : Pachira speciosa; Plant lipase; Biocatalyst; Lipase activity; Immobilization; Chitosan; Alginate; Magnetic beads; Residual activity; Bioconversion.

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