Peptides derived from atlantic salmon skin gelatin as dipeptidyl-peptidase IV inhibitors

J Agric Food Chem. 2012 Feb 1;60(4):973-8. doi: 10.1021/jf204720q. Epub 2012 Jan 20.

Abstract

The dipeptidyl-peptidase IV (DPP-IV)-inhibitory activity of peptides derived from Atlantic salmon skin gelatin hydrolyzed by alcalase (ALA), bromelain (BRO), and Flavourzyme (FLA) was determined. The FLA hydrolysate with the enzyme/substrate ratio of 6% showed the greatest DPP-IV-inhibitory activity. The hydrolysate was fractionated by ultrafiltration with 1 and 2.5 kDa cutoff membranes, and the <1 kDa fraction had the highest DPP-IV-inhibitory activity with an IC(50) value of 1.35 mg/mL. The F-1 fraction further isolated by HPLC showed the IC(50) value against DPP-IV of 57.3 μg/mL, and the peptide sequences were identified as Gly-Pro-Ala-Glu (372.4 Da) and Gly-Pro-Gly-Ala (300.4 Da). The synthetic peptides showed dose-dependent inhibition effects on DPP-IV with IC(50) values of 49.6 and 41.9 μM, respectively. The results suggest that the peptides derived from Atlantic salmon skin gelatin would be beneficial ingredients for functional foods or pharmaceuticals against type 2 diabetes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bromelains / metabolism
  • Dipeptidyl-Peptidase IV Inhibitors / chemistry
  • Dipeptidyl-Peptidase IV Inhibitors / isolation & purification*
  • Dipeptidyl-Peptidase IV Inhibitors / pharmacology
  • Endopeptidases / metabolism
  • Gelatin / chemistry*
  • Hydrolysis
  • Peptides / chemistry
  • Peptides / isolation & purification*
  • Peptides / pharmacology*
  • Salmo salar*
  • Skin / chemistry*
  • Subtilisins / metabolism

Substances

  • Dipeptidyl-Peptidase IV Inhibitors
  • Peptides
  • Gelatin
  • Bromelains
  • Endopeptidases
  • flavourzyme
  • Subtilisins