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Lipase-catalyzed synthesis of 2-ethylhexyl palmitate in a solvent free system using step changes in temperature

Authors
Choi, SuhyeonKim, Byung HeeNo, Da SomYoon, Sung WonLee, Moon-WonIm, Dong JoongKim, In-Hwan
Issue Date
1월-2022
Publisher
ELSEVIER
Keywords
2-Ethylhexyl palmitate; Eversa immobilized lipase; Hydrophobic carrier; Step change; Temperature
Citation
BIOCHEMICAL ENGINEERING JOURNAL, v.177
Indexed
SCIE
SCOPUS
Journal Title
BIOCHEMICAL ENGINEERING JOURNAL
Volume
177
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/135286
DOI
10.1016/j.bej.2021.108261
ISSN
1369-703X
Abstract
Lipase-catalyzed synthesis of 2-ethylhexyl palmitate (2-EHP) from 2-ethylhocyl alcohol and palmitic acid was carried out in a solvent-free system. A commercial liquid lipase (Eversa Transform 2.0, Novozymes) from Thermomyces lanuginosus was immobilized on Lewatit VP OC 1600, a macroporous hydrophobic carrier. The efficacy of this Eversa immobilized lipase prepared in this study was evaluated on the synthesis of 2-EHP compared with that of Novozym 435 (from Candida antarctica), Lipozyme RM IM (from Rhizomucor miehei), Lipozyme TL IM (from Thermomyces lanuginosus), and the liquid Eversa lipase (commercial name: Eversa Transform 2.0). Among these lipases, the Eversa immobilized lipase was the most effective for the synthesis of 2-EHP. Optimum conditions for the synthesis of 2-EHP using this enzyme were a temperature of 55 degrees C and enzyme loading of 2% (based on the total weight of substrate). The conversion of 97% was achieved under these optimum conditions. Finally, as a cost-saving strategy, a step change in the reaction temperature was introduced. When a step change in the reaction temperature between 55 degrees C and 45 degrees C used, an identical degree of conversion was achieved compared to a constant reaction temperature of 55 degrees C throughout the reaction.
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Kim, In Hwan
보건과학대학 (바이오시스템의과학부)
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