Antihypertensive effect of a bovine lactoferrin pepsin hydrolysate: Identification of novel active peptides

Ruiz-Giménez, Pedro; Salom, Juan B.; Marcos, José F.; Vallés, Salvador; Martínez-Maqueda, Daniel; Recio, Isidra; Torregrosa, Germán; Alborch, Enrique; Manzanares, Paloma

doi:10.1016/j.foodchem.2011.08.076

Cited by 64 publications

(46 citation statements)

References 29 publications

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“…These peptides acted as antihypertensive agents to SHR. The peptide LIWKL had the most remarkable antihypertensive activity compared to RPYL and LNNSRAP and the effect of BP reduction remained significant for up to 24 h postadministration (Ruiz‐Giménez and others ).…”

Section: Milk and Dairy Productsmentioning

confidence: 97%

Food‐Originating ACE Inhibitors, Including Antihypertensive Peptides, as Preventive Food Components in Blood Pressure Reduction

Iwaniak

Minkiewicz

Darewicz

2014

Comp Rev Food Sci Food Safe

266

214

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This work is a literature overview on angiotensin-converting enzyme (ACE) inhibitory/antihypertensive peptides in food protein sources. The following aspects related to peptides with the above-mentioned bioactivity are discussed: (i) mechanism of action of ACE, (ii) the structural character of ACE inhibitors/antihypertensive peptide sequences determined by different methods, including quantitative structure-activity relationship studies, (iii) their food sources, (iv) absorption of peptides, (v) in vitro and in vivo approaches involved in the production and potential release of peptide ACE inhibitors as well as in silico methods applied in research concerning peptides.

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Section: Milk and Dairy Productsmentioning

confidence: 97%

Food‐Originating ACE Inhibitors, Including Antihypertensive Peptides, as Preventive Food Components in Blood Pressure Reduction

Iwaniak

Minkiewicz

Darewicz

2014

Comp Rev Food Sci Food Safe

266

214

View full text Add to dashboard Cite

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“…The fraction containing the most active peptides is then subjected to high pressure liquid chromatography (HPLC) separation using a reverse-phase column (RP-HPLC). This allows obtaining peptides subfractions with different hydrophobic behavior, but more than one RP-HPLC round will be required in order to obtain highly pure peptides in a sufficient amount (de Gobba et al, 2014a;Chi et al, 2015;Ruiz-Gim enez et al, 2012). Furthermore, hydrophilic interaction liquid chromatography (HILIC) has recently been suggested for an improved separation of homologous short peptides (Le Maux et al, 2015).…”

Section: Removing Bitternessmentioning

confidence: 99%

Peptides: Production, bioactivity, functionality, and applications

Hajfathalian

Ghelichi

Moreno

et al. 2017

Critical Reviews in Food Science and Nutrition

133

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Production of peptides with various effects from proteins of different sources continues to receive academic attention. Researchers of different disciplines are putting increasing efforts to produce bioactive and functional peptides from different sources such as plants, animals, and food industry by-products. The aim of this review is to introduce production methods of hydrolysates and peptides and provide a comprehensive overview of their bioactivity in terms of their effects on immune, cardiovascular, nervous, and gastrointestinal systems. Moreover, functional and antioxidant properties of hydrolysates and isolated peptides are reviewed. Finally, industrial and commercial applications of bioactive peptides including their use in nutrition and production of pharmaceuticals and nutraceuticals are discussed.

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“…The hydrolysates were centrifuged (6000 × g for 15 min) and the supernatants were collected. The protein concentration of supernatants was determined by the bicinchoninic acid method using bovine serum albumin as a standard 21 . The hydrolysates were passed through ultrafiltration membranes with a cut-off of 5 kDa.…”

Section: Extracellular Proteases Preparationmentioning

confidence: 99%

Casein Hydrolysates by Lactobacillus brevis and Lactococcus lactis Proteases: Peptide Profile Discriminates Strain-Dependent Enzyme Specificity

Bounouala

Roudj

Karam

et al. 2017

J. Agric. Food Chem.

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Casein from ovine and bovine milk were hydrolyzed with two extracellular protease preparations from Lactobacillus brevis and Lactococcus lactis. The hydrolysates were analyzed by HPLC-MS/MS for peptide identification. A strain-dependent peptide profile could be observed, regardless of the casein origin, and the specificity of these two proteases could be computationally ascribed. The cleavage pattern yielding phenylalanine, leucine, or tyrosine at C-terminal appeared both at L. lactis and Lb. brevis hydrolysates. However, the cleavage C-terminal to lysine was favored with Lb. brevis protease. The hydrolysates showed ACE-inhibitory activity with IC in the 16-70 μg/mL range. Ovine casein hydrolysates yielded greater ACE-inhibitory activity. Previously described antihypertensive and opioid peptides were found in these ovine and bovine casein hydrolysates and prediction of the antihypertensive activity of the sequences based on quantitative structure and activity relationship (QSAR) was performed. This approach might represent a useful classification tool regarding health-related properties prior to further purification.

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Antihypertensive effect of a bovine lactoferrin pepsin hydrolysate: Identification of novel active peptides

Cited by 64 publications

References 29 publications

Food‐Originating ACE Inhibitors, Including Antihypertensive Peptides, as Preventive Food Components in Blood Pressure Reduction

Food‐Originating ACE Inhibitors, Including Antihypertensive Peptides, as Preventive Food Components in Blood Pressure Reduction

Peptides: Production, bioactivity, functionality, and applications

Casein Hydrolysates by Lactobacillus brevis and Lactococcus lactis Proteases: Peptide Profile Discriminates Strain-Dependent Enzyme Specificity

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