The kinetic parameters of the Michaelis-Menten equation
(Equation 4) were determined by varying the olive oil concentration from 1 to 70% in the enzymatic hydrolysis reaction.
The film kinetics were characterized using the simplest and most common approach which consists in using the Michaelis-Menten equation
From linear plots of the Michaelis-Menten equation
such as Lineweaver-Burk or Hanes-Woolf plot using an Excel curve-fitting program (Microsoft Excel 2010, San Francisco, CA, USA), kinetic parameters, [K.
Frontal analysis made it possible to treat chromatography as a saturation phenomenon and express the phenomenon by a simple equation equivalent to the Langmuir's adsorption isotherm and also to the Michaelis-Menten equation
In order to analyze the efficiency of the enzyme catalysis, the substrate specificity was determined through enzyme kinetics utilizing Michaelis-Menten equation
Then, for each trial, the initial velocity of ClpB was plotted versus the final concentration of ATP; and the data set was fit using nonlinear regression according to the Michaelis-Menten equation
1] , which can be described with the Michaelis-Menten equation
with competitive product inhibition by galactose .
A revered textbook formula that describes how these crucial molecular catalysts speed up reactions, the Michaelis-Menten equation
, assumes that enzymes don't usually get stuck in traffic.
To obtain an objectively derived P critical threshold with standard errors for maximum growth rate, we fitted a Michaelis-Menten equation
to the relative growth rate as a function of [P.
The accurate fit of the data to the Michaelis-Menten equation
provides a good test for the simple apparatus used.
The mean rate of conversion was plotted vs the mean substrate concentration at the chosen time interval (20), and the results were directly fitted to the Michaelis-Menten equation
A good place to start looking at kinetics is the classic enzyme kinetics described by the Michaelis-Menten equation