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The Effect of Solvent Hydrophilicity on the Enzymatic Ring-Opening Polymerization of L-Lactide by Candida rugosa Lipase
Contradictions have been reported on the effect of organic solvents, especially toluene, on enzymatic ring-opening polymerization (eROP) of L-lactide. Studies have shown that log P, a common measure of hydrophilicity, affects enzyme activity. This study examines the effect of solvents with various l...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9505578/ https://www.ncbi.nlm.nih.gov/pubmed/36146005 http://dx.doi.org/10.3390/polym14183856 |
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author | Curie, Catia Angli Darmawan, Muhammad Arif Dianursanti, Dianursanti Budhijanto, Wiratni Gozan, Misri |
author_facet | Curie, Catia Angli Darmawan, Muhammad Arif Dianursanti, Dianursanti Budhijanto, Wiratni Gozan, Misri |
author_sort | Curie, Catia Angli |
collection | PubMed |
description | Contradictions have been reported on the effect of organic solvents, especially toluene, on enzymatic ring-opening polymerization (eROP) of L-lactide. Studies have shown that log P, a common measure of hydrophilicity, affects enzyme activity. This study examines the effect of solvents with various log P values on the eROP of L-lactide, performed using Candida rugosa lipase (CRL). N,N-dimethylacetamide (DMA), 1,2-dimethoxybenzene, 1,4-dimethoxybenzene, diphenyl ether, and dodecane were used as the organic solvents. The eROP in ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate ([BMIM][PF(6)]) was also conducted to compare its performance with the organic solvents. The results show that [BMIM][PF(6)]-mediated eROP gave better conversion and molecular weight than the organic solvent-mediated eROP. In this study, the effects of solvents hydrophilicity are discussed, including the possibility of hexafluorophosphate ion ([PF(6)](−)) hydrolysis to occur. |
format | Online Article Text |
id | pubmed-9505578 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-95055782022-09-24 The Effect of Solvent Hydrophilicity on the Enzymatic Ring-Opening Polymerization of L-Lactide by Candida rugosa Lipase Curie, Catia Angli Darmawan, Muhammad Arif Dianursanti, Dianursanti Budhijanto, Wiratni Gozan, Misri Polymers (Basel) Article Contradictions have been reported on the effect of organic solvents, especially toluene, on enzymatic ring-opening polymerization (eROP) of L-lactide. Studies have shown that log P, a common measure of hydrophilicity, affects enzyme activity. This study examines the effect of solvents with various log P values on the eROP of L-lactide, performed using Candida rugosa lipase (CRL). N,N-dimethylacetamide (DMA), 1,2-dimethoxybenzene, 1,4-dimethoxybenzene, diphenyl ether, and dodecane were used as the organic solvents. The eROP in ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate ([BMIM][PF(6)]) was also conducted to compare its performance with the organic solvents. The results show that [BMIM][PF(6)]-mediated eROP gave better conversion and molecular weight than the organic solvent-mediated eROP. In this study, the effects of solvents hydrophilicity are discussed, including the possibility of hexafluorophosphate ion ([PF(6)](−)) hydrolysis to occur. MDPI 2022-09-15 /pmc/articles/PMC9505578/ /pubmed/36146005 http://dx.doi.org/10.3390/polym14183856 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Curie, Catia Angli Darmawan, Muhammad Arif Dianursanti, Dianursanti Budhijanto, Wiratni Gozan, Misri The Effect of Solvent Hydrophilicity on the Enzymatic Ring-Opening Polymerization of L-Lactide by Candida rugosa Lipase |
title | The Effect of Solvent Hydrophilicity on the Enzymatic Ring-Opening Polymerization of L-Lactide by Candida rugosa Lipase |
title_full | The Effect of Solvent Hydrophilicity on the Enzymatic Ring-Opening Polymerization of L-Lactide by Candida rugosa Lipase |
title_fullStr | The Effect of Solvent Hydrophilicity on the Enzymatic Ring-Opening Polymerization of L-Lactide by Candida rugosa Lipase |
title_full_unstemmed | The Effect of Solvent Hydrophilicity on the Enzymatic Ring-Opening Polymerization of L-Lactide by Candida rugosa Lipase |
title_short | The Effect of Solvent Hydrophilicity on the Enzymatic Ring-Opening Polymerization of L-Lactide by Candida rugosa Lipase |
title_sort | effect of solvent hydrophilicity on the enzymatic ring-opening polymerization of l-lactide by candida rugosa lipase |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9505578/ https://www.ncbi.nlm.nih.gov/pubmed/36146005 http://dx.doi.org/10.3390/polym14183856 |
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