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Numerical and Monte Carlo simulations of phenolic polymerizations catalyzed by peroxidase
Author(s) -
Ryu Keungarp,
McEldoon James P.,
Pokora Alexander R.,
Cyrus William,
Dordick Jonathan S.
Publication year - 1993
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260420704
Subject(s) - chemistry , polymerization , horseradish peroxidase , reaction rate constant , phenols , dispersity , reactivity (psychology) , radical polymerization , catalysis , substituent , peroxidase , photochemistry , organic chemistry , kinetics , enzyme , polymer , medicine , physics , alternative medicine , pathology , quantum mechanics
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.