Production of dipeptidyl peptidase IV inhibitory peptides from defatted rice bran.

Food Chem

Okayama Prefectural Technology Center for Agriculture, Forestry, and Fisheries, Research Institute for Biological Sciences (RIBS), Okayama, 7549-1 Kibichuo-cho, Kaga-gun, Okayama 716-1241, Japan.

Published: September 2012

AI Article Synopsis

  • The hormone glucagon-like peptide-1 is quickly broken down by the enzyme DPP-IV, which plays a crucial role in managing type 2 diabetes.
  • Researchers focused on rice bran (RB) to create peptides that inhibit DPP-IV, finding that those produced with the enzyme Umamizyme G were significantly more effective than those from Bioprase SP.
  • Among the identified inhibitory peptides, Ile-Pro was the strongest, showing competitive inhibition of DPP-IV with a specific concentration value and making it a promising candidate for diabetes treatment.

Article Abstract

The insulinotropic hormone glucagon-like peptide-1 is metabolised extremely rapidly by the ubiquitous enzyme dipeptidyl peptidase IV (DPP-IV). Therefore, human DPP-IV is a key regulator involved in the prevention and treatment of type 2 diabetes. To simplify the method of producing an inhibitory peptide against DPP-IV, we focused on rice bran (RB) as a source and subjected proteins from defatted RB to enzymatic proteolysis using 2 commercial enzymes. The RB peptides produced with Umamizyme G exhibited 10 times the inhibitory activity as those produced with Bioprase SP. The half-maximal inhibitory concentration (IC(50)) value of the RB peptides was 2.3 ± 0.1mg/ml. Leu-Pro and Ile-Pro were identified as the inhibitory peptides among the RB peptides produced with Umamizyme G. Ile-Pro was the strongest DPP-IV inhibitor among the 15 Xaa-Pro dipeptides and Pro-Ile tested. Ile-Pro competitively inhibited DPP-IV (K(i)=0.11 mM). Mass spectrometry indicated that the contents of Leu-Pro and Ile-Pro in the RB peptides were 2.91 ± 0.52 μg/mg.

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http://dx.doi.org/10.1016/j.foodchem.2012.02.183DOI Listing

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