Conformational Changes of Lipases in Aqueous Media: A Comparative Computational Study and Experimental Implications
Abstract 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 sit...
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crwiley:10.1002/adsc.201100397 2024-06-23T07:47:02+00:00 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 2011 http://dx.doi.org/10.1002/adsc.201100397 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fadsc.201100397 https://onlinelibrary.wiley.com/doi/pdf/10.1002/adsc.201100397 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Advanced Synthesis & Catalysis volume 353, issue 13, page 2466-2480 ISSN 1615-4150 1615-4169 journal-article 2011 crwiley https://doi.org/10.1002/adsc.201100397 2024-06-13T04:21:57Z Abstract 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 Wiley Online Library Advanced Synthesis & Catalysis 353 13 2466 2480 |
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English |
description |
Abstract 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). |
format |
Article in Journal/Newspaper |
author |
Ferrario, Valerio Ebert, Cynthia Knapic, Lorena Fattor, Diana Basso, Alessandra Spizzo, Patrizia Gardossi, Lucia |
spellingShingle |
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 |
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 |
publisher |
Wiley |
publishDate |
2011 |
url |
http://dx.doi.org/10.1002/adsc.201100397 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fadsc.201100397 https://onlinelibrary.wiley.com/doi/pdf/10.1002/adsc.201100397 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Advanced Synthesis & Catalysis volume 353, issue 13, page 2466-2480 ISSN 1615-4150 1615-4169 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/adsc.201100397 |
container_title |
Advanced Synthesis & Catalysis |
container_volume |
353 |
container_issue |
13 |
container_start_page |
2466 |
op_container_end_page |
2480 |
_version_ |
1802650349646905344 |