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spelling ftunivnantes:oai:HAL:hal-01918043v1 2023-05-15T13:35:52+02:00 Lipases/Acyltransferases for Lipid Modification in Aqueous Media Subileau, Maeva Jan, Anne Hélène Dubreucq, Eric Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE) Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro) 2018 https://hal.archives-ouvertes.fr/hal-01918043 https://doi.org/10.1016/B978-0-12-813167-1.00003-7 en eng HAL CCSD Academic Press info:eu-repo/semantics/altIdentifier/doi/10.1016/B978-0-12-813167-1.00003-7 ISBN: 9780128131671 hal-01918043 https://hal.archives-ouvertes.fr/hal-01918043 doi:10.1016/B978-0-12-813167-1.00003-7 PRODINRA: 451069 Lipid Modification by Enzymes and Engineered Microbes https://hal.archives-ouvertes.fr/hal-01918043 Lipid Modification by Enzymes and Engineered Microbes, Academic Press, 2018, 9780128131671. ⟨10.1016/B978-0-12-813167-1.00003-7⟩ Acyltransfer Alcoholysis Biocatalysis CAL-A from Moeziomyces antarcticus (Candida antarctica) CpLIP2 from Candida parapsilosis Structure/function Transesterification aqueous medium acétyltransférase hydrolase milieu aqueux lipase [SDV.IDA]Life Sciences [q-bio]/Food engineering info:eu-repo/semantics/bookPart Book sections 2018 ftunivnantes https://doi.org/10.1016/B978-0-12-813167-1.00003-7 2022-08-10T05:57:01Z Lipases/acyltransferases are a special group of lipases with highly enhanced affinity for other nucleophiles than water compared to classical lipases. In the presence of a suitable acceptor, they catalyze acyltransfer reactions (such as alcoholysis, aminolysis, or perhydrolysis) much faster than hydrolysis even in aqueous media with a high thermodynamic activity of water (aW). This allows kinetically controlled reactions where the donor ester is fully converted into the ester product before any significant release of free fatty acids. This chapter will discuss the kinetic aspects of the competitive reactions catalyzed by lipases/acyltransferases, propose a model, and a procedure to quantify their acyltransferase character, present some applications, and give an overview of currently known lipases/acyltransferases and of the structural studies and protein engineering strategies that have aimed at further improving their catalytic properties or even at turning lipases into acyltransferases. Book Part Antarc* Antarctica antarcticus Université de Nantes: HAL-UNIV-NANTES 45 68
institution Open Polar
collection Université de Nantes: HAL-UNIV-NANTES
op_collection_id ftunivnantes
language English
topic Acyltransfer
Alcoholysis
Biocatalysis
CAL-A from Moeziomyces antarcticus (Candida antarctica)
CpLIP2 from Candida parapsilosis
Structure/function
Transesterification
aqueous medium
acétyltransférase
hydrolase
milieu aqueux
lipase
[SDV.IDA]Life Sciences [q-bio]/Food engineering
spellingShingle Acyltransfer
Alcoholysis
Biocatalysis
CAL-A from Moeziomyces antarcticus (Candida antarctica)
CpLIP2 from Candida parapsilosis
Structure/function
Transesterification
aqueous medium
acétyltransférase
hydrolase
milieu aqueux
lipase
[SDV.IDA]Life Sciences [q-bio]/Food engineering
Subileau, Maeva
Jan, Anne Hélène
Dubreucq, Eric
Lipases/Acyltransferases for Lipid Modification in Aqueous Media
topic_facet Acyltransfer
Alcoholysis
Biocatalysis
CAL-A from Moeziomyces antarcticus (Candida antarctica)
CpLIP2 from Candida parapsilosis
Structure/function
Transesterification
aqueous medium
acétyltransférase
hydrolase
milieu aqueux
lipase
[SDV.IDA]Life Sciences [q-bio]/Food engineering
description Lipases/acyltransferases are a special group of lipases with highly enhanced affinity for other nucleophiles than water compared to classical lipases. In the presence of a suitable acceptor, they catalyze acyltransfer reactions (such as alcoholysis, aminolysis, or perhydrolysis) much faster than hydrolysis even in aqueous media with a high thermodynamic activity of water (aW). This allows kinetically controlled reactions where the donor ester is fully converted into the ester product before any significant release of free fatty acids. This chapter will discuss the kinetic aspects of the competitive reactions catalyzed by lipases/acyltransferases, propose a model, and a procedure to quantify their acyltransferase character, present some applications, and give an overview of currently known lipases/acyltransferases and of the structural studies and protein engineering strategies that have aimed at further improving their catalytic properties or even at turning lipases into acyltransferases.
author2 Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE)
Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)
format Book Part
author Subileau, Maeva
Jan, Anne Hélène
Dubreucq, Eric
author_facet Subileau, Maeva
Jan, Anne Hélène
Dubreucq, Eric
author_sort Subileau, Maeva
title Lipases/Acyltransferases for Lipid Modification in Aqueous Media
title_short Lipases/Acyltransferases for Lipid Modification in Aqueous Media
title_full Lipases/Acyltransferases for Lipid Modification in Aqueous Media
title_fullStr Lipases/Acyltransferases for Lipid Modification in Aqueous Media
title_full_unstemmed Lipases/Acyltransferases for Lipid Modification in Aqueous Media
title_sort lipases/acyltransferases for lipid modification in aqueous media
publisher HAL CCSD
publishDate 2018
url https://hal.archives-ouvertes.fr/hal-01918043
https://doi.org/10.1016/B978-0-12-813167-1.00003-7
genre Antarc*
Antarctica
antarcticus
genre_facet Antarc*
Antarctica
antarcticus
op_source Lipid Modification by Enzymes and Engineered Microbes
https://hal.archives-ouvertes.fr/hal-01918043
Lipid Modification by Enzymes and Engineered Microbes, Academic Press, 2018, 9780128131671. ⟨10.1016/B978-0-12-813167-1.00003-7⟩
op_relation info:eu-repo/semantics/altIdentifier/doi/10.1016/B978-0-12-813167-1.00003-7
ISBN: 9780128131671
hal-01918043
https://hal.archives-ouvertes.fr/hal-01918043
doi:10.1016/B978-0-12-813167-1.00003-7
PRODINRA: 451069
op_doi https://doi.org/10.1016/B978-0-12-813167-1.00003-7
container_start_page 45
op_container_end_page 68
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