期刊
FOOD AND CHEMICAL TOXICOLOGY
卷 47, 期 8, 页码 2071-2075出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.fct.2009.05.025
关键词
Trypsin; Melanoidin; Enzyme inhibition; Enzyme activity
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. (C) 2009 Elsevier Ltd. All rights reserved.
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