Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2586083 | Food and Chemical Toxicology | 2009 | 5 Pages |
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 αKi of the substrate–inhibitor complex is higher than the inhibition constant Ki of the complex enzyme–inhibitor with a α value of 1.88.
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Authors
Albert Ibarz, Alfonso Garvín, Salvador Garza, Jordi Pagán,