NOVEL Cu/Ag-ENZYME BIOHYBRIDS AS ARTIFICIAL METALLOENZYME
In recent years, the synthesis of novel artificial metalloenzymes by the combination of metal or complex organometallic systems and enzymes is rapidly growing field of research in catalytic applications. In this study, new artificial metalloenzymes have been designed and developed based on the combi...
Main Authors: | , , , , , |
---|---|
Format: | Conference Object |
Language: | English |
Published: |
Belgrade : University, Faculty of Technology and Metallurgy
2023
|
Subjects: | |
Online Access: | http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6959 https://hdl.handle.net/21.15107/rcub_technorep_6959 |
id |
ftunivbelgradftm:oai:TechnoRep.tmf.bg.ac.rs:123456789/6959 |
---|---|
record_format |
openpolar |
spelling |
ftunivbelgradftm:oai:TechnoRep.tmf.bg.ac.rs:123456789/6959 2024-01-14T10:01:22+01:00 NOVEL Cu/Ag-ENZYME BIOHYBRIDS AS ARTIFICIAL METALLOENZYME Ortega-Nieto, Clara Losada-Gracia, Noelia Vukoičić, Ana Milivojević, Ana Bezbradica, Dejan Palomo, Jose M. 2023 http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6959 https://hdl.handle.net/21.15107/rcub_technorep_6959 en eng Belgrade : University, Faculty of Technology and Metallurgy info:eu-repo/grantAgreement/MESTD/inst-2020/200135/RS// info:eu-repo/grantAgreement/MESTD/inst-2020/200287/RS// Horizon Europe 2021-2027 research and innovation programme under grant agreement ID 101060130 (TwinPrebioEnz) 978-86-7401-389-2 http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6959 https://hdl.handle.net/21.15107/rcub_technorep_6959 restrictedAccess ARR Book of Abstracts / International Conference Biochemical Engineering and Biotechnology for Young Scientists, 7-8 December, 2023, Belgrade metalloenzymes copper silver phloridzin lacasse-like activity conferenceObject publishedVersion 2023 ftunivbelgradftm 2023-12-19T17:19:59Z In recent years, the synthesis of novel artificial metalloenzymes by the combination of metal or complex organometallic systems and enzymes is rapidly growing field of research in catalytic applications. In this study, new artificial metalloenzymes have been designed and developed based on the combination of an enzyme and different metal salts. For this purpose, novel synthesis method has been used, where the enzyme, Lipase B from Candida antarctica (CALB), acts as an inducer of metal nanoparticles of copper and silver. Obtained biohybrids show improved stability properties compared to natural enzymes. Moreover, the synergetic effect between copper and silver has been evaluated, looking for an improvement in the catalytic efficiency of an only copper-metalloenzyme previously developed. The copper-silver-CALB metalloenzymes have been characterized by X-Ray diffraction analysis, mass spectrometry, and SEM and TEM as microscopies techniques. After that, their catalytic efficiency was tested in different reactions, in particular in the phloridzin oligomerization as laccase-like activity. Conference Object Antarc* Antarctica TechnoRep - Faculty of Technology and Metallurgy Repository |
institution |
Open Polar |
collection |
TechnoRep - Faculty of Technology and Metallurgy Repository |
op_collection_id |
ftunivbelgradftm |
language |
English |
topic |
metalloenzymes copper silver phloridzin lacasse-like activity |
spellingShingle |
metalloenzymes copper silver phloridzin lacasse-like activity Ortega-Nieto, Clara Losada-Gracia, Noelia Vukoičić, Ana Milivojević, Ana Bezbradica, Dejan Palomo, Jose M. NOVEL Cu/Ag-ENZYME BIOHYBRIDS AS ARTIFICIAL METALLOENZYME |
topic_facet |
metalloenzymes copper silver phloridzin lacasse-like activity |
description |
In recent years, the synthesis of novel artificial metalloenzymes by the combination of metal or complex organometallic systems and enzymes is rapidly growing field of research in catalytic applications. In this study, new artificial metalloenzymes have been designed and developed based on the combination of an enzyme and different metal salts. For this purpose, novel synthesis method has been used, where the enzyme, Lipase B from Candida antarctica (CALB), acts as an inducer of metal nanoparticles of copper and silver. Obtained biohybrids show improved stability properties compared to natural enzymes. Moreover, the synergetic effect between copper and silver has been evaluated, looking for an improvement in the catalytic efficiency of an only copper-metalloenzyme previously developed. The copper-silver-CALB metalloenzymes have been characterized by X-Ray diffraction analysis, mass spectrometry, and SEM and TEM as microscopies techniques. After that, their catalytic efficiency was tested in different reactions, in particular in the phloridzin oligomerization as laccase-like activity. |
format |
Conference Object |
author |
Ortega-Nieto, Clara Losada-Gracia, Noelia Vukoičić, Ana Milivojević, Ana Bezbradica, Dejan Palomo, Jose M. |
author_facet |
Ortega-Nieto, Clara Losada-Gracia, Noelia Vukoičić, Ana Milivojević, Ana Bezbradica, Dejan Palomo, Jose M. |
author_sort |
Ortega-Nieto, Clara |
title |
NOVEL Cu/Ag-ENZYME BIOHYBRIDS AS ARTIFICIAL METALLOENZYME |
title_short |
NOVEL Cu/Ag-ENZYME BIOHYBRIDS AS ARTIFICIAL METALLOENZYME |
title_full |
NOVEL Cu/Ag-ENZYME BIOHYBRIDS AS ARTIFICIAL METALLOENZYME |
title_fullStr |
NOVEL Cu/Ag-ENZYME BIOHYBRIDS AS ARTIFICIAL METALLOENZYME |
title_full_unstemmed |
NOVEL Cu/Ag-ENZYME BIOHYBRIDS AS ARTIFICIAL METALLOENZYME |
title_sort |
novel cu/ag-enzyme biohybrids as artificial metalloenzyme |
publisher |
Belgrade : University, Faculty of Technology and Metallurgy |
publishDate |
2023 |
url |
http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6959 https://hdl.handle.net/21.15107/rcub_technorep_6959 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Book of Abstracts / International Conference Biochemical Engineering and Biotechnology for Young Scientists, 7-8 December, 2023, Belgrade |
op_relation |
info:eu-repo/grantAgreement/MESTD/inst-2020/200135/RS// info:eu-repo/grantAgreement/MESTD/inst-2020/200287/RS// Horizon Europe 2021-2027 research and innovation programme under grant agreement ID 101060130 (TwinPrebioEnz) 978-86-7401-389-2 http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6959 https://hdl.handle.net/21.15107/rcub_technorep_6959 |
op_rights |
restrictedAccess ARR |
_version_ |
1788067147291820032 |