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Updated: Jan 19, 2026

Author Spotlight: Eco-Friendly Extraction of Bioactive Compounds Using Polyol-Based Microwave-Assisted Techniques
Published on: August 23, 2024
Interaction of Structurally Diverse Phenolic Compounds with Porcine Pancreatic α-Amylase
Julia A H Kaeswurm1, Birgit Claasen2, Max-Philipp Fischer3
1Department of Food Chemistry, Institute of Biochemistry and Technical Biochemistry , University of Stuttgart , Allmandring 5b , 70569 Stuttgart , Germany.
Abstract:
A blood glucose level lowering effect is postulated for polyphenols (PPs), which is in part attributed to the inhibition of α-amylase. To estimate structure-effect relationships, chlorogenic acid (CA), phlorizin (PHL), epigallocatechin gallate (EGCG), epicatechin (EC), and malvidin-3-glucoside (Mlv-3-glc) were used as inhibitors in an enzyme assay, on the basis of the conversion of GalG2CNP by α-amylase. The detection of CNP was performed by UV/vis spectroscopy. The data reveal that the inhibitor strength decreases as follows: EGCG > Mlv-3-glc > EC > PHL ∼ CA. Detection of the substrate conversion by isothermal titration calorimetry supports these results. All PPs showed mixed inhibition, except for CA and EGCG wherein the competitive proportion was predominant. Investigations by saturation transfer difference NMR revealed interaction of PPs with α-amylase prevalently based on interactions with the aromatic or conjugated system. A correlation between the extent of the conjugated system and the IC50 of the PP could be found.
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