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...

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Main Authors: Ortega-Nieto, Clara, Losada-Gracia, Noelia, Vukoičić, Ana, Milivojević, Ana, Bezbradica, Dejan, Palomo, Jose M.
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
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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
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