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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...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2020
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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. |
format | Online Article Text |
id | pubmed-7465053 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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