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The value of Km (Michaelis Menten constant) was evaluated to be 4.38 gL−1.
Study of kinetic parameters (Km, Vmax) revealed the value of Km for covalently immobilized uricase to be ∼1.2-fold higher than that of free enzyme.
Laccase in 1 2 and 1 5 T P ratios had 83 and 100 mM value of Km respectively as compared to 33 mM for free laccase.
Fig. 4 Time evolutions of (defined by Eq. (18)) for the constant value of km and various values of yr (dotted line), yr (solid line), and yr (dashed line).
The low value of Km indicated that BCJ2315 had high affinity toward mandelonitrile.
In this notation, the larger diffusion restriction would lead to the larger value of Km(ADP).
The lowest value of KM was obtained for the enzyme covalently bound to the carboxyl groups of the polymer.
Km is a measure of the binding affinity between the enzyme and the substrate, and a lower value of Km indicates a higher affinity.
The lower value of Km and higher Vmax values for immobilized enzyme indicated that immobilization enhanced the substrate affinity and catalytic efficiency of LiP.
The lower value of Km observed for TrCrtC shows that this enzyme presents higher affinity for the substrate lycopene than RgCrtC.
There are amino acids uniquely involved in acetyl-CoA binding, for which there is a change of only the value of Km,app-acetyl-CoA upon mutation.
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CEO of Professional Science Editing for Scientists @ prosciediting.com