Numerical and Monte Carlo simulations of phenolic polymerizations catalyzed by peroxidase

Keungarp Ryu, James P. McEldoon, Alexander R. Pokora, William Cyrus, Jonathan S. Dordick

Research output: Contribution to journalArticlepeer-review

59 Scopus citations

Abstract

Numerical and Monte Carlo simulations of horseradish peroxidase–catalyzed phenolic polymerizations have been performed. Kinetic constants for the simulations were fit to data from the oxidation and polymerization of bisphenol A. Simulations of peroxidase‐catalyzed phenolic polymerization were run as a function of enzyme concentration and radical transfer and radical coupling rate constants. Predictions were performed with respect to conversion vs. time and number average molecular weight and polydispersity vs. conversion. It is shown that the enzymatic polymerization of phenols can be optimized with respect to high molecular weights by employing low enzyme concentrations and phenols with low radical coupling rate constants coupled with relatively high radical transfer rate constants. Such phenols may be identified by using linear free energy relationships that relate radical reactivity to electron donating/withdrawing potential of the phenolic substituent. © 1993 John Wiley & Sons, Inc.

Original languageEnglish
Pages (from-to)807-814
Number of pages8
JournalBiotechnology and Bioengineering
Volume42
Issue number7
DOIs
StatePublished - 20 Sep 1993
Externally publishedYes

Keywords

  • Monte‐Carlo simulations
  • numerical modeling
  • peroxidase‐catalyzed polymerizations

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