Lipasa de semillas de Pachira speciosa inmovilizadas en esferas de quitosano: un sistema bio-catalítico reusable

Plant lipases are highly versatile biocatalysts due to their chemo-selectivity, enantio-selectivity, and region-selectivity. The purpose was to obtain a recyclable biocatalytic system from Pachira speciosa seed lipases, applicable to lipid biotransformation. 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 method. 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 0.49±0.01 U/mg at 40 °C and pH 9. The immobilization percentage and LAs of each biocatalytic system 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 biocatalytic system was 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 new biocatalyst.

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Bibliographic Details
Main Authors: Mendoza Meza, Dary, Valenzuela Jaramillo, Ivon Esher
Format: Digital revista
Language:spa
Published: Universidad del Cauca -Facultad de ciencias Agrarias 2021
Online Access:https://revistas.unicauca.edu.co/index.php/biotecnologia/article/view/1890
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