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


Topal Y., Tapan S. , Gokturk E., Sahmetlioglu E.

JOURNAL OF SAUDI CHEMICAL SOCIETY, vol.21, no.6, pp.731-740, 2017 (Journal Indexed in SCI) identifier identifier

  • Publication Type: Article / Article
  • Volume: 21 Issue: 6
  • Publication Date: 2017
  • Doi Number: 10.1016/j.jscs.2017.03.006
  • Title of Journal : JOURNAL OF SAUDI CHEMICAL SOCIETY
  • Page Numbers: pp.731-740

Abstract

Enzymatic 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.