Potencial de inhibición cuantitativa de α-amilasa o tripsina por trigo refinado, integral y einkorn utilizando cromatografía de capa fina de alto rendimiento-nanoGIT frente a espectrofotometría convencional
Video Experimental Relacionado
Updated: Feb 22, 2026
Qualitative and Quantitative Assays for Detection and Characterization of Protein Antimicrobials
Published on: April 10, 2016
Isabel Müller1, Ilka Scheibelhut1, Gertrud E Morlock1
1Chair of Food Science, Institute of Nutritional Science, and Interdisciplinary Research Centre for Biosystems, Land Use and Nutrition, Justus Liebig University Giessen, Heinrich-Buff-Ring 26-32, 35392 Giessen, Germany.
Abstract:
The current analysis of α-amylase/trypsin inhibitors (ATIs) is complicated due to the missing link between inhibition potential and inhibitors. Two on-surface assays (nanoGIT) were developed to quantify the inhibition of α-amylase and trypsin by flour extracts of refined wheat, whole wheat, and einkorn, followed by direct analysis (on the same surface) of the metabolisation products via high-performance thin-layer chromatography (HPTLC). The HPTLC-nanoGIT (amylolysis inhibition)-FLD/Vis revealed a lower α-amylase inhibition of einkorn than refined or whole wheat, whereby both latter wheat types showed no differences. The HPTLC-nanoGIT (proteolysis inhibition)-Vis confirmed only partially the 100% inhibition at high extract concentrations of the three cereal types obtained by the spectrophotometric trypsin inhibition assay. The HPTLC-nanoGIT workflows not only confirmed the inhibitory effects obtained by spectrophotometric assays but also provided substantial resolution of saccharide-specific interactions and specific profile patterns of the released individual metabolisation products.
