Synthesis, characterization, thermal stability and electrochemical properties of ortho-imine-functionalized oligophenol via enzymatic oxidative polycondensation
Küçük Resim Yok
Tarih
2016
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
SPRINGER
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
Ortho-imine functionalized oligophenol was synthesized via enzymatic polymerization of 2-((4-nitrophenylimino) methyl) phenol (NPIMP). Enzymatic polymerization was catalyzed by Horseradish peroxidase (HRP) enzyme and hydrogen peroxide (H2O2) oxidizer yielded oligophenol with imine functionality on the side-chain. Effects of various factors including reaction pH, temperature and solvent system on the polymerization were studied. Optimum polymerization with the highest yield (96 %) and number-average molecular weight (M-n = 7300 g/mol, degree of polymerization approximate to 30) was accomplished using equivolume mixture of acetone/pH 7.0 phosphate buffer medium at 35 degrees C in 24 h under air. Characterization of the resulting oligomer was accomplished by ultraviolet-visible spectroscopy (UV-Vis), fourier transform infrared spectroscopy (FT-IR), H-1 and C-13 nuclear magnetic resonance (H-1 and C-13 NMR), thermogravimetric analysis (TGA), differential scanning calorimetry (DSC), cyclic voltammetry (CV) and gel permeation chromatography (GPC). The polymerization involved elimination of hydrogen from NPIMP, and the oligomer possessed phenolic -OH end groups. The oligomer backbone was composed of oxyphenylene and phenylene repeat units. The optical band gaps (Eg) of NPIMP and oligo(NPIMP) were measured as 3.21 and 3.39 Eg, respectively. Thermal stability of the oligo(NPIMP) was also found to be relatively high, and lost 5 % of its mass at 175 degrees C and lost 50 % of its mass at 600 degrees C.
Açıklama
Anahtar Kelimeler
Phenol, Enzymatic polymerization, Horseradish peroxidase (HRP) enzyme, Oligophenol, pH, Hydrogen peroxide
Kaynak
JOURNAL OF POLYMER RESEARCH
WoS Q Değeri
Q2
Scopus Q Değeri
Q2
Cilt
23
Sayı
3
