Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity

López‐Fandiño, Rosina; Otte, Jeanette; Camp, John Van

doi:10.1016/j.idairyj.2006.06.004

Cited by 325 publications

(235 citation statements)

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“…The effect of Ile-Pro-Pro and ValPro-Pro seems to be related to ACE-inhibitory activity (Ahimastos et al, 2005;Ló pez-Fandiño et al 2006;Hong et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

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Long-term intervention with Lactobacillus helveticus fermented milk reduces augmentation index in hypertensive subjects

et al. 2010

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Background: The milk casein-derived biologically active tripeptides, isoleucyl-prolyl-proline (Ile-Pro-Pro) and valyl-prolyl-proline (Val-Pro-Pro), have documented antihypertensive effect probably related to reduced angiotensin formation. It has been suggested that these tripeptides may reduce arterial stiffness and improve endothelial function. Our aim was to evaluate whether the milk-based drink containing Ile-Pro-Pro and Val-Pro-Pro influence arterial stiffness, measured as augmentation index (AIx), and endothelial function in man. Methods: In a double-blind parallel group intervention study, 89 hypertensive subjects received daily peptide milk containing a low dose of tripeptides (5 mg/day) for 12 weeks and a high dose (50 mg/day) for the following 12 weeks, or a placebo milk drink to titrate the dose-response effect. Arterial stiffness was assessed by pulse wave analysis at the beginning and end of each intervention period. Endothelial function was tested by examining pulse wave reflection response to sublingual nitroglycerin and salbutamol inhalation. Blood pressure was measured by using office and 24-h ambulatory blood pressure measurement. Results: At the end of the second intervention period, AIx decreased significantly in the peptide group compared with the placebo group (peptide group À1.53% (95% confidence interval (CI) À2.95 to À0.12), placebo group 1.20% (95% CI 0.09-2.32), P ¼ 0 Á 013). No change in endothelial function index was observed (peptide group 0.02 (95% CI À0.06 to 0.08), placebo group 0.04 (95% CI À0.04 to 0.12), P ¼ 0.85). There were no statistically significant differences between the effects of the peptide and placebo treatment on office and 24-h ambulatory blood pressure. Conclusions: Long-term treatment with Lactobacillus helveticus-fermented milk containing bioactive peptides reduces arterial stiffness expressed as AIx in hypertensive subjects.

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“…The effect of Ile-Pro-Pro and ValPro-Pro seems to be related to ACE-inhibitory activity (Ahimastos et al, 2005;Ló pez-Fandiño et al 2006;Hong et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

“…By contrast, two recent studies suggested that milk tripeptides have no significant blood pressure-lowering effects (Engberink et al, 2008;van der Zander et al, 2008). The antihypertensive effects of milkderived peptides have recently been reviewed (FitzGerald et al, 2004;Ló pez-Fandiño et al, 2006;Hong et al, 2008;Korhonen 2009). …”

Section: Introductionmentioning

confidence: 99%

Long-term intervention with Lactobacillus helveticus fermented milk reduces augmentation index in hypertensive subjects

et al. 2010

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“…Milk proteins are particularly good sources of ACE-inhibitory peptides and had been widely studied in the past (da Costa et al 2007;López-Fandiño et al 2006;Miguel et al 2009;Ortiz-Chao et al 2009). To obtain the peptides with high ACE-inhibitory activity, a lot of works have been carried out by in vitro enzymatic hydrolysis ) or fermentation (Pihlanto et al 2010) of food proteins.…”

Section: Introductionmentioning

confidence: 99%

Optimization of some conditions of Neutrase-catalyzed plastein reaction to mediate ACE-inhibitory activity in vitro of casein hydrolysate prepared by Neutrase

Kong

Zhao

2011

J Food Sci Technol

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Casein hydrolysate was prepared by hydrolyzing casein with Neutrase and then modified by a Neutrasecatalyzed plastein reaction. The prepared hydrolysate had a degree of hydrolysis of 13.0% and exhibited ACE inhibition in vitro with an IC 50 value of 40.4 μg⋅mL −1 . With the decreased amount of free amino groups of the modified hydrolysate as the response, some conditions of the plastein reaction including substrate concentration, enzyme to substrate ratio, reaction temperature and time were studied by single factor experiments and response surface methodology, and optimized finally as 62% (w/w), 3.0 kU⋅g −1 peptides, 30°C and 6.3 h, respectively. The maximum decreased amount of free amino groups of the modified hydrolysate prepared under these optimized conditions was 210.0 μmol⋅g −1 peptides, while corresponding IC 50 value was lowered to 14.7 μg⋅mL −1 . The present result indicates that Neutrase-catalyzed plastein reaction was capable of enhancing ACE-inhibitory activity in vitro of casein hydrolysate, and also highlights the importance of a forthcoming study to investigate the peptide compositions of the modified hydrolysate and the role of protease used in the plastein reaction.

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“…It seems that amino acids (esp. hydrophobic amino acids) at each of the three C-terminal positions are very important to the ACE-inhibition of the peptides (López-Fandiño et al 2006). During the plastein reaction, some new peptides are formed as a result of condensation or transpeptidation (Yamashita et al 1976).…”

Section: Plastein Reaction Of Casein Hydrolysate and Its Impact On Acmentioning

confidence: 99%

Properties of casein hydrolysate as affected by plastein reaction in ethanol-water medium

Zhang¹,

Zhao²

2013

Czech J. Food Sci.

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Zhang Y., Zhao X.-H. (2013): Properties of casein hydrolysate as affected by plastein reaction in ethanol-water medium. Czech J. Food Sci., 31: 559-567.Casein hydrolysate with in vitro ACE-inhibitory activity of 44.4% at 0.3 mg/ml was generated from casein by Alcalase and modified by the Alcalase-catalysed plastein reaction in an ethanol-water medium. Eight treated hydrolysates were prepared using the reaction time of 1-8 h under ethanol or substrate concentration, Alcalase addition and reaction temperature of 56.8% (v/v) or 56.8% (w/v), 8.4 kU/g peptides and 37.5°C, respectively. Most of the treated hydrolysates showed enhanced ACE-inhibition compared to casein hydrolysate, and a reaction time of 4 h brought about the highest ACE-inhibition. All treated hydrolysates had lower zinc-or calcium-chelation but slightly higher iron(II)-chelation than casein hydrolysate, and a reaction time of 4 or 2 h could grant the treated hydrolysates the highest zinc-or calcium-chelation. Kinetic evaluation indicated that casein hydrolysate and two treated hydrolysates were competitive inhibitors to ACE. ACE-inhibition of these evaluated hydrolysates originated from themselves but was uncorrelated with their zinc-chelation, while their CaCO 3 precipitation inhibition was clearly correlated with their measured calcium-chelation (P < 0.05).

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Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity

Cited by 325 publications

References 127 publications

Long-term intervention with Lactobacillus helveticus fermented milk reduces augmentation index in hypertensive subjects

Long-term intervention with Lactobacillus helveticus fermented milk reduces augmentation index in hypertensive subjects

Optimization of some conditions of Neutrase-catalyzed plastein reaction to mediate ACE-inhibitory activity in vitro of casein hydrolysate prepared by Neutrase

Properties of casein hydrolysate as affected by plastein reaction in ethanol-water medium

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