Peroxidase/H2O2 Catalyzed Oxidative Oligomerization of 1-Aminopyrene
A new florescent oligo(aminopyrene) (OAP) was successfully synthesized by enzymatic approach. For this, H2O2 and Horse Radish peroxidase (HRP) were used as catalyst and oxidant, respectively. The structures of monomer and oxidation product were confirmed by NMR, FT-IR and UV-Vis measurements. The oxidation product was characterized by gel permeation chromatography (GPC), thermogravimetry (TG), differential scanning calorimetry (DSC), cyclic voltammetry (CV), photoluminescence (PL) and scanning electron microscopy (SEM) analyses. OAP was soluble in a wide range of organic solvents. UV-Vis spectrum of the OAP showed a dramatic red shift compared to that of the monomer. The optical and electrochemical band gaps of OAP were found to be 1.65 and 1.56 eV, respectively. OAP emitted turquoise color in THF and green color in toluene. SEM observations indicated the presence of a heterogeneous cauliflower like morphology.
I. Kaya et al., "Peroxidase/H2O2 Catalyzed Oxidative Oligomerization of 1-Aminopyrene," Journal of Macromolecular Science, Part A: Pure and Applied Chemistry, vol. 54, no. 4, pp. 243-248, Taylor and Francis Inc., Apr 2017.
The definitive version is available at http://dx.doi.org/10.1080/10601325.2017.1282698
Materials Science and Engineering
Keywords and Phrases
Differential scanning calorimetry; Energy gap; Gel permeation chromatography; Monomers; Photoluminescence; Polymerization; Scanning electron microscopy; Thermogravimetric analysis; 1-Aminopyrene; Enzymatic Polymerization; Gel permeation chromatography (GPC); Horse-radish peroxidase; Oxidation products; Oxidative polymerization; SEM observation; UV-Vis spectrum; Cyclic voltammetry
International Standard Serial Number (ISSN)
Article - Journal
© 2017 Taylor and Francis Inc., All rights reserved.