Continuous lipase-catalyzed production of pseudo-ceramides in a packed-bed bioreactor
International audience Ceramides are spingolipid compounds that are very attractive as active components in both the phar-maceutical and the cosmetic industries. In this study, the synthesis of ceramide analogs, the so-calledpseudo-ceramides, was carried out using for the first time a two-step conti...
Published in: | Journal of Molecular Catalysis B: Enzymatic |
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Online Access: | https://hal.archives-ouvertes.fr/hal-01070430 https://hal.archives-ouvertes.fr/hal-01070430/document https://hal.archives-ouvertes.fr/hal-01070430/file/Article_HAL.pdf https://doi.org/10.1016/j.molcatb.2014.08.022 |
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ftccsdartic:oai:HAL:hal-01070430v1 2023-05-15T13:56:06+02:00 Continuous lipase-catalyzed production of pseudo-ceramides in a packed-bed bioreactor Le Joubioux, Florian Bridiau, Nicolas Sanekli, Mehdi Graber, Marianne Maugard, Thierry LIttoral ENvironnement et Sociétés - UMRi 7266 (LIENSs) Université de La Rochelle (ULR)-Centre National de la Recherche Scientifique (CNRS) ANR Expenantio ANR-08-CP2D-0010,EXPENANTIO,Vers une voie durable pour la synthèse de molécules chirales: approches expérimentales et théoriques innovantes pour la compréhension des bases moléculaires de l'énantiosélectivité des lipases et des estérases - Towards green synthesis of chiral molecules(2008) 2014-09-06 https://hal.archives-ouvertes.fr/hal-01070430 https://hal.archives-ouvertes.fr/hal-01070430/document https://hal.archives-ouvertes.fr/hal-01070430/file/Article_HAL.pdf https://doi.org/10.1016/j.molcatb.2014.08.022 en eng HAL CCSD Elsevier info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2014.08.022 hal-01070430 https://hal.archives-ouvertes.fr/hal-01070430 https://hal.archives-ouvertes.fr/hal-01070430/document https://hal.archives-ouvertes.fr/hal-01070430/file/Article_HAL.pdf doi:10.1016/j.molcatb.2014.08.022 info:eu-repo/semantics/OpenAccess ISSN: 1381-1177 Journal of Molecular Catalysis B: Enzymatic https://hal.archives-ouvertes.fr/hal-01070430 Journal of Molecular Catalysis B: Enzymatic, Elsevier, 2014, 109, pp.143-153. ⟨10.1016/j.molcatb.2014.08.022⟩ [SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology info:eu-repo/semantics/article Journal articles 2014 ftccsdartic https://doi.org/10.1016/j.molcatb.2014.08.022 2021-10-24T12:57:05Z International audience Ceramides are spingolipid compounds that are very attractive as active components in both the phar-maceutical and the cosmetic industries. In this study, the synthesis of ceramide analogs, the so-calledpseudo-ceramides, was carried out using for the first time a two-step continuous enzymatic processwith immobilized Candida antarctica lipase B (Novozym®435) in a packed-bed bioreactor. The first stepinvolved the selective N-acylation of 3-amino-1,2-propanediol using stearic acid as the first acyl donor(i). This was followed by the selective O-acylation of the N-stearyl 3-amino-1,2-propanediol synthesizedin the first step, with myristic acid as the second acyl donor, to produce a N,O-diacyl 3-amino-1,2-propanediol-type pseudo-ceramide, namely 1-O-myristyl,3-N-stearyl 3-amino-1,2-propanediol (ii). Theprocess was first optimized by evaluating the influences of three factors: feed flow rate, quantity of bio-catalyst and substrate concentration. Under optimal conditions an amide synthesis yield of 92% and asatisfying production rate of almost 3.15 mmol h−1gbiocatalyst−1(1128 mg h−1gbiocatalyst−1) were obtained.The second step, N-acyl 3-amino-1,2-propanediol O-acylation, was similarly optimized and in additionthe effect of the substrate molar ratio was studied. Thus, an optimal pseudo-ceramide synthesis yield of54% and a production rate of 0.46 mmol h−1gbiocatalyst−1(261 mg h−1gbiocatalyst−1) were reached at a 1:3ratio of amide to fatty acid. In addition, it was demonstrated that this two-step process has great potentialfor the production of N,O-diacyl 3-amino-1,2-propanediol-type pseudo-ceramides on an industrial scale.It was shown in particular that Novozym®435 could be used for more than 3 weeks without a drop inthe yield during the first step of 3-amino-1,2-propanediol N-acylation, proving that this biocatalyst isvery stable under these operational conditions. This factor would greatly reduce the need for biocatalystreplacement and significantly lower the associated cost. Article in Journal/Newspaper Antarc* Antarctica Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) Journal of Molecular Catalysis B: Enzymatic 109 143 153 |
institution |
Open Polar |
collection |
Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) |
op_collection_id |
ftccsdartic |
language |
English |
topic |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology |
spellingShingle |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology Le Joubioux, Florian Bridiau, Nicolas Sanekli, Mehdi Graber, Marianne Maugard, Thierry Continuous lipase-catalyzed production of pseudo-ceramides in a packed-bed bioreactor |
topic_facet |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology |
description |
International audience Ceramides are spingolipid compounds that are very attractive as active components in both the phar-maceutical and the cosmetic industries. In this study, the synthesis of ceramide analogs, the so-calledpseudo-ceramides, was carried out using for the first time a two-step continuous enzymatic processwith immobilized Candida antarctica lipase B (Novozym®435) in a packed-bed bioreactor. The first stepinvolved the selective N-acylation of 3-amino-1,2-propanediol using stearic acid as the first acyl donor(i). This was followed by the selective O-acylation of the N-stearyl 3-amino-1,2-propanediol synthesizedin the first step, with myristic acid as the second acyl donor, to produce a N,O-diacyl 3-amino-1,2-propanediol-type pseudo-ceramide, namely 1-O-myristyl,3-N-stearyl 3-amino-1,2-propanediol (ii). Theprocess was first optimized by evaluating the influences of three factors: feed flow rate, quantity of bio-catalyst and substrate concentration. Under optimal conditions an amide synthesis yield of 92% and asatisfying production rate of almost 3.15 mmol h−1gbiocatalyst−1(1128 mg h−1gbiocatalyst−1) were obtained.The second step, N-acyl 3-amino-1,2-propanediol O-acylation, was similarly optimized and in additionthe effect of the substrate molar ratio was studied. Thus, an optimal pseudo-ceramide synthesis yield of54% and a production rate of 0.46 mmol h−1gbiocatalyst−1(261 mg h−1gbiocatalyst−1) were reached at a 1:3ratio of amide to fatty acid. In addition, it was demonstrated that this two-step process has great potentialfor the production of N,O-diacyl 3-amino-1,2-propanediol-type pseudo-ceramides on an industrial scale.It was shown in particular that Novozym®435 could be used for more than 3 weeks without a drop inthe yield during the first step of 3-amino-1,2-propanediol N-acylation, proving that this biocatalyst isvery stable under these operational conditions. This factor would greatly reduce the need for biocatalystreplacement and significantly lower the associated cost. |
author2 |
LIttoral ENvironnement et Sociétés - UMRi 7266 (LIENSs) Université de La Rochelle (ULR)-Centre National de la Recherche Scientifique (CNRS) ANR Expenantio ANR-08-CP2D-0010,EXPENANTIO,Vers une voie durable pour la synthèse de molécules chirales: approches expérimentales et théoriques innovantes pour la compréhension des bases moléculaires de l'énantiosélectivité des lipases et des estérases - Towards green synthesis of chiral molecules(2008) |
format |
Article in Journal/Newspaper |
author |
Le Joubioux, Florian Bridiau, Nicolas Sanekli, Mehdi Graber, Marianne Maugard, Thierry |
author_facet |
Le Joubioux, Florian Bridiau, Nicolas Sanekli, Mehdi Graber, Marianne Maugard, Thierry |
author_sort |
Le Joubioux, Florian |
title |
Continuous lipase-catalyzed production of pseudo-ceramides in a packed-bed bioreactor |
title_short |
Continuous lipase-catalyzed production of pseudo-ceramides in a packed-bed bioreactor |
title_full |
Continuous lipase-catalyzed production of pseudo-ceramides in a packed-bed bioreactor |
title_fullStr |
Continuous lipase-catalyzed production of pseudo-ceramides in a packed-bed bioreactor |
title_full_unstemmed |
Continuous lipase-catalyzed production of pseudo-ceramides in a packed-bed bioreactor |
title_sort |
continuous lipase-catalyzed production of pseudo-ceramides in a packed-bed bioreactor |
publisher |
HAL CCSD |
publishDate |
2014 |
url |
https://hal.archives-ouvertes.fr/hal-01070430 https://hal.archives-ouvertes.fr/hal-01070430/document https://hal.archives-ouvertes.fr/hal-01070430/file/Article_HAL.pdf https://doi.org/10.1016/j.molcatb.2014.08.022 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ISSN: 1381-1177 Journal of Molecular Catalysis B: Enzymatic https://hal.archives-ouvertes.fr/hal-01070430 Journal of Molecular Catalysis B: Enzymatic, Elsevier, 2014, 109, pp.143-153. ⟨10.1016/j.molcatb.2014.08.022⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2014.08.022 hal-01070430 https://hal.archives-ouvertes.fr/hal-01070430 https://hal.archives-ouvertes.fr/hal-01070430/document https://hal.archives-ouvertes.fr/hal-01070430/file/Article_HAL.pdf doi:10.1016/j.molcatb.2014.08.022 |
op_rights |
info:eu-repo/semantics/OpenAccess |
op_doi |
https://doi.org/10.1016/j.molcatb.2014.08.022 |
container_title |
Journal of Molecular Catalysis B: Enzymatic |
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109 |
container_start_page |
143 |
op_container_end_page |
153 |
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