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Action of lipolytical enzymes in biphasic organic‐aqueous systems: Dynamics of the irreversible Michaelis–Menten reaction
Author(s) -
Tsai ShauWei,
Wei HwaJou,
Chiang ChenLi
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.260410602
Subject(s) - chemistry , michaelis–menten kinetics , aqueous solution , steady state (chemistry) , thermodynamics , action (physics) , enzyme , substrate (aquarium) , kinetic energy , computational chemistry , stereochemistry , biochemistry , enzyme assay , physics , classical mechanics , ecology , biology , quantum mechanics
Through simple model analysis, the mass action kinetic model for lipolytic enzymes in biphasic aqueous‐organic systems can be simplified using the quasi–steady state assumption (or the quasi–equilibrium state assumption) for the adsorbed enzyme E * or the enzyme–substrate complex E * S . Some parameter combinations leading to the above assumptions are derived confirmed by full numerical integration of the whole enzymatic process. The results may be classified into three categories: (1) the quasi–equilibrium state assumption for E *, (2) the quasi–steady state assumption for E *, and (3) the quasi–steady state assumption for E * S . Further simplification for both E * and E * S is also discussed. © 1993 Wiley & Sons, Inc.