Structural analysis of a new anti-hypertensive peptide (β-lactosin B) isolated from a commercial whey product

M. Murakami, H. Tonouchi, R. Takahashi, H. Kitazawa, Y. Kawai, H. Negishi, T. Saito

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78 Citations (Scopus)


Angiotensin-converting enzyme (ACE) inhibitory activities and anti-hypertensive activities in spontaneously hypertensive rats (SHR) of 12 kinds of commercial peptides of food additive grade were measured. Four peptide products derived from milk proteins showed strong anti-hypertensive activities (>-18.0 mm Hg). A sample of WE80BG derived from whey proteins showed the strongest anti-hypertensive activity (-21.2 ± 16.9 mm Hg) with a medium level of ACE inhibitory activity (53.6%), and it was subjected to hydrophobic and gel filtration chromatography. From the low molecular weight fraction, an anti-hypertensive peptide was isolated by using reversed-phase HPLC, and it was found to be a tetrapeptide, alanine-leucine-proline-methionine (Ala-Leu-Pro-Met, ALPM), the origin of which was estimated to be β-lactoglobulin f 142 to 145. At 8 h after oral administration of ALPM in SHR, systolic blood pressure was significantly decreased (-21.4 ± 7.8 mm Hg), but the IC50 value (concentration of peptide needed to inhibit 50% of the ACE activity) of ALPM was not so high. We named the Ala-Leu-Pro-Met "β-lactosin B." This peptide is the second anti-hypertensive peptide found from β-lactoglobulin. Because WE80BG containing ALPM was also found to show the strongest anti-hypertensive activity (-24.5 ± 10 mm Hg) at 8 h after oral administration in SHR, WE80BG would be suitable for application to the development of a new food expected to have anti-hypertensive effects.

Original languageEnglish
Pages (from-to)1967-1974
Number of pages8
JournalJournal of Dairy Science
Issue number7
Publication statusPublished - 2004 Jul


  • Angiotensin-converting enzyme
  • Anti-hypertensive peptide
  • Whey

ASJC Scopus subject areas

  • Food Science
  • Animal Science and Zoology
  • Genetics

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