Polymers produced by horseradish-peroxidase-catalyzed coupling of phenols have been explored as potential substitutes for phenol-formaldehyde resins. To overcome low substrate solubilities and product molecular weights in water, enzymatic polymerizations in aqueous-organic mixtures have been examine
Kinetics of phenolic polymerization catalyzed by peroxidase in organic media
β Scribed by Dr. Yue-Ping Xu; Guo-Lan Huang; Yao-Ting Yu
- Publisher
- John Wiley and Sons
- Year
- 1995
- Tongue
- English
- Weight
- 274 KB
- Volume
- 47
- Category
- Article
- ISSN
- 0006-3592
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β¦ Synopsis
Phenolic polymerization was carried out by enzymatic catalysis in organic media, and its kinetics was studied by using high-pressure liquid chromatography (HPLC). Phenols and aromatic amines with electron-withdrawing groups could hardly be polymerized by HRP catalysis, but phenols and aromatic amines with electron-donating groups could easily be polymerized. The reaction rate of either the para-substituted substrate or meta-substituted substrate was higher than that of ortho-substituted substrate. When ortho-position of hydroxy group of phenols was occupied by an electron-donating group and if another electron-donating group occupied para-position of hydroxy group, the reaction rate increased. Horseradish peroxidase and lactoperoxidase could easily catalyze the polymerization, but chloroperoxidase and laccase failed to yield polymers. Metallic ions such as Mn2+, Fe2+, or Fe3+, and Cu2+ could poison horseradish peroxidase to various extents, but ions such as Co2+, Cd2+, Zn2+, and K+ were not found to inhibit the reaction.
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## Abstract **Summary:** Peroxidaseβcatalyzed oxidative polymerization of phenol has been examined using the template, poly(ethylene glycol) monododecyl ether (PEGMDE), in water. The role of this template, which forms a complex with phenol in the polymerization, was verified by UV measurements. Dur