Antidiabetic bio-peptides of soft and hard wheat glutens

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(m) (0.04 ± 0.002 mM), K(cat)/K(m) (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(w) 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.