Esterification of phenolic acids catalyzed by lipases immobilized in organogels

Abstract Lipases from Rhizomucor miehei and Candida antarctica B were immobilized in hydroxypropylmethyl cellulose organogels based on surfactant-free microemulsions consisting of n-hexane, 1-propanol and water. Both lipases kept their catalytic activity, catalyzing the esterification reactions of v...

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Published in:Biotechnology Letters
Language:English
Published: Springer Netherlands 2011
Subjects:
Online Access:http://hdl.handle.net/2262/55931
https://doi.org/10.1007/s10529-010-0305-x
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spelling fttrinitycoll:oai:tara.tcd.ie:2262/55931 2023-05-15T14:04:40+02:00 Esterification of phenolic acids catalyzed by lipases immobilized in organogels 2011-05-21T01:02:00Z http://hdl.handle.net/2262/55931 https://doi.org/10.1007/s10529-010-0305-x en eng Springer Netherlands Dordrecht 0141-5492 (pISSN) 1573-6776 (eISSN) 0141-5492 (ISSN) 10529 (JournalID) s10529-010-0305-x (publisherID) 305 (ArticleID) http://hdl.handle.net/2262/55931 Biotechnology Letters 32 10 1457 1462 doi:10.1007/s10529-010-0305-x Springer Science+Business Media B.V., 2010 12 months Biocatalysis Antioxidants Hydroxypropylmethyl cellulose 2011 fttrinitycoll https://doi.org/10.1007/s10529-010-0305-x 2020-02-16T13:52:12Z Abstract Lipases from Rhizomucor miehei and Candida antarctica B were immobilized in hydroxypropylmethyl cellulose organogels based on surfactant-free microemulsions consisting of n-hexane, 1-propanol and water. Both lipases kept their catalytic activity, catalyzing the esterification reactions of various phenolic acids including cinnamic acid derivatives. High reaction rates and yields (up to 94%) were obtained when lipase from C. antarctica was used. Kinetic studies have been performed and apparent kinetic constants were determined showing that ester synthesis catalyzed by immobilized lipases occurs via the Michaelis?Menten mechanism. phone: +302107273762 (Xenakis, A.) arisx@eie.gr (Xenakis, A.) Institute of Biological Research and Biotechnology, National Hellenic Research Foundation - Athens - GREECE (Zoumpanioti, M.) Institute of Biological Research and Biotechnology, National Hellenic Research Foundation - Athens - GREECE (Merianou, E.) Biological Applications and Technologies Department, University of Ioannina - Ioannina - GREECE (Merianou, E.) Institute of Biological Research and Biotechnology, National Hellenic Research Foundation - Athens - GREECE (Karandreas, T.) Biological Applications and Technologies Department, University of Ioannina - Ioannina - GREECE (Stamatis, H.) Institute of Biological Research and Biotechnology, National Hellenic Research Foundation - Athens - GREECE (Xenakis, A.) GREECE Registration: 2010-05-11 Received: 2010-03-10 Accepted: 2010-05-10 ePublished: 2010-05-21 Other/Unknown Material Antarc* Antarctica The University of Dublin, Trinity College: TARA (Trinity's Access to Research Archive) Biotechnology Letters 32 10 1457 1462
institution Open Polar
collection The University of Dublin, Trinity College: TARA (Trinity's Access to Research Archive)
op_collection_id fttrinitycoll
language English
topic Biocatalysis
Antioxidants
Hydroxypropylmethyl cellulose
spellingShingle Biocatalysis
Antioxidants
Hydroxypropylmethyl cellulose
Esterification of phenolic acids catalyzed by lipases immobilized in organogels
topic_facet Biocatalysis
Antioxidants
Hydroxypropylmethyl cellulose
description Abstract Lipases from Rhizomucor miehei and Candida antarctica B were immobilized in hydroxypropylmethyl cellulose organogels based on surfactant-free microemulsions consisting of n-hexane, 1-propanol and water. Both lipases kept their catalytic activity, catalyzing the esterification reactions of various phenolic acids including cinnamic acid derivatives. High reaction rates and yields (up to 94%) were obtained when lipase from C. antarctica was used. Kinetic studies have been performed and apparent kinetic constants were determined showing that ester synthesis catalyzed by immobilized lipases occurs via the Michaelis?Menten mechanism. phone: +302107273762 (Xenakis, A.) arisx@eie.gr (Xenakis, A.) Institute of Biological Research and Biotechnology, National Hellenic Research Foundation - Athens - GREECE (Zoumpanioti, M.) Institute of Biological Research and Biotechnology, National Hellenic Research Foundation - Athens - GREECE (Merianou, E.) Biological Applications and Technologies Department, University of Ioannina - Ioannina - GREECE (Merianou, E.) Institute of Biological Research and Biotechnology, National Hellenic Research Foundation - Athens - GREECE (Karandreas, T.) Biological Applications and Technologies Department, University of Ioannina - Ioannina - GREECE (Stamatis, H.) Institute of Biological Research and Biotechnology, National Hellenic Research Foundation - Athens - GREECE (Xenakis, A.) GREECE Registration: 2010-05-11 Received: 2010-03-10 Accepted: 2010-05-10 ePublished: 2010-05-21
title Esterification of phenolic acids catalyzed by lipases immobilized in organogels
title_short Esterification of phenolic acids catalyzed by lipases immobilized in organogels
title_full Esterification of phenolic acids catalyzed by lipases immobilized in organogels
title_fullStr Esterification of phenolic acids catalyzed by lipases immobilized in organogels
title_full_unstemmed Esterification of phenolic acids catalyzed by lipases immobilized in organogels
title_sort esterification of phenolic acids catalyzed by lipases immobilized in organogels
publisher Springer Netherlands
publishDate 2011
url http://hdl.handle.net/2262/55931
https://doi.org/10.1007/s10529-010-0305-x
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_relation 0141-5492 (pISSN)
1573-6776 (eISSN)
0141-5492 (ISSN)
10529 (JournalID)
s10529-010-0305-x (publisherID)
305 (ArticleID)
http://hdl.handle.net/2262/55931
Biotechnology Letters
32
10
1457
1462
doi:10.1007/s10529-010-0305-x
op_rights Springer Science+Business Media B.V., 2010
12 months
op_doi https://doi.org/10.1007/s10529-010-0305-x
container_title Biotechnology Letters
container_volume 32
container_issue 10
container_start_page 1457
op_container_end_page 1462
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