Porcine skeletal muscle troponin is a good source of peptides with angiotensin-I converting enzyme inhibitory activity and anti hypertensive effects in spontaneously hypertensive rats

Katayama K., Anggraeni H. E. , Mori T., Ahhmed A. , Kawahara S., SUGIYAMA M., ...More

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, vol.56, no.2, pp.355-360, 2008 (Journal Indexed in SCI) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 56 Issue: 2
  • Publication Date: 2008
  • Doi Number: 10.1021/jf071408j
  • Journal Indexes: Science Citation Index Expanded, Scopus
  • Page Numbers: pp.355-360


In the search for novel peptides that inhibit the angiotensin I-converting enzyme (ACE), porcine skeletal troponin was hydrolyzed with pepsin, and the products were subjected to various types of chromatography to isolate active peptides. Glu-Lys-Glu-Arg-Glu-Arg-Gln (EKERERQ) and Lys-Arg-Gln-Lys-Tyr-Asp-lle (KRQKYDI) were identified as active peptides, and their 50% inhibitory concentrations were found to be 552.5 and 26.2 mu M, respectively. These are novel ACE inhibitory peptides, and the activity of KRQKYDI was the strongest among previously reported troponin-originated peptides. KRQKYDI was slowly hydrolyzed by treatment with ACE, and kinetic studies indicated that this peptide was a competitive inhibitor of the enzyme. When KRQKYDI was administered orally to spontaneously hypertensive rats (SHR) at a dose of 10 mg/kg, a temporary antihypertensive activity was observed at 3 and 6 h after administration.