Production of a novel wheat gluten hydrolysate containing dipeptidyl peptidase-IV inhibitory tripeptides using ginger protease.

Abstract

Wheat gluten is a Pro-rich protein complex comprising glutenins and gliadins. Previous studies have reported that oral intake of enzymatic hydrolysates of gluten has beneficial effects, such as suppression of muscle injury and improvement of hepatitis. Here, we utilized ginger protease that preferentially cleaves peptide bonds with Pro at the P2 position to produce a novel type of wheat gluten hydrolysate. Ginger protease efficiently hydrolyzed gluten, particularly under weak acidic conditions, to peptides with an average molecular weight of <600 Da. In addition, the gluten hydrolysate contained substantial amounts of tripeptides, including Gln-Pro-Gln, Gln-Pro-Gly, Gln-Pro-Phe, Leu-Pro-Gln, and Ser-Pro-Gln (e.g. 40.7 mg/g at pH 5.2). These gluten-derived tripeptides showed high inhibitory activity on dipeptidyl peptidase-IV with IC50 values of 79.8, 70.9, 71.7, 56.7, and 78.9 μM, respectively, suggesting that the novel gluten hydrolysate prepared using ginger protease can be used as a functional food for patients with type 2 diabetes.

• Authors: Yuki Taga, Osamu Hayashida, Masashi Kusubata, Kiyoko Ogawa-Goto, Shunji Hattori
• Journal: Bioscience, biotechnology, and biochemistry (Biosci Biotechnol Biochem) Vol. 81 Issue 9 Pg. 1823-1828 (Sep 2017) ISSN: 1347-6947 [Electronic] England
• PMID: 28675098 (Publication Type: Journal Article)

Chemical References

• Dipeptidyl-Peptidase IV Inhibitors
• Oligopeptides
• Glutens
• Peptide Hydrolases
• Dipeptidyl Peptidase 4

Topics

• Dipeptidyl Peptidase 4 (metabolism)
• Dipeptidyl-Peptidase IV Inhibitors (metabolism)
• Ginger (enzymology)
• Glutens (metabolism)
• Hydrogen-Ion Concentration
• Hydrolysis
• Oligopeptides (metabolism)
• Peptide Hydrolases (metabolism)
• Substrate Specificity
• Triticum (chemistry)