Kinetics of phenolic polymerization catalyzed by peroxidase in organic media
- 5 July 1995
- journal article
- other
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 47 (1) , 117-119
- https://doi.org/10.1002/bit.260470114
Abstract
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. © 1995 John Wiley & Sons, Inc.Keywords
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