Potential of Quantitative α‑Amylase or Trypsin Inhibition by Refined and Whole Wheat and Einkorn Using High-Performance Thin-Layer Chromatography–NanoGIT versus Conventional Spectrophotometry
Isabel Müller, Ilka Scheibelhut, Gertrud E. Morlock
TL;DR
This study compares the inhibition of enzymes by different wheat types using a new method that combines chromatography and nanoGIT assays.
Contribution
The novel HPTLC–nanoGIT workflows provide detailed insights into enzyme inhibition and metabolite profiles.
Findings
Einkorn showed lower α-amylase inhibition compared to refined and whole wheat.
High extract concentrations of all cereals showed 100% trypsin inhibition.
The new method revealed specific interactions and metabolite profiles not detectable by conventional methods.
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…
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Taxonomy
TopicsEnzyme Production and Characterization · Protein Interaction Studies and Fluorescence Analysis · Food composition and properties