Abstract
In this work the effect of the presence of the melanoidins from glucose–asparagine on the enzymatic activity of trypsin is studied. It was observed that an excess of Nα-benzoyl- l-arginine ethyl ester (BAEE) has an inhibiting effect on this enzyme activity. The maximum reaction rate was obtained for a 0.06 mN substrate concentration. It is also observed that the presence of melanoidin inhibits the enzymatic activity of trypsin. This inhibition can be described as a linear mixed type where the inhibition constant αK i of the substrate–inhibitor complex is higher than the inhibition constant K i of the complex enzyme–inhibitor with a α value of 1.88.
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