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Received March 29, 2004
Accepted May 31, 2004
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Determination of Multiple Steady States in Oxidation of Monophenols by Tyrosinase with Enzymatic-Enzymatic-Chemical Model
Department of Chemical Engineering, National United University, Miao-Li 360, Taiwan
chuang@nuu.edu.tw
Korean Journal of Chemical Engineering, September 2004, 21(5), 963-969(7), 10.1007/BF02705578
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Abstract
A family of an enzymatically catalyzed reaction network is studied, which involves the oxidation of monophenols by tyrosinase with enzymatic-enzymatic-chemical model in an isothermal continuous flow stirred tank reacor(CFSTR). This system consists of 11 coupled non-linear equations and is determined to have the capacity to The phenomena of bistability, hysteresis and bifurcation are discussed. Moreover, the capacity of steady state multiplicity is extended to its family of reaction networks.
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