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

Küçük Resim Yok

Tarih

2017

Dergi Başlığı

Dergi ISSN

Cilt Başlığı

Yayıncı

ELSEVIER SCIENCE BV

Erişim Hakkı

info:eu-repo/semantics/openAccess

Özet

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.

Açıklama

Anahtar Kelimeler

Horseradish peroxidase, Enzymatic polymerization, Hydrogen peroxide, Imine functionality, Phenol

Kaynak

JOURNAL OF SAUDI CHEMICAL SOCIETY

WoS Q Değeri

Q2

Scopus Q Değeri

Q1

Cilt

21

Sayı

6

Künye