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Updated: Sep 25, 2025

Author Spotlight: Integrating Biochemical Functions of β-Glucanases and Peroxidase Enzymes in Wheat-RWA Interaction
Published on: July 26, 2024
Antidiabetic bio-peptides of soft and hard wheat glutens
Babak Mousavi1, Mohammad-Hossein Azizi1, Soleiman Abbasi1
1Department of Food Science & Technology, Faculty of Agriculture, Tarbiat Modares University, P.O. Box 14115-336, Tehran, Iran.
Abstract:
The effects of various purification techniques on kiwifruit enzyme characteristics (protease activity, kinetic parameters, and protein patterns) and production of wheat gluten bio-active peptides were investigated. The enzyme extract purified by ammonium sulfate precipitation method exhibited the highest protease activity (26), K (0.04 ± 0.002 mM), K /K (40), and yield (96%). Using actinidin, the hard and soft wheat gluten subunit proteins produced antidiabetic inhibitory (α-glucosidase and α-amylase) peptides. The smallest M fraction of soft wheat gliadin peptide (<1 kDa) showed the highest inhibitory capacity against α-glucosidase (18.4 ± 0.7%) and α-amylase (53.3 ± 1.9%). The presence of high levels of amino acids with hydroxyl groups and proline in P3 sub-fraction had a critical role on α-glucosidase (47.2%) and α-amylase (71.2%) inhibitory activities. In conclusion, wheat gluten subunit peptides showed significant metabolic effects relevant to glucose and insulin control in vitro.
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