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

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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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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institution UNICAUCA CO
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country Colombia
countrycode CO
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databasecode rev-bsaa-co
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libraryname Biblioteca de la UNICAUCA de Colombia
language spa
format Digital
author Mendoza Meza, Dary
Valenzuela Jaramillo, Ivon Esher
spellingShingle Mendoza Meza, Dary
Valenzuela Jaramillo, Ivon Esher
Lipasa de semillas de Pachira speciosa inmovilizadas en esferas de quitosano: un sistema bio-catalítico reusable
author_facet Mendoza Meza, Dary
Valenzuela Jaramillo, Ivon Esher
author_sort Mendoza Meza, Dary
title Lipasa de semillas de Pachira speciosa inmovilizadas en esferas de quitosano: un sistema bio-catalítico reusable
title_short Lipasa de semillas de Pachira speciosa inmovilizadas en esferas de quitosano: un sistema bio-catalítico reusable
title_full Lipasa de semillas de Pachira speciosa inmovilizadas en esferas de quitosano: un sistema bio-catalítico reusable
title_fullStr Lipasa de semillas de Pachira speciosa inmovilizadas en esferas de quitosano: un sistema bio-catalítico reusable
title_full_unstemmed Lipasa de semillas de Pachira speciosa inmovilizadas en esferas de quitosano: un sistema bio-catalítico reusable
title_sort lipasa de semillas de pachira speciosa inmovilizadas en esferas de quitosano: un sistema bio-catalítico reusable
description 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.
publisher Universidad del Cauca -Facultad de ciencias Agrarias
publishDate 2021
url https://revistas.unicauca.edu.co/index.php/biotecnologia/article/view/1890
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AT valenzuelajaramilloivonesher lipasadesemillasdepachiraspeciosainmovilizadasenesferasdequitosanounsistemabiocataliticoreusable
AT mendozamezadary lipaseofpachiraspeciosaseedsimmobilizedinchitosanbeadsarecyclablebiocatalyticsystem
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spelling rev-bsaa-co-article-18902021-12-23T20:21:44Z Lipasa de semillas de Pachira speciosa inmovilizadas en esferas de quitosano: un sistema bio-catalítico reusable Lipase of Pachira speciosa seeds immobilized in chitosan beads: a recyclable bio-catalytic system Mendoza Meza, Dary Valenzuela Jaramillo, Ivon Esher Lipasa vegetal Inmovilización Actividad Lipolitica Biocatalizador Quitosano Pachira speciosa Bioconversion Actividad residual Esferas magnéticas Alginato Plant Lipase Immobilization Lipolytic Activity Biocatalyst Chitosan Bioconversion Residual activity Magnetic beads Alginate Pachira speciosa 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. Las lipasas vegetales son biocatalizadores altamente versátiles debido a su quimioselectividad, enantioselectividad y regioselectividad. El propósito fue obtener un sistema biocatalítico reciclable a partir de lipasas de semillas de Pachira speciosa, aplicable a la biotransformación de lípidos. Se obtuvo una lipasa parcialmente purificada de extractos de semillas de P. speciosa, mediante cromatografía de filtración en gel en Sephadex G-100; la actividad específica lipasa (ALe) se determinó por el método de titulación de ácidos grasos libres. Se aplicó un diseño de superficie de repuesta Box-Behnken para establecer las condiciones que maximizan la inmovilización de la lipasa a tres soportes: esferas de quitosano (Q), esferas de alginato de calcio cubiertas con quitosano (Alg-Q) y esferas magnéticas de quitosano-Fe(OH)3 (Q-Fe). La mayor ALe de la enzima libre fue 0,49±0,01U/mg, a 40 °C y pH 9. El porcentaje de inmovilización y la ALe de cada biocatalízador fue: Q = 90,6 % y 3,74±0,3 nKat/mg; Alg-Q = 88,5 % y 3,62±0,1 nKat/mg; EQ-Fe = 76,4 % y 2,88±0,1 nKat/mg. El sistema biocatalítico más estable fue la lipasa inmovilizada en quitosano, con 85 % de rentención de la ALe hasta el tercer ciclo catalítico. Estudios futuros estarán enfocados a establecer los parámetros cinéticos del nuevo biocatalizador. 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