Exploring mild enzymatic sustainable routes for the synthesis of bio‐degradable aromatic‐aliphatic oligoesters

Abstract The application of Candida antarctica lipase B in enzyme‐catalyzed synthesis of aromatic‐aliphatic oligoesters is here reported. The aim of the present study is to systematically investigate the most favorable conditions for the enzyme catalyzed synthesis of aromatic‐aliphatic oligomers usi...

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Published in:Biotechnology Journal
Main Authors: Pellis, Alessandro, Guarneri, Alice, Brandauer, Martin, Acero, Enrique Herrero, Peerlings, Henricus, Gardossi, Lucia, Guebitz, Georg M.
Other Authors: European Commission Seventh Framework Programme, Erasmus Universiteit
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2016
Subjects:
Online Access:http://dx.doi.org/10.1002/biot.201500544
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spelling crwiley:10.1002/biot.201500544 2024-09-15T17:44:53+00:00 Exploring mild enzymatic sustainable routes for the synthesis of bio‐degradable aromatic‐aliphatic oligoesters Pellis, Alessandro Guarneri, Alice Brandauer, Martin Acero, Enrique Herrero Peerlings, Henricus Gardossi, Lucia Guebitz, Georg M. European Commission Seventh Framework Programme Erasmus Universiteit 2016 http://dx.doi.org/10.1002/biot.201500544 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbiot.201500544 https://onlinelibrary.wiley.com/doi/pdf/10.1002/biot.201500544 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Biotechnology Journal volume 11, issue 5, page 642-647 ISSN 1860-6768 1860-7314 journal-article 2016 crwiley https://doi.org/10.1002/biot.201500544 2024-07-30T04:22:54Z Abstract The application of Candida antarctica lipase B in enzyme‐catalyzed synthesis of aromatic‐aliphatic oligoesters is here reported. The aim of the present study is to systematically investigate the most favorable conditions for the enzyme catalyzed synthesis of aromatic‐aliphatic oligomers using commercially available monomers. Reaction conditions and enzyme selectivity for polymerization of various commercially available monomers were considered using different inactivated/activated aromatic monomers combined with linear polyols ranging from C 2 to C 12 . The effect of various reaction solvents in enzymatic polymerization was assessed and toluene allowed to achieve the highest conversions for the reaction of dimethyl isophthalate with 1,4‐butanediol and with 1,10‐decanediol (88 and 87% monomer conversion respectively). M w as high as 1512 Da was obtained from the reaction of dimethyl isophthalate with 1,10‐decanediol. The obtained oligomers have potential applications as raw materials in personal and home care formulations, for the production of aliphatic‐aromatic block co‐polymers or can be further functionalized with various moieties for a subsequent photo‐ or radical polymerization. Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library Biotechnology Journal 11 5 642 647
institution Open Polar
collection Wiley Online Library
op_collection_id crwiley
language English
description Abstract The application of Candida antarctica lipase B in enzyme‐catalyzed synthesis of aromatic‐aliphatic oligoesters is here reported. The aim of the present study is to systematically investigate the most favorable conditions for the enzyme catalyzed synthesis of aromatic‐aliphatic oligomers using commercially available monomers. Reaction conditions and enzyme selectivity for polymerization of various commercially available monomers were considered using different inactivated/activated aromatic monomers combined with linear polyols ranging from C 2 to C 12 . The effect of various reaction solvents in enzymatic polymerization was assessed and toluene allowed to achieve the highest conversions for the reaction of dimethyl isophthalate with 1,4‐butanediol and with 1,10‐decanediol (88 and 87% monomer conversion respectively). M w as high as 1512 Da was obtained from the reaction of dimethyl isophthalate with 1,10‐decanediol. The obtained oligomers have potential applications as raw materials in personal and home care formulations, for the production of aliphatic‐aromatic block co‐polymers or can be further functionalized with various moieties for a subsequent photo‐ or radical polymerization.
author2 European Commission Seventh Framework Programme
Erasmus Universiteit
format Article in Journal/Newspaper
author Pellis, Alessandro
Guarneri, Alice
Brandauer, Martin
Acero, Enrique Herrero
Peerlings, Henricus
Gardossi, Lucia
Guebitz, Georg M.
spellingShingle Pellis, Alessandro
Guarneri, Alice
Brandauer, Martin
Acero, Enrique Herrero
Peerlings, Henricus
Gardossi, Lucia
Guebitz, Georg M.
Exploring mild enzymatic sustainable routes for the synthesis of bio‐degradable aromatic‐aliphatic oligoesters
author_facet Pellis, Alessandro
Guarneri, Alice
Brandauer, Martin
Acero, Enrique Herrero
Peerlings, Henricus
Gardossi, Lucia
Guebitz, Georg M.
author_sort Pellis, Alessandro
title Exploring mild enzymatic sustainable routes for the synthesis of bio‐degradable aromatic‐aliphatic oligoesters
title_short Exploring mild enzymatic sustainable routes for the synthesis of bio‐degradable aromatic‐aliphatic oligoesters
title_full Exploring mild enzymatic sustainable routes for the synthesis of bio‐degradable aromatic‐aliphatic oligoesters
title_fullStr Exploring mild enzymatic sustainable routes for the synthesis of bio‐degradable aromatic‐aliphatic oligoesters
title_full_unstemmed Exploring mild enzymatic sustainable routes for the synthesis of bio‐degradable aromatic‐aliphatic oligoesters
title_sort exploring mild enzymatic sustainable routes for the synthesis of bio‐degradable aromatic‐aliphatic oligoesters
publisher Wiley
publishDate 2016
url http://dx.doi.org/10.1002/biot.201500544
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbiot.201500544
https://onlinelibrary.wiley.com/doi/pdf/10.1002/biot.201500544
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source Biotechnology Journal
volume 11, issue 5, page 642-647
ISSN 1860-6768 1860-7314
op_rights http://onlinelibrary.wiley.com/termsAndConditions#vor
op_doi https://doi.org/10.1002/biot.201500544
container_title Biotechnology Journal
container_volume 11
container_issue 5
container_start_page 642
op_container_end_page 647
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