Determination of multiple steady states in oxidation of monophenols by tyrosinase with enzymatic-enzymatic-chemical model

Autor:	An-Chong Chao, Guo-Syong Chuang, Hsing-Ya Li
Rok vydání:	2004
Předmět:	Hysteresis Reaction rate constant Bistability Chemistry Quantitative Biology::Molecular Networks General Chemical Engineering Tyrosinase Thermodynamics Continuous stirred-tank reactor General Chemistry Bifurcation Isothermal process Catalysis
Zdroj:	Korean Journal of Chemical Engineering. 21:963-969
ISSN:	1975-7220 0256-1115
DOI:	10.1007/bf02705578
Popis:	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 reactor (CFSTR). This system consists of 11 coupled non-linear equations and is determined to have the capacity to exhibit computational multiple steady states. A set of rate constants and two corresponding steady states are computed. The phenomena of bistability, hysteresis and bifurcation are discussed. Moreover, the capacity of steady state multiplicity is extended to its family of reaction networks.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::109a8968c0b65ff226ef7c5c05477ee5 https://doi.org/10.1007/bf02705578 Zobrazit plný text záznamu Full text from SpringerLink