Utilize este identificador para referenciar este registo:
https://hdl.handle.net/1822/60578
Registo completo
Campo DC | Valor | Idioma |
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dc.contributor.author | Noro, Jennifer | por |
dc.contributor.author | Castro, T. | por |
dc.contributor.author | Gonçalves, Filipa | por |
dc.contributor.author | Ribeiro, Artur | por |
dc.contributor.author | Cavaco-Paulo, Artur | por |
dc.contributor.author | Silva, Carla | por |
dc.date.accessioned | 2019-06-18T16:43:52Z | - |
dc.date.available | 2019-06-18T16:43:52Z | - |
dc.date.issued | 2019-05-20 | - |
dc.identifier.citation | Jennifer Noro; Castro, T.; Gonçalves, Filipa; Ribeiro, Artur; Cavaco-Paulo, Artur; Silva, Carla, Catalytic activation of esterases by PEGylation for polyester synthesis. ChemCatChem, 11(10), 2490-2499, 2019 | por |
dc.identifier.issn | 1867-3880 | por |
dc.identifier.uri | https://hdl.handle.net/1822/60578 | - |
dc.description.abstract | In this work we explored PEGylation as an efficient strategy to improve esterases catalytic performance. For this, we PEGylated three esterases, namely lipase from Candida antarctica B (CALB), lipase from Thermomyces lanuginosus (TL) and cutinase from Fusarium solani pisi (CUT) and evaluated their catalytic performance by using the biosynthesis of poly(ethylene glutarate) as model reaction. After PEGylation with a 5 kDa aldehydePEG, CALB and cutinase revealed an increase of activity against pnitrophenyl butyrate hydrolysis (2fold of increase for CALB and 4fold of increase for cutinase). Unmodified and PEGylated lipase TL displayed however similar activity results. The polymerase activity of native and PEGylated esterases was also assessed. The data revealed a higher polymerase activity for the lipase TL and cutinase PEGylated forms (88 % conversion for PEGlipase TL and 34 % for PEGcutinase). Molecular dynamics were used to evaluate the effect of PEG on the geometry of the active site of enzymes with lid domain (TL and CALB). These studies corroborate the experimental data revealing a more open active site cavity for the PEGylated catalysts facilitating the catalysis. | por |
dc.description.sponsorship | This study was supported by the Portuguese Foundation for Science and Technology (FCT) under the scope of the strategic funding of UID/BIO/04469/2019 unit and BioTecNorte operation (NORTE‐01‐0145‐FEDER‐000004) funded by European Regional Development Fund under the scope of Norte2020 ‐ Programa Operacional Regional do Norte. The authors thanks to FCT for funding their scholarship: Jennifer Noro (SFRH/BD/121673/2016), Filipa Gonçalves (SFRH/BD/114684/2016) and Artur Ribeiro (SFRH/BPD/98388/2013). Carla Silva is an investigator FCT (SFRH/IF/00186/2015). Tarsila Castro thanks the senior position funded by the European Union through the European Regional Development Fund (ERDF) under the Competitiveness Operational Program (BioCell‐NanoART=Novel Bio‐inspired Cellular Nano‐architectures, POC‐A1.1.4‐E‐2015 nr. 30/01. 09. 2016). Access to computing resources funded by the Project “Search‐ON2: Revitalization of HPC infrastructure of UMinho” (NORTE‐07‐0162‐FEDER‐000086), cofounded by the North Portugal Regional Operational Programme (ON.2‐O Novo Norte), under the National Strategic Reference Framework (NSRF), through the European Regional Development Fund (ERDF), is also gratefully acknowledged. | por |
dc.language.iso | eng | por |
dc.publisher | Wiley-Blackwell | por |
dc.relation | UID/BIO/04469/2019 | por |
dc.relation | SFRH/BD/121673/2016 | por |
dc.relation | SFRH/BD/114684/2016 | por |
dc.relation | info:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBPD%2F98388%2F2013/PT | por |
dc.relation | SFRH/IF/00186/2015 | por |
dc.rights | openAccess | por |
dc.subject | PEGylation | por |
dc.subject | esterases | por |
dc.subject | activity | por |
dc.subject | catalysis | por |
dc.subject | polyester | por |
dc.title | Catalytic activation of esterases by PEGylation for polyester synthesis | por |
dc.type | article | - |
dc.peerreviewed | yes | por |
dc.relation.publisherversion | http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1867-3899 | por |
dc.comments | CEB51666 | por |
oaire.citationStartPage | 2490 | por |
oaire.citationEndPage | 2499 | por |
oaire.citationIssue | 10 | por |
oaire.citationConferencePlace | Germany | - |
oaire.citationVolume | 11 | por |
dc.date.updated | 2019-06-01T11:28:03Z | - |
dc.identifier.eissn | 1867-3899 | por |
dc.identifier.doi | 10.1002/cctc.201900451 | por |
dc.description.publicationversion | info:eu-repo/semantics/publishedVersion | por |
dc.subject.wos | Science & Technology | por |
sdum.journal | Chemcatchem | por |
Aparece nas coleções: | CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series |
Ficheiros deste registo:
Ficheiro | Descrição | Tamanho | Formato | |
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document_51666_1.pdf | 1,46 MB | Adobe PDF | Ver/Abrir |