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 N alpha-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 alpha K(i) of the substrate-inhibitor complex is higher than the inhibition constant K(i) of the complex enzyme-inhibitor with a alpha value of 1.88.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1016/j.fct.2009.05.025 | DOI Listing |
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!