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Flowerlike hybrid horseradish peroxidase nanobiocatalyst for the polymerization of guaiacol

In this study, the catalytic activity and stability of flowerlike hybrid horseradish peroxidase (HRP) nanobiocatalyst (HRP-Cu (2+) ) obtained from Cu (2+) ions and HRP enzyme in the polymerization reaction of guaiacol were analyzed. We demonstrated that HRP-Cu (2+) and hydrogen peroxide (H (2) O (2)...

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Autor principal: GÖKTÜRK, Ersen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Scientific and Technological Research Council of Turkey 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7751901/
https://www.ncbi.nlm.nih.gov/pubmed/33488229
http://dx.doi.org/10.3906/kim-2005-32
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author GÖKTÜRK, Ersen
author_facet GÖKTÜRK, Ersen
author_sort GÖKTÜRK, Ersen
collection PubMed
description In this study, the catalytic activity and stability of flowerlike hybrid horseradish peroxidase (HRP) nanobiocatalyst (HRP-Cu (2+) ) obtained from Cu (2+) ions and HRP enzyme in the polymerization reaction of guaiacol were analyzed. We demonstrated that HRP-Cu (2+) and hydrogen peroxide (H (2) O (2) ) initiator showed significantly increased catalytic activity and stability on the polymerization of guaiacol compared to that of free HRP enzyme. Poly(guaiacol) was observed with quite high yields (88%) and molecular weights (38,000 g/mol) under pH 7.4 phosphate-buffered saline (PBS) conditions at 60 °C with 5 weight% of HRP-Cu (2+) loading. HRP-Cu (2+) also shows very high thermal stability and works even at 70 °C reaction temperature; free HRP enzyme denatures at that temperature. Furthermore, HRP-Cu (2+) provided considerable repeated use and showed some degree of catalytic activity, even after the fourth recycle, in the polymerization of guaiacol.
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spelling pubmed-77519012021-01-22 Flowerlike hybrid horseradish peroxidase nanobiocatalyst for the polymerization of guaiacol GÖKTÜRK, Ersen Turk J Chem Article In this study, the catalytic activity and stability of flowerlike hybrid horseradish peroxidase (HRP) nanobiocatalyst (HRP-Cu (2+) ) obtained from Cu (2+) ions and HRP enzyme in the polymerization reaction of guaiacol were analyzed. We demonstrated that HRP-Cu (2+) and hydrogen peroxide (H (2) O (2) ) initiator showed significantly increased catalytic activity and stability on the polymerization of guaiacol compared to that of free HRP enzyme. Poly(guaiacol) was observed with quite high yields (88%) and molecular weights (38,000 g/mol) under pH 7.4 phosphate-buffered saline (PBS) conditions at 60 °C with 5 weight% of HRP-Cu (2+) loading. HRP-Cu (2+) also shows very high thermal stability and works even at 70 °C reaction temperature; free HRP enzyme denatures at that temperature. Furthermore, HRP-Cu (2+) provided considerable repeated use and showed some degree of catalytic activity, even after the fourth recycle, in the polymerization of guaiacol. The Scientific and Technological Research Council of Turkey 2020-10-26 /pmc/articles/PMC7751901/ /pubmed/33488229 http://dx.doi.org/10.3906/kim-2005-32 Text en Copyright © 2020 The Author(s) This article is distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/4.0/ ), which permits unrestricted use and redistribution provided that the original author and source are credited.
spellingShingle Article
GÖKTÜRK, Ersen
Flowerlike hybrid horseradish peroxidase nanobiocatalyst for the polymerization of guaiacol
title Flowerlike hybrid horseradish peroxidase nanobiocatalyst for the polymerization of guaiacol
title_full Flowerlike hybrid horseradish peroxidase nanobiocatalyst for the polymerization of guaiacol
title_fullStr Flowerlike hybrid horseradish peroxidase nanobiocatalyst for the polymerization of guaiacol
title_full_unstemmed Flowerlike hybrid horseradish peroxidase nanobiocatalyst for the polymerization of guaiacol
title_short Flowerlike hybrid horseradish peroxidase nanobiocatalyst for the polymerization of guaiacol
title_sort flowerlike hybrid horseradish peroxidase nanobiocatalyst for the polymerization of guaiacol
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7751901/
https://www.ncbi.nlm.nih.gov/pubmed/33488229
http://dx.doi.org/10.3906/kim-2005-32
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