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Enzymatic Synthesis of Formate Ester through Immobilized Lipase and Its Reuse

Octyl formate is an important substance used in the perfume industry in products such as cosmetics, perfumes, and flavoring. Octyl formate is mostly produced by chemical catalysts. However, using enzymes as catalysts has gathered increasing interest due to their environment-friendly proprieties. In...

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Autores principales: Baek, Yesol, Lee, Jonghwa, Son, Jemin, Lee, Taek, Sobhan, Abdus, Lee, Jinyoung, Koo, Sang-Mo, Shin, Weon Ho, Oh, Jong-Min, Park, Chulhwan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7465053/
https://www.ncbi.nlm.nih.gov/pubmed/32796735
http://dx.doi.org/10.3390/polym12081802
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author Baek, Yesol
Lee, Jonghwa
Son, Jemin
Lee, Taek
Sobhan, Abdus
Lee, Jinyoung
Koo, Sang-Mo
Shin, Weon Ho
Oh, Jong-Min
Park, Chulhwan
author_facet Baek, Yesol
Lee, Jonghwa
Son, Jemin
Lee, Taek
Sobhan, Abdus
Lee, Jinyoung
Koo, Sang-Mo
Shin, Weon Ho
Oh, Jong-Min
Park, Chulhwan
author_sort Baek, Yesol
collection PubMed
description Octyl formate is an important substance used in the perfume industry in products such as cosmetics, perfumes, and flavoring. Octyl formate is mostly produced by chemical catalysts. However, using enzymes as catalysts has gathered increasing interest due to their environment-friendly proprieties. In the present study, we aimed to identify the optimal conditions for the synthesis of octyl formate through immobilized enzyme-mediated esterification. We investigated the effects of enzymatic reaction parameters including the type of immobilized enzyme, enzyme concentration, molar ratio of reactants, reaction temperature, and type of solvent using the optimization method of one factor at a time (OFAT). The maximum conversion achieved was 96.51% with Novozym 435 (15 g/L), a 1:7 formic acid to octanol ratio, a reaction temperature of 40 °C, and with 1,2-dichloroethane as solvent. Moreover, we demonstrated that the Novozym 435 can be reused under the optimal conditions without affecting the octyl formate yield, which could help reduce the economic burden associated with enzymatic synthesis.
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spelling pubmed-74650532020-09-04 Enzymatic Synthesis of Formate Ester through Immobilized Lipase and Its Reuse Baek, Yesol Lee, Jonghwa Son, Jemin Lee, Taek Sobhan, Abdus Lee, Jinyoung Koo, Sang-Mo Shin, Weon Ho Oh, Jong-Min Park, Chulhwan Polymers (Basel) Article Octyl formate is an important substance used in the perfume industry in products such as cosmetics, perfumes, and flavoring. Octyl formate is mostly produced by chemical catalysts. However, using enzymes as catalysts has gathered increasing interest due to their environment-friendly proprieties. In the present study, we aimed to identify the optimal conditions for the synthesis of octyl formate through immobilized enzyme-mediated esterification. We investigated the effects of enzymatic reaction parameters including the type of immobilized enzyme, enzyme concentration, molar ratio of reactants, reaction temperature, and type of solvent using the optimization method of one factor at a time (OFAT). The maximum conversion achieved was 96.51% with Novozym 435 (15 g/L), a 1:7 formic acid to octanol ratio, a reaction temperature of 40 °C, and with 1,2-dichloroethane as solvent. Moreover, we demonstrated that the Novozym 435 can be reused under the optimal conditions without affecting the octyl formate yield, which could help reduce the economic burden associated with enzymatic synthesis. MDPI 2020-08-11 /pmc/articles/PMC7465053/ /pubmed/32796735 http://dx.doi.org/10.3390/polym12081802 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Baek, Yesol
Lee, Jonghwa
Son, Jemin
Lee, Taek
Sobhan, Abdus
Lee, Jinyoung
Koo, Sang-Mo
Shin, Weon Ho
Oh, Jong-Min
Park, Chulhwan
Enzymatic Synthesis of Formate Ester through Immobilized Lipase and Its Reuse
title Enzymatic Synthesis of Formate Ester through Immobilized Lipase and Its Reuse
title_full Enzymatic Synthesis of Formate Ester through Immobilized Lipase and Its Reuse
title_fullStr Enzymatic Synthesis of Formate Ester through Immobilized Lipase and Its Reuse
title_full_unstemmed Enzymatic Synthesis of Formate Ester through Immobilized Lipase and Its Reuse
title_short Enzymatic Synthesis of Formate Ester through Immobilized Lipase and Its Reuse
title_sort enzymatic synthesis of formate ester through immobilized lipase and its reuse
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7465053/
https://www.ncbi.nlm.nih.gov/pubmed/32796735
http://dx.doi.org/10.3390/polym12081802
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