Peptide profiles and angiotensin-I-converting enzyme inhibitory activity of fermented milk products: Effect of bacterial strain, fermentation pH, and storage time

Nielsen, Mette S.; Martinussen, Torben; Flambard, Bénédicte; Sørensen, Kim I.; Otte, Jeanette

doi:10.1016/j.idairyj.2008.10.003

Cited by 122 publications

(119 citation statements)

References 43 publications

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“…Similarly, other L. helveticus strains such as NCC 2765 [100], PR4 [69] or 130B4 from camel milk [113] and in a further study [82] two highly proteolytic strains of L. helveticus (MI 1198, MI 1263), as well as strains of Lc. lactis ssp.…”

Section: Starter Culturesmentioning

confidence: 92%

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

Sieber

Bütikofer

Egger

et al. 2009

Dairy Sci. Technol.

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-During the ripening of cheese, a large number of peptides are formed from casein. Some of these peptides have been shown to exert an antihypertensive effect due to their angiotensin-I-converting enzyme (ACE)-inhibitory activity. Recently, several studies have investigated the ACE-inhibiting potential of cheese, and various ACE-inhibiting peptides have been isolated and identified from different cheese varieties. The present review focuses on the occurrence of two tripeptides, Val-Pro-Pro and Ile-Pro-Pro, in cheese. These tripeptides were first described in fermented-milk products and have been demonstrated to exert a blood pressure-lowering effect in humans with mild hypertension. The influence of cheesemaking and ripening on the release of ACE-inhibiting peptides is revealed. Finally, the antihypertensive potential of cheese with high ACE-inhibitory activity is discussed with regard to the bioavailability of the peptides involved.

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Section: Starter Culturesmentioning

confidence: 92%

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

Sieber

Bütikofer

Egger

et al. 2009

Dairy Sci. Technol.

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“…As reported by Atlan et al (1990) PepX is located in cytoplasm, so these long periods of aging possibly resulted in cell lysis, leading to release of PepX that during storage of yoghurt degraded and BCMs formed. In addition, during fermentation, the proteases associated with the cell wall of the starter culture or contaminating bacteria can hydrolyze caseins into large peptides and possibly even BCM7, which subsequently are transported into the bacteria cell and then hydrolyzed into a large number of smaller peptides, e.g., di and tri-peptides (Nielsen et al, 2009). Consequently, L. delbrueckii ssp.…”

Section: Yoghurtmentioning

confidence: 99%

“…In fermented milk manufacture, fermentation commonly ends at pH 3.5-4.6 before subsequent cold storage. According to Nielsen et al (2009), milk inoculated with L. lactis strains and L. helviticus strains fermented to pH 4.6 and 4.3 resulted in large peptides being released from b-casein after 7-day cold storage, but no BCMs. The authors also observed no change in peptide profile during storage for milk inoculated with S. thermophilus fermented to pH 4.6 and 4.3.…”

Section: Effect Of Fermentation Processmentioning

confidence: 99%

Formation and Degradation of Beta-casomorphins in Dairy Processing

Doan

Johnson

Busetti

et al. 2014

Critical Reviews in Food Science and Nutrition

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Milk proteins including casein are sources of peptides with bioactivity. One of these peptides is beta-casomorphin (BCM) which belongs to a group of opioid peptides formed from b-casein variants. Beta-casomorphin 7 (BCM7) has been demonstrated to be enzymatically released from the A1 or B b-casein variant. Epidemiological evidence suggests the peptide BCM 7 is a risk factor for development of human diseases, including increased risk of type 1 diabetes and cardiovascular diseases but this has not been thoroughly substantiated by research studies. High performance liquid chromatography coupled to UV-Vis and mass spectrometry detection as well as enzyme-linked immunosorbent assay (ELISA) has been used to analyze BCMs in dairy products. BCMs have been detected in raw cow's milk and human milk and a variety of commercial cheeses, but their presence has yet to be confirmed in commercial yoghurts. The finding that BCMs are present in cheese suggests they could also form in yoghurt, but be degraded during yoghurt processing. Whether BCMs do form in yoghurt and the amount of BCM forming or degrading at different processing steps needs further investigation and possibly will depend on the heat treatment and fermentation process used, but it remains an intriguing unknown.

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“…Fermentation from pH 4.6 to 4.3 with these strains slightly increased the ACEI activity, whilst fermentation to pH 3.5 with Lb. helveticus reduced the ACEI activity [39]. Moreover, four different Enterococcus faecalis strains, isolated from raw milk, produced fermented milk with potent ACEI activity [40].…”

Section: Fermented Milkmentioning

confidence: 99%

Lactic Fermentation and Bioactive Peptides

Pihlanto¹

2013

Lactic Acid Bacteria - R &Amp; D for Food, Health and Livestock Purposes

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Peptide profiles and angiotensin-I-converting enzyme inhibitory activity of fermented milk products: Effect of bacterial strain, fermentation pH, and storage time

Cited by 122 publications

References 43 publications

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

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

Formation and Degradation of Beta-casomorphins in Dairy Processing

Lactic Fermentation and Bioactive Peptides

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