Enlarging the tools for efficient enzymatic polycondensation: structural and catalytic features of cutinase 1 from Thermobifida cellulosilytica
Cutinase 1 from Thermobifida cellulosilytica is reported for the first time as an efficient biocatalyst in polycondensation reactions. Under thin film conditions the covalently immobilized enzyme catalyzes the synthesis of oligoesters of dimetil adipate with different polyols leading to higher Mw (~...
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ftunitriestiris:oai:arts.units.it:11368/2880286 2023-05-15T13:54:54+02:00 Enlarging the tools for efficient enzymatic polycondensation: structural and catalytic features of cutinase 1 from Thermobifida cellulosilytica Pellis, Alessandro Zartl, Barbara Brandauer, Martin Gamerith, Caroline Herrero Acero, Enrique Guebitz, Georg FERRARIO, VALERIO EBERT, CYNTHIA GARDOSSI, Lucia Pellis, Alessandro Ferrario, Valerio Zartl, Barbara Brandauer, Martin Gamerith, Caroline Herrero Acero, Enrique Ebert, Cynthia Gardossi, Lucia Guebitz, Georg 2016 ELETTRONICO http://hdl.handle.net/11368/2880286 https://doi.org/10.1039/C5CY01746G http://pubs.rsc.org/en/content/articlelanding/2015/cy/c5cy01746g/unauth#!divAbstract eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000376090900012 volume:6 issue:10 firstpage:3430 lastpage:3442 numberofpages:13 journal:CATALYSIS SCIENCE & TECHNOLOGY info:eu-repo/grantAgreement/EC/FP7/289253 (REFINE project) http://hdl.handle.net/11368/2880286 doi:10.1039/C5CY01746G info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84970967364 http://pubs.rsc.org/en/content/articlelanding/2015/cy/c5cy01746g/unauth#!divAbstract info:eu-repo/semantics/openAccess cutinase polyester polycondensation biocatalysi bio-based polymer molecular modeling info:eu-repo/semantics/article 2016 ftunitriestiris https://doi.org/10.1039/C5CY01746G 2023-04-09T06:13:33Z Cutinase 1 from Thermobifida cellulosilytica is reported for the first time as an efficient biocatalyst in polycondensation reactions. Under thin film conditions the covalently immobilized enzyme catalyzes the synthesis of oligoesters of dimetil adipate with different polyols leading to higher Mw (~1900) and Mn (~1000) if compared to lipase B from Candida antarctica or cutinase from Humicola insolens. Computational analysis discloses the structural features that make this enzyme readily accessible to substrates and optimally suited for covalent immobilization. As lipases and other cutinase enzymes, it presents hydrophobic superficial regions around the active site. However, molecular dynamics simulations indicate the absence of interfacial activation, similarly to what already documented for lipase B from Candida antarctica. Notably, cutinase from Humicola insolens displays a “breathing like” conformational movement, which modifies the accessibility of the active site. These observations stimulate wider experimental and bioinformatics studies aiming at a systematic comparison of functional differences between cutinases and lipases. Article in Journal/Newspaper Antarc* Antarctica Università degli studi di Trieste: ArTS (Archivio della ricerca di Trieste) Catalysis Science & Technology 6 10 3430 3442 |
institution |
Open Polar |
collection |
Università degli studi di Trieste: ArTS (Archivio della ricerca di Trieste) |
op_collection_id |
ftunitriestiris |
language |
English |
topic |
cutinase polyester polycondensation biocatalysi bio-based polymer molecular modeling |
spellingShingle |
cutinase polyester polycondensation biocatalysi bio-based polymer molecular modeling Pellis, Alessandro Zartl, Barbara Brandauer, Martin Gamerith, Caroline Herrero Acero, Enrique Guebitz, Georg FERRARIO, VALERIO EBERT, CYNTHIA GARDOSSI, Lucia Enlarging the tools for efficient enzymatic polycondensation: structural and catalytic features of cutinase 1 from Thermobifida cellulosilytica |
topic_facet |
cutinase polyester polycondensation biocatalysi bio-based polymer molecular modeling |
description |
Cutinase 1 from Thermobifida cellulosilytica is reported for the first time as an efficient biocatalyst in polycondensation reactions. Under thin film conditions the covalently immobilized enzyme catalyzes the synthesis of oligoesters of dimetil adipate with different polyols leading to higher Mw (~1900) and Mn (~1000) if compared to lipase B from Candida antarctica or cutinase from Humicola insolens. Computational analysis discloses the structural features that make this enzyme readily accessible to substrates and optimally suited for covalent immobilization. As lipases and other cutinase enzymes, it presents hydrophobic superficial regions around the active site. However, molecular dynamics simulations indicate the absence of interfacial activation, similarly to what already documented for lipase B from Candida antarctica. Notably, cutinase from Humicola insolens displays a “breathing like” conformational movement, which modifies the accessibility of the active site. These observations stimulate wider experimental and bioinformatics studies aiming at a systematic comparison of functional differences between cutinases and lipases. |
author2 |
Pellis, Alessandro Ferrario, Valerio Zartl, Barbara Brandauer, Martin Gamerith, Caroline Herrero Acero, Enrique Ebert, Cynthia Gardossi, Lucia Guebitz, Georg |
format |
Article in Journal/Newspaper |
author |
Pellis, Alessandro Zartl, Barbara Brandauer, Martin Gamerith, Caroline Herrero Acero, Enrique Guebitz, Georg FERRARIO, VALERIO EBERT, CYNTHIA GARDOSSI, Lucia |
author_facet |
Pellis, Alessandro Zartl, Barbara Brandauer, Martin Gamerith, Caroline Herrero Acero, Enrique Guebitz, Georg FERRARIO, VALERIO EBERT, CYNTHIA GARDOSSI, Lucia |
author_sort |
Pellis, Alessandro |
title |
Enlarging the tools for efficient enzymatic polycondensation: structural and catalytic features of cutinase 1 from Thermobifida cellulosilytica |
title_short |
Enlarging the tools for efficient enzymatic polycondensation: structural and catalytic features of cutinase 1 from Thermobifida cellulosilytica |
title_full |
Enlarging the tools for efficient enzymatic polycondensation: structural and catalytic features of cutinase 1 from Thermobifida cellulosilytica |
title_fullStr |
Enlarging the tools for efficient enzymatic polycondensation: structural and catalytic features of cutinase 1 from Thermobifida cellulosilytica |
title_full_unstemmed |
Enlarging the tools for efficient enzymatic polycondensation: structural and catalytic features of cutinase 1 from Thermobifida cellulosilytica |
title_sort |
enlarging the tools for efficient enzymatic polycondensation: structural and catalytic features of cutinase 1 from thermobifida cellulosilytica |
publishDate |
2016 |
url |
http://hdl.handle.net/11368/2880286 https://doi.org/10.1039/C5CY01746G http://pubs.rsc.org/en/content/articlelanding/2015/cy/c5cy01746g/unauth#!divAbstract |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:000376090900012 volume:6 issue:10 firstpage:3430 lastpage:3442 numberofpages:13 journal:CATALYSIS SCIENCE & TECHNOLOGY info:eu-repo/grantAgreement/EC/FP7/289253 (REFINE project) http://hdl.handle.net/11368/2880286 doi:10.1039/C5CY01746G info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84970967364 http://pubs.rsc.org/en/content/articlelanding/2015/cy/c5cy01746g/unauth#!divAbstract |
op_rights |
info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.1039/C5CY01746G |
container_title |
Catalysis Science & Technology |
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6 |
container_issue |
10 |
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3430 |
op_container_end_page |
3442 |
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