Kinetic and Thermodynamic Study of 2-Ethylhexyl Oleate Synthesis Catalyzed by Candida antarctica Lipase Immobilized on a Magnetic Hybrid Support

This study investigated the kinetic and thermodynamic parameters of the synthesis of 2-ethylhexyl oleate catalyzed by Candida antarctica lipase (CALB) immobilized on magnetic poly(styrene- co -divinylbenzene) (STY-DVB-M). The influence of acid/alcohol molar ratio and temperature on oleic acid conver...

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Bibliographic Details
Published in:Catalysis letters 2021-05, Vol.151 (5), p.1239-1247
Main Authors: da Silva, Mateus V. C., Rangel, Amanda B. S., Dutra, Fellipe P., de Castro, Heizir F., de Freitas, Larissa
Format: Article
Language:English
Subjects:
Biocatalysts
Catalysis
Chemical reaction, Rate of
Chemical synthesis
Chemical tests and reagents
Chemistry
Chemistry and Materials Science
Divinylbenzene
Endothermic reactions
Industrial applications
Industrial Chemistry/Chemical Engineering
Lipase
Monounsaturated fatty acids
Oleic acid
Organometallic Chemistry
Parameters
Phenolphthalein
Physical Chemistry
Polystyrene resins
Productivity
Reaction kinetics
Reagents
Stability tests
Thermal properties
Thermal stability
Thermodynamics
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Summary:This study investigated the kinetic and thermodynamic parameters of the synthesis of 2-ethylhexyl oleate catalyzed by Candida antarctica lipase (CALB) immobilized on magnetic poly(styrene- co -divinylbenzene) (STY-DVB-M). The influence of acid/alcohol molar ratio and temperature on oleic acid conversion, ester concentration, and productivity was also assessed. Excess of one of the reagents resulted in high conversions, but the highest productivities were obtained at the stoichiometric ratio. Thus, a 1:1 molar ratio was considered optimal. Thermodynamic parameters calculated from the van’t Hoff equation (Δ S  =  + 850.64 J mol −1  K −1 , Δ H  =  + 273.78 kJ mol −1 ) revealed that the reaction is endothermic with a positive entropy change. Temperatures below 45 °C negatively affected reaction kinetics, explained by the positive Δ G values. CALB-STY-DVB-M showed a hydrolytic activity of 522.97 ± 19.14 U g −1 and was about 1.7 times more thermally stable at 60 °C than the free enzyme. In an operational stability test, conducted for 7 consecutive cycles of 24 h, the biocatalyst had a half-life of 739 h. CALB-STY-DVB-M showed satisfactory performance in the synthesis of 2-ethylhexyl oleate, providing oleic acid conversions close to 100%, ester concentration of 450 g L −1 , and productivity of 0.5 mmol g −1  h −1 . The biocatalyst holds promise for industrial applications. Graphic Abstract
ISSN:1011-372X
1572-879X
DOI:10.1007/s10562-020-03391-w