Conformational changes of lipases in aqueous media: A comparative computational study and experimental implications
Conformational changes occurring to the open form of five different lipases were studied by means of molecular dynamic simulations in explicit water. The conformational changes indicate remarkable differences among the lipases considered, not only in terms of accessibility of the active site but als...
Published in: | Advanced Synthesis & Catalysis |
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Online Access: | http://hdl.handle.net/11368/2400671 https://doi.org/10.1002/adsc.201100397 http://onlinelibrary.wiley.com/doi/10.1002/adsc.201100397/abstract |
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ftunitriestiris:oai:arts.units.it:11368/2400671 2023-05-15T14:00:24+02:00 Conformational changes of lipases in aqueous media: A comparative computational study and experimental implications FERRARIO, VALERIO EBERT, CYNTHIA KNAPIC, Lorena FATTOR, DIANA BASSO, ALESSANDRA SPIZZO, PATRIZIA GARDOSSI, Lucia Ferrario, Valerio Ebert, Cynthia Knapic, Lorena Fattor, Diana Basso, Alessandra Spizzo, Patrizia Gardossi, Lucia 2011 STAMPA http://hdl.handle.net/11368/2400671 https://doi.org/10.1002/adsc.201100397 http://onlinelibrary.wiley.com/doi/10.1002/adsc.201100397/abstract eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000295230900026 volume:353 issue:13 firstpage:2466 lastpage:2480 numberofpages:15 journal:ADVANCED SYNTHESIS & CATALYSIS http://hdl.handle.net/11368/2400671 doi:10.1002/adsc.201100397 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-80052799567 http://onlinelibrary.wiley.com/doi/10.1002/adsc.201100397/abstract info:eu-repo/semantics/closedAccess catalytic machinery conformational changes enzyme immobilization lipases molecular dynamic simulation info:eu-repo/semantics/article 2011 ftunitriestiris https://doi.org/10.1002/adsc.201100397 2023-04-09T06:07:29Z Conformational changes occurring to the open form of five different lipases were studied by means of molecular dynamic simulations in explicit water. The conformational changes indicate remarkable differences among the lipases considered, not only in terms of accessibility of the active site but also of modification of the geometry of the catalytic machinery. Lipase B from Candida antarctica undergoes minor conformational change at either level, so that it appears to be the most suitable lipase for being applied and formulated in aqueous environments or other hydrophilic media. On the other side, lipase from Pseudomonas cepacia undergoes the most relevant conformational variations both at the level of the catalytic triad and the residues involved in the oxyanion stabilization, suggesting that its “interfacial activation” is not simply related to a variation of the accessibility of the active site. Indeed, preliminary experimental data here reported indicate that covalent immobilization of lipase from Pseudomonas cepacia performed in the presence of hydrophobic solvent allows one to achieve a more than 10-fold increase in immobilization yield as compared to similar protocols performed in simple aqueous buffer. On the contrary, the benefit coming from immobilizing lipase B from Candida antarctica in hydrophobic solvent appears more limited (two-fold higher immobilization yield). Article in Journal/Newspaper Antarc* Antarctica Università degli studi di Trieste: ArTS (Archivio della ricerca di Trieste) Advanced Synthesis & Catalysis 353 13 2466 2480 |
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Open Polar |
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Università degli studi di Trieste: ArTS (Archivio della ricerca di Trieste) |
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ftunitriestiris |
language |
English |
topic |
catalytic machinery conformational changes enzyme immobilization lipases molecular dynamic simulation |
spellingShingle |
catalytic machinery conformational changes enzyme immobilization lipases molecular dynamic simulation FERRARIO, VALERIO EBERT, CYNTHIA KNAPIC, Lorena FATTOR, DIANA BASSO, ALESSANDRA SPIZZO, PATRIZIA GARDOSSI, Lucia Conformational changes of lipases in aqueous media: A comparative computational study and experimental implications |
topic_facet |
catalytic machinery conformational changes enzyme immobilization lipases molecular dynamic simulation |
description |
Conformational changes occurring to the open form of five different lipases were studied by means of molecular dynamic simulations in explicit water. The conformational changes indicate remarkable differences among the lipases considered, not only in terms of accessibility of the active site but also of modification of the geometry of the catalytic machinery. Lipase B from Candida antarctica undergoes minor conformational change at either level, so that it appears to be the most suitable lipase for being applied and formulated in aqueous environments or other hydrophilic media. On the other side, lipase from Pseudomonas cepacia undergoes the most relevant conformational variations both at the level of the catalytic triad and the residues involved in the oxyanion stabilization, suggesting that its “interfacial activation” is not simply related to a variation of the accessibility of the active site. Indeed, preliminary experimental data here reported indicate that covalent immobilization of lipase from Pseudomonas cepacia performed in the presence of hydrophobic solvent allows one to achieve a more than 10-fold increase in immobilization yield as compared to similar protocols performed in simple aqueous buffer. On the contrary, the benefit coming from immobilizing lipase B from Candida antarctica in hydrophobic solvent appears more limited (two-fold higher immobilization yield). |
author2 |
Ferrario, Valerio Ebert, Cynthia Knapic, Lorena Fattor, Diana Basso, Alessandra Spizzo, Patrizia Gardossi, Lucia |
format |
Article in Journal/Newspaper |
author |
FERRARIO, VALERIO EBERT, CYNTHIA KNAPIC, Lorena FATTOR, DIANA BASSO, ALESSANDRA SPIZZO, PATRIZIA GARDOSSI, Lucia |
author_facet |
FERRARIO, VALERIO EBERT, CYNTHIA KNAPIC, Lorena FATTOR, DIANA BASSO, ALESSANDRA SPIZZO, PATRIZIA GARDOSSI, Lucia |
author_sort |
FERRARIO, VALERIO |
title |
Conformational changes of lipases in aqueous media: A comparative computational study and experimental implications |
title_short |
Conformational changes of lipases in aqueous media: A comparative computational study and experimental implications |
title_full |
Conformational changes of lipases in aqueous media: A comparative computational study and experimental implications |
title_fullStr |
Conformational changes of lipases in aqueous media: A comparative computational study and experimental implications |
title_full_unstemmed |
Conformational changes of lipases in aqueous media: A comparative computational study and experimental implications |
title_sort |
conformational changes of lipases in aqueous media: a comparative computational study and experimental implications |
publishDate |
2011 |
url |
http://hdl.handle.net/11368/2400671 https://doi.org/10.1002/adsc.201100397 http://onlinelibrary.wiley.com/doi/10.1002/adsc.201100397/abstract |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:000295230900026 volume:353 issue:13 firstpage:2466 lastpage:2480 numberofpages:15 journal:ADVANCED SYNTHESIS & CATALYSIS http://hdl.handle.net/11368/2400671 doi:10.1002/adsc.201100397 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-80052799567 http://onlinelibrary.wiley.com/doi/10.1002/adsc.201100397/abstract |
op_rights |
info:eu-repo/semantics/closedAccess |
op_doi |
https://doi.org/10.1002/adsc.201100397 |
container_title |
Advanced Synthesis & Catalysis |
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353 |
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13 |
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2466 |
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2480 |
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