Hostname: page-component-76fb5796d-vvkck Total loading time: 0 Render date: 2024-04-26T07:54:16.988Z Has data issue: false hasContentIssue false
  • English
  • Français

Effect of simulated gastrointestinal digestion on the antihypertensive properties of synthetic β-lactoglobulin peptide sequences

Published online by Cambridge University Press:  30 April 2007

Blanca Hernández-Ledesma ,
Marta Miguel ,
Lourdes Amigo ,
Maria Amaya Aleixandre  and
Isidra Recio
Blanca Hernández-Ledesma
Affiliation:
Instituto de Fermentaciones Industriales (CSIC). Madrid. Spain
Marta Miguel
Affiliation:
Instituto de Fermentaciones Industriales (CSIC). Madrid. Spain
Lourdes Amigo
Affiliation:
Instituto de Fermentaciones Industriales (CSIC). Madrid. Spain
Maria Amaya Aleixandre
Affiliation:
Instituto de Farmacología y Toxicología (CSIC). Departamento de Farmacología, Facultad de Medicina, Univ. Complutense, Madrid, Spain
Isidra Recio*
Affiliation:
Instituto de Fermentaciones Industriales (CSIC). Madrid. Spain
*
*For correspondence; e-mail: recio@ifi.csic.es
Get access Rights & Permissions [Opens in a new window]

Abstract

In this study, the antihypertensive activity in spontaneously hypertensive rats of two peptides isolated from β-lactoglobulin hydrolysates with thermolysin was evaluated. These peptides, with sequences LLF [β-lg f(103–105)] and LQKW [β-lg f(58–61)], showed potent in vitro ACE-inhibitory activity. Two hours after administration, both sequences caused a clear and significant decrease in the blood pressure of these rats. The impact of a simulated gastrointestinal digestion on ACE-inhibitory and antihypertensive activities of these peptides was also studied. The results showed that both fragments were susceptible to proteolytic degradation after incubation with pepsin and Corolase PP®. In addition, their in vitro ACE-inhibitory activity decreased after the simulated digestion. It is likely that fragment LQK was the active end product of the gastrointestinal digestion of peptide LQKW. The fragment LL, observed after digestion of peptide LLF, probably exert its antihypertensive effect through a mechanism of action different than ACE-inhibition.

Keywords

β-lactoglobulin peptidesACE-inhibitory activityantihypertensive effectsimulated gastrointestinal digestion
Type
Research Article
Information
Journal of Dairy Research , Volume 74 , Issue 3 , August 2007 , pp. 336 - 339
Copyright
Copyright © Proprietors of Journal of Dairy Research 2007

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Alting, AC, Meijer, RJGM & van Beresteijn, ECH 1997 Incomplete elimination of the ABBOS epitope of bovine serum albumin under simulated gastointestinal conditions of infants. Diabetes Care 20 875–880CrossRefGoogle Scholar
Chobert, J-M, El-Zahar, K, Sitohy, M, Dalgalarrondo, M, Métro, F, Choiset, Y & Haertlé, T 2005 Angiotensin I-converting-enzyme (ACE)-inhibitory activity of tryptic peptides of ovine β-lactoglobulin and of milk yoghurts obtained by using different starters. Lait 85 141–152CrossRefGoogle Scholar
Costa, EL, Almeida, AR, Netto, FM & Gontijo, JAR 2005 Effect of intraperitoneally administered hydrolyzed whey protein on blood pressure and renal sodium handling in awake spontaneously hypertensive rats. Brazilian Journal of Medical and Biological Research 38 1817–1824CrossRefGoogle ScholarPubMed
Cushman, DW & Cheung, HS 1971 Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochemical Pharmacology 20 1637–1648CrossRefGoogle ScholarPubMed
Fitzgerald, RJ & Meisel, H 2000 Milk protein-derived peptide inhibitors of angiotensin-I-converting enzyme. British Journal of Nutrition 84 S33–S37Google Scholar
Gómez-Ruiz, JA, Recio, I & Belloque, J 2004 ACE-inhibitory activity and structural properties of peptide Asp-Lys-Ile-His-Pro[β-CN f(47–51)]. Study of peptide forms synthesized by different methods. Journal of Agricultural and Food Chemistry 52 6315–6319Google Scholar
Hernández-Ledesma, B, Amigo, L, Ramos, M & Recio, I 2004 Application of HPLC-MS/MS to the identification of biologically active peptides produced by milk fermentation and simulated gastrointestinal digestion. Journal of Chromatography A 1049 107–114CrossRefGoogle Scholar
Hernández-Ledesma, B, Ramos, M, Recio, I & Amigo, L 2006 Effect of beta-lactoglobulin hydrolysis with thermolysin under denaturing temperatures on the release of bioactive peptides. Journal of Chromatography A 1116 31–37Google Scholar
Hernández-Ledesma, B, Recio, I, Ramos, M & Amigo, L 2002 Preparation of ovine and caprine β-lactoglobulin hydrolysates with ACE-inhibitory activity. Identification of active peptides from caprine β-lactoglobulin hydrolysed with thermolysin. International Dairy Journal 12 805–812CrossRefGoogle Scholar
Miguel, M, Aleixandre, MA, Ramos, M & López-Fandiño, R 2006 Effect of simulated gastrointestinal digestion on the antihypertensive properties of ACE-inhibitory peptides derived from ovalbumin. Journal of Agricultural and Food Chemistry 54 726–731CrossRefGoogle ScholarPubMed
Miguel, M, López-Fandiño, R, Ramos, M & Aleixandre, MA 2005 Short-term effect of egg white hydrolysate products on the arterial blood pressure of hypertensive rats. British Journal of Nutrition 94 731–737CrossRefGoogle ScholarPubMed
Pihlanto-Leppälä, A, Koskinen, P, Piilola, K, Tupasela, T & Korhonen, H 2000 Angiotensin-I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides. Journal of Dairy Research 67 53–64Google Scholar
Quirós, A, Hernández-Ledesma, B, Ramos, M, Amigo, L & Recio, I 2005 Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir. Journal of Dairy Science 88 3480–3487Google Scholar
Sipola, M, Finckenberg, P, Vapaatalo, H, Pihlanto-Leppälä, A, Korhonen, H, Korpela, R & Nurminen, ML 2002 α-lactorphin and β-lactorphin improve arterial function in spontaneously hypertensive rats. Life Sciences 71 1245–1253Google Scholar