Antihypertensive peptides derived from milk proteins

Nahrung. 1999 Jun;43(3):159-64. doi: 10.1002/(SICI)1521-3803(19990601)43:3<159::AID-FOOD159>3.0.CO;2-R.


This paper reviews the angiotensin I-converting enzyme inhibitory peptides originated from milk proteins. Focus was put on the peptides derived from milk casein by the action of some proteolytic enzymes and fermented products by lactic acid bacteria. Some of the angiotensin I-converting enzyme inhibitory peptides exhibit significant antihypertensive effects in spontaneously hypertensive rats. However, there were some antihypertensive peptides with low inhibitory activity of this enzyme. Key factors needed for the peptide to demonstrate the antihypertensive effects are discussed. Fermented milk, which has inhibitory activity of the enzyme, showed the reduction of blood pressure of hypertensive subjects. The possibility of the bioactive peptides for functional foods are also discussed.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Angiotensin-Converting Enzyme Inhibitors / chemistry*
  • Angiotensin-Converting Enzyme Inhibitors / pharmacology*
  • Animals
  • Antihypertensive Agents / chemistry*
  • Antihypertensive Agents / pharmacology*
  • Humans
  • Milk Proteins / chemistry*
  • Milk Proteins / pharmacology*
  • Molecular Sequence Data
  • Peptides / chemistry
  • Peptides / isolation & purification
  • Rats
  • Rats, Inbred SHR


  • Angiotensin-Converting Enzyme Inhibitors
  • Antihypertensive Agents
  • Milk Proteins
  • Peptides