Kinetics of phenolic polymerization catalyzed by peroxidase in organic media
- Nankai Univ., Tianjin (China). Inst. for Molecular Biology
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 by 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 Mn{sup 2+}, Fe{sup 2+}, or Fe{sup 3+}, and Cu{sup 2+} could poison horseradish peroxidase to various extents, but ions such as Co{sup 2+}, Cd{sup 2+}, Zn{sup 2+}, and K{sup +} were not found to inhibit the reaction.
- Sponsoring Organization:
- USDOE
- OSTI ID:
- 78140
- Journal Information:
- Biotechnology and Bioengineering, Journal Name: Biotechnology and Bioengineering Journal Issue: 1 Vol. 47; ISSN BIBIAU; ISSN 0006-3592
- Country of Publication:
- United States
- Language:
- English
Similar Records
Hammett rho sigma correlation for reactions of horseradish peroxidase compound II with phenols
Polymerization of phenols catalyzed by peroxidase in nonaqueous media