The nonlinear dependence of the rate expressions associated with enzymecatalysed reactions on the concentration of substrate implies that the corresponding integrated form of the substrate mass balance in a batch reactor cannot be expressed as an explicit function of time..This paper addresses this problem for the classical case of Michaelis—Menten kinetics by providing a self-pacing exploration of the characteristics of a Taylor expansion of the substrate concentration on time. The accuracy of such an approximation is discussed. The procedure presented is appropriate to model situations of technological and practical interest
We re-visit previous analyses of the classical Michaelis-Menten substrate-enzyme reaction and, with ...
We describe a new data-processing method for the kinetic quantification of substrates of enzyme-cata...
The mass action kinetic model of the irreversible Michaelis-Menten reaction mechanism is mathematica...
The use of the classic Henry-Michaelis-Menten (HMM) model (or simply, Michaelis-Menten model) to stu...
The Michaelis-Menten kinetics and the reverse Michaelis-Menten kinetics are two popular mathematical...
The Michaelis-Menten kinetics and the reverse Michaelis-Menten kinetics are two popular mathematical...
The problem of expressing the concentration of each of a set of substrates in a batch reactor as an ...
The rate of product formation is an important measure of the speed of enzyme reactions. Classical st...
The principal aim of studies of enzyme-mediated reactions has been to provide comparative and quanti...
The principal aim of studies of enzyme-mediated reactions has been to provide comparative and quanti...
Michaelis-Menten analysis of the rates of enzymatic reactions as a function of substrate concentrati...
The kinetic performance of enzymes, the catalysts designed by nature to accelerate the chemical reac...
For some time now, there has been growing interest in pre-steady-state (PSS) kinetic parameters for ...
The application of the quasi-steady-state approximation (QSSA) in biochemical kinetics allows the re...
We re-visit previous analyses of the classical Michaelis-Menten substrate-enzyme reaction and, with ...
We re-visit previous analyses of the classical Michaelis-Menten substrate-enzyme reaction and, with ...
We describe a new data-processing method for the kinetic quantification of substrates of enzyme-cata...
The mass action kinetic model of the irreversible Michaelis-Menten reaction mechanism is mathematica...
The use of the classic Henry-Michaelis-Menten (HMM) model (or simply, Michaelis-Menten model) to stu...
The Michaelis-Menten kinetics and the reverse Michaelis-Menten kinetics are two popular mathematical...
The Michaelis-Menten kinetics and the reverse Michaelis-Menten kinetics are two popular mathematical...
The problem of expressing the concentration of each of a set of substrates in a batch reactor as an ...
The rate of product formation is an important measure of the speed of enzyme reactions. Classical st...
The principal aim of studies of enzyme-mediated reactions has been to provide comparative and quanti...
The principal aim of studies of enzyme-mediated reactions has been to provide comparative and quanti...
Michaelis-Menten analysis of the rates of enzymatic reactions as a function of substrate concentrati...
The kinetic performance of enzymes, the catalysts designed by nature to accelerate the chemical reac...
For some time now, there has been growing interest in pre-steady-state (PSS) kinetic parameters for ...
The application of the quasi-steady-state approximation (QSSA) in biochemical kinetics allows the re...
We re-visit previous analyses of the classical Michaelis-Menten substrate-enzyme reaction and, with ...
We re-visit previous analyses of the classical Michaelis-Menten substrate-enzyme reaction and, with ...
We describe a new data-processing method for the kinetic quantification of substrates of enzyme-cata...
The mass action kinetic model of the irreversible Michaelis-Menten reaction mechanism is mathematica...