ACE-inhibitory activity and ACE-inhibiting peptides in different cheese varieties

Sieber, R.; Bütikofer, Ueli; Egger, Lotti; Portmann, Reto; Walther, Barbara; Wechsler, Daniel

doi:10.1051/dst/2009049

Cited by 78 publications

(66 citation statements)

References 124 publications

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“…Also, there is a great influence of non-starter autochthonous bacteria to these differences (Sieber et al, 2010).…”

Section: Antihypertensive Peptidesmentioning

confidence: 99%

“…presents an overview of currently known forms of peptide bioactivity in milk and milk products. Bioactive peptides contained in fermented milk products are mainly derived from casein hydrolysis by proteases and peptidases originating from milk, rennet, starter-and non-starter bacteria (Sieber et al, 2010;Sahingil et al, 2014). Besides caseins, whey proteins and their proteolytic products also exert bioactivity (Korhonen et al, 1998; Lisak-Jakopović et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

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White cheeses as a potential source of bioactive peptides

et al. 2017

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In addition to the nutritional value, cheese and other fermented milk-based products are a good source of biologically active proteins and peptides. Bioactive peptides in cheese are mainly formed during cheese production, especially during ripening, which is one of the most important stages in cheese production. Since the ripening process differ significantly depending on the cheese type, it can be assumed that their bioactivity is also substantially different. White brined cheeses are specific for the region of South-Eastern Europe. They are characterized by relatively intensive proteolysis and as such may be of interest as products with favorable functional characteristics. Yet, their functionality is still insufficiently characterized. This paper presents an overview of the current knowledge on white brined cheese's bioactive peptides.

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“…Also, there is a great influence of non-starter autochthonous bacteria to these differences (Sieber et al, 2010).…”

Section: Antihypertensive Peptidesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

White cheeses as a potential source of bioactive peptides

et al. 2017

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“…A search for the biological activity of peptides identified was conducted through the Dziuba database (http://www.uwm.edu.pl/ biochemia/biopep/start_biopep.php) and by comparing sequences either reviewed or described in numerous articles (19)(20)(21)(22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35)(36).…”

Section: Identification Of Bioactive Peptidesmentioning

confidence: 99%

Sequential release of milk protein–derived bioactive peptides in the jejunum in healthy humans

Boutrou

Gaudichon²,

Dupont³

et al. 2013

The American Journal of Clinical Nutrition

253

158

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Background:The digestive hydrolysis of dietary proteins leads to the release of peptides in the intestinal tract, where they may exert a variety of functions, but their characterization and quantification are difficult. Objectives: We aimed to characterize and determine kinetics of the formation of peptides present in the jejunum of humans who ingested casein or whey proteins by using mass spectrometry and to look for and quantify bioactive peptides. Design: Subjects were equipped with a double-lumen nasogastric tube that migrated to the proximal jejunum. A sample collection was performed for 6 h after the ingestion of 30 g 15 N-labeled casein (n = 7) or whey proteins (WPs; n = 6). Nitrogen flow rates were measured, and peptides were identified by using mass spectrometry. Results: After casein ingestion, medium-size peptides (750-1050 kDa) were released during 6 h, whereas larger peptides (1050-1800 kDa) were released from WPs in the first 3 h. A total of 356 and 146 peptides were detected and sequenced in the jejunum after casein and WP ingestion, respectively. b-casein was the most important precursor of peptides, including bioactive peptides with various activities. The amounts of b-casomorphins (b-casein 57-, 58-, 59-, and 60-66) and b-casein 108-113 released on the postprandial window were sufficient to elicit the biological action of these peptides (ie, opioid and antihypertensive, respectively). Conclusions: Clear evidence is shown of the presence of bioactive peptides in the jejunum of healthy humans who ingested casein. Our findings raise the question about the physiologic conditions under which these peptides can express their bioactivity in humans. This trial was registered at clinicaltrials.gov as NCT00862329.Am J Clin Nutr 2013;97:1314-23.

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“…The most active subfraction (Aghh-III-2a), which contained according to TLC three components with MWs about 2.5 kDa, was not a homogeneous peptide. Nevertheless, the activity of inhibitors obtained pure (Aghh-III-4 and -4a) was fully comparable with that of the strongest known ACEIs [7][8][9]11]. Table 1 presents results from activity testing of ACEIs in the obtained subfractions.…”

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confidence: 71%

Isolation and Characterization of Angiotensin-Converting Enzyme Inhibitors from Agkistrodon halys halys Venom

et al. 2013

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547.993The peptide fraction of venom from the Eastern pit viper Agkistrodon halys halys (Crotalidae) that was obtained by gel-filtration over Sephacryl S-100 HR exhibited high activity as an angiotensin-converting enzyme (ACE, EC 3.4.15.1) inhibitor. Separation of the materials over TSK HW-40F and SP-Sephadex C-25 produced purified (chromatographically pure) ACE inhibitors (ACEI) of molecular weight up to 2.5 kDa and IC 50 values in the range 0.48-15.3 Pg/mL.Angiotensin-converting enzyme (ACE) inhibitors (ACEIs) are the leading drugs for treating cardiovascular diseases. Structural data of low-molecular-weight peptides from snake venoms [1] modified by sulfhydryl, carboxyl, and phosphate groups (captopril, enalapril, and fosinopril, respectively) were used to create them [2]. These drugs are not very selective for ACE [1, 2] so that their systemic administration produces uncontrolled side effects (cough, skin rashes, vessel edema, etc.). Hence, the search for and comparisons of new ACEIs with minimal effects on other in vivo systems from various sources including snake venoms is timely [1, 3-9].The activity of ACEIs from venoms was shown earlier [6] to decrease in the series pit-viper > common northern viper > blunt-nosed viper > steppe viper. Therefore, research on their isolation was performed using pit-viper venom. The ACEI fraction was obtained using chromatography of the venom on a high-resolution calibrated column of Sephacryl S-100 HR 16/60, separating them as a sum of peptides of different molecular weights (MWs) (Fig. 1). According to gel-filtration, a fraction (Aghh-III) of peptides with MWs 8.0-0.5 kDa and 6.6, 4.5, and 1.1 kDa was formed.We found earlier during screening of ACEIs in venoms of Central Asian snakes [5, 6] that this fraction contained lowmolecular-weight peptides that were characterized by weak absorption at 280 nm that was apparently due to an insignificant content of aromatic amino acids. They did not appear as separate peaks on densitograms. However, their weight content was substantial. Electrophoresis of the studied fraction (under denaturing conditions) did not detect in it discrete components with MWs > 2.0 kDa. This suggested that the components with MW 8.0-2.0 kDa that were observed by gel-filtration were aggregates of peptides of lesser MW.Data on the hydrolysis of Aghh-III by HCl (5.7 N) or a mixture of proteolytic enzymes (trypsin, chymotrypsin, carboxypeptidase Y) argued in favor of the peptide nature of the identified inhibitors. As a result, the ACEI activity decreased by an average of 80%. The remaining 20% of the activity was associated with the presence in the studied materials of an N-terminal pyroglutamate residue that was not hydrolyzed under the experimental conditions and was shown to be an ACEI [10].The inhibitory activity of peptide fraction Aghh-III for ACE was estimated from the IC 50 value, i.e., the peptide concentration at which the enzyme activity was inhibited by 50%. A least-squares method (linear regression) was used to calculate the kinetic parameters....

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ACE-inhibitory activity and ACE-inhibiting peptides in different cheese varieties

Cited by 78 publications

References 124 publications

White cheeses as a potential source of bioactive peptides

White cheeses as a potential source of bioactive peptides

Sequential release of milk protein–derived bioactive peptides in the jejunum in healthy humans

Isolation and Characterization of Angiotensin-Converting Enzyme Inhibitors from Agkistrodon halys halys Venom

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