Horseradish peroxidase-catalyzed polymerization of ortho-imino-phenol: Synthesis, characterization, thermal stability and electrochemical properties

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dc.authoridGokturk, ersen/0000-0001-6742-2847
dc.authoridSahmetlioglu, Ertugrul/0000-0002-7324-0385
dc.contributor.authorTopal, Yasemin
dc.contributor.authorTapan, Senem
dc.contributor.authorGokturk, Ersen
dc.contributor.authorSahmetlioglu, Ertugrul
dc.date.accessioned2024-09-18T20:26:49Z
dc.date.available2024-09-18T20:26:49Z
dc.date.issued2017
dc.departmentHatay Mustafa Kemal Üniversitesien_US
dc.description.abstractEnzymatic polymerization of phenols has been investigated extensively over the last decades. However, involving imine functional group in the side chain of an oligophenol and its effect on polymerization is poorly understood. Therefore, the influence of the imine functionality in the side chain of oligophenol for enzymatic polymerization is explored in this work. Ortho-imine substituted phenol, (E)-2-((p-tolylimino) methyl) phenol (PTIMP), was enzymatically polymerized using horseradish peroxidase (HRP) enzyme in aqueous organic solvents and hydrogen peroxide (H2O2) as an oxidant. Different parameters (solvent system, pH and reaction temperature) on polymerization were investigated. EtOH/pH 6.0 buffer (50: 50 vol.%) at 25 degrees C in 24 h under air was found to be the optimum polymerization condition with 65% of yield and Mn = 6100 g/mol (DP approximate to 29, PDI = 1.09). Polymerization of PTIMP in the presence of HRP enzyme catalyst leads to the formation of an oligophenol containing phenylene and oxyphenylene repeat units. The resulting oligophenol is soluble in most of the organic solvents. Characterization of oligo(PTIMP) was achieved by NMR, UV-Vis, CV, FT-IR spectroscopy and thermogravimetric analysis. (C) 2017 King Saud University. Production and hosting by Elsevier B. V. This is an open access article under the CC BY-NC-ND license.en_US
dc.description.sponsorshipscientific research fund of Erciyes University - Turkey [FBA-2016-6611]en_US
dc.description.sponsorshipThis research was supported by scientific research fund of Erciyes University - Turkey (FBA-2016-6611). We would also like to thank retired Prof. Dr. Huseyin Yuruk for sharing his valuable comments with us during the research.en_US
dc.identifier.doi10.1016/j.jscs.2017.03.006
dc.identifier.endpage740en_US
dc.identifier.issn1319-6103
dc.identifier.issn2212-4640
dc.identifier.issue6en_US
dc.identifier.scopus2-s2.0-85017242625en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage731en_US
dc.identifier.urihttps://doi.org/10.1016/j.jscs.2017.03.006
dc.identifier.urihttps://hdl.handle.net/20.500.12483/10547
dc.identifier.volume21en_US
dc.identifier.wosWOS:000414214000012en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherElsevier Science Bven_US
dc.relation.ispartofJournal of Saudi Chemical Societyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectHorseradish peroxidaseen_US
dc.subjectEnzymatic polymerizationen_US
dc.subjectHydrogen peroxideen_US
dc.subjectImine functionalityen_US
dc.subjectPhenolen_US
dc.titleHorseradish peroxidase-catalyzed polymerization of ortho-imino-phenol: Synthesis, characterization, thermal stability and electrochemical propertiesen_US
dc.typeArticleen_US

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