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DIFFERENT POLYPHENOLS HAVE DIFFERENT AFFINITIES FOR C‐TERMINAL SUBUNITS OF MALTASE‐GLUCOAMYLASE AND SUCRASEISOMALTASE FOR THE MODULATION OF GLUCOSE RELEASE
Author(s) -
Simsek Meric,
QuezadaCalvillo Roberto,
Nichols Buford L.,
Hamaker Bruce R.
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.637.33
Subject(s) - chemistry , caffeic acid , maltase , gallic acid , biochemistry , chlorogenic acid , enzyme , gallate , polyphenol , polyphenol oxidase , antioxidant , food science , nuclear chemistry , peroxidase
Some polyphenolic compounds inhibit the intestinal alpha‐glucosidases. However, it is not clear how those compounds affect the enzyme activity of the individual C or N terminals subunits of maltase‐glucoamylase (Mgam) and sucrase‐isomaltase (Si). Objective To modulate the enzymatic activity of the most active C terminal‐Mgam (Ct‐Mgam) and C terminal Si (Ct‐Si) by selected polyphenols in order to control the glucose release from the starch digestion. Methods Maltase activities of recombinant Ct‐Mgam and Ct‐Si subunits were measured by Tris Glucose‐ Oxidase (TGO) method. The reactions were stopped by TGO and the optical density was measured at 450 nm. Results Maltase activity of both enzymes was inhibited. IC 50 values were 0.58 and 0.571 mM for caffeic acid, 0.039 and 0.014 mM chlorogenic acid, 0.139 and 0.213 mM for (+)‐catechin hydrate, 0.383 and 0.177 mM for gallic acid, 0.041 and 0.014 mM for (−) epigallocatechin gallate for Ct‐Si and Ct‐Mgam, respectively. Conclusions The results indicate that the potencies of inhibition of each polyphenol differ against each Ct‐Mgam and Ct‐Si subunits. This opens the possibility for the use of polyphenols as subunit‐specific inhibitors.