Antihypertensive Peptides from Milk Proteins

Jäkälä, Pauliina; Vapaatalo, Heikki

doi:10.3390/ph3010251

Cited by 123 publications

(72 citation statements)

References 107 publications

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“…Simulated GI digestion has been carried out on a range of protein sources to assess the effect of GI digestion on ACEinhibitory peptides [19][20][21][22][23][24]. More commonly, ACE-inhibitory peptides are produced through enzymatic hydrolysis with GI enzymes such as pepsin and trypsin or with enzyme combinations such as Alcalase™ [25]. ACE-inhibitory peptides have also been produced during the fermentation of milk during cheese production.…”

Section: Hypotensive Mechanisms Of Actionmentioning

confidence: 99%

Antihypertensive Peptides from Food Proteins

Norris¹,

Fitzgerald²

2013

Bioactive Food Peptides in Health and Disease

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Section: Hypotensive Mechanisms Of Actionmentioning

confidence: 99%

Antihypertensive Peptides from Food Proteins

Norris¹,

Fitzgerald²

2013

Bioactive Food Peptides in Health and Disease

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“…process of fermentation [5]. The consumption of fermented dairy products reduces the level of cholesterol in blood serum [6].…”

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confidence: 99%

Examination of pH, Titratable Acidity and Antioxidant Activity in Fermented Milk

Tomovska¹,

Gjorgievski²,

Makarijoski³

2016

JMSE-A

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As a fermentation medium homogenized and sterilized whole milk is used. The length of the fermentation was 4 hours, symbiosis of Streptococcus thermophilus and Lactobacillus delbruesciissp. Bulgaricus were used, to achieve the isoelectric point of casein 4.6 pH. Monitored parameters were: pH, titratable acidity and antioxidant activity (AOA) in a period of 15 days. It has been determined a decrease of pH value from 6.67 to 4.19, an increase of titratable acidity from 8.0 to 36.07 o SH and an enhancement of AOA from 6.13 to 47.4%.The determination of AOA was accordeda method which is used for different types of food, by using stable 2,2-diphenyl-1-pikrilhidrazil (DPPH) free radical and the absorbance was measured at 517nm on a spectrophotometer Spectroquant Pharo 300, Merck. The neutralization activity of the free radical was expressed as a percentage of inhibition of absorbance of DPPH. Milk fermented with Lactobacillus delbrueckii ssp. Bulgaricus, the highest level of AOA registered immediately after the process of fermentation with a value of 52.44%. The lowest value of AOA for the same symbiosis of cultures was observed at the third day after fermentation process kept at a temperature of 4 °C, with a value of 39.43%.

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“…stomach conditions (29,30)), and the resulting released peptides were analyzed for function. Through this approach, dozens of protein fragments, mostly from bovine milk, but also from human milk, have been shown to have different functions (31), including antimicrobial (32,33), antihypertensive (34,35), immunomodulatory (36,37), and opioid-like (38) actions. However, such in vitro digestion approaches fail to reveal the peptide content present endogenously in milk.…”

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confidence: 99%

Mechanistic Peptidomics: Factors That Dictate Specificity in the Formation of Endogenous Peptides in Human Milk

Guerrero

Dallas

Contreras

et al. 2014

Molecular & Cellular Proteomics

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An extensive mass spectrometry analysis of the human milk peptidome has revealed almost 700 endogenous peptides from 30 different proteins. Two in-house computational tools were created and used to visualize and interpret the data through both alignment of the peptide quasi-molecular ion intensities and estimation of the differential enzyme participation. These results reveal that the endogenous proteolytic activity in the mammary gland is remarkably specific and well conserved. Certain proteins-not necessarily the most abundant ones-are digested by the proteases present in milk, yielding endogenous peptides from selected regions. Our results strongly suggest that factors such as the presence of specific proteases, the position and concentration of cleavage sites, and, more important, the intrinsic disorder of segments of the protein drive this proteolytic specificity in the mammary gland. As a consequence of this selective hydrolysis, proteins that typically need to be cleaved at specific positions in order to exert their activity are properly digested, and bioactive peptides encoded in certain protein sequences are released. Proteins that must remain intact in order to maintain their activity in the mammary gland or in the neonatal gastrointestinal tract are unaffected by the hydrolytic environment present in milk. These results provide insight into the intrinsic structural mechanisms that facilitate the selectivity of the endogenous milk protease activity and might be useful to those studying the peptidomes of other biofluids. Molecular &

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Antihypertensive Peptides from Milk Proteins

Cited by 123 publications

References 107 publications

Antihypertensive Peptides from Food Proteins

Antihypertensive Peptides from Food Proteins

Examination of pH, Titratable Acidity and Antioxidant Activity in Fermented Milk

Mechanistic Peptidomics: Factors That Dictate Specificity in the Formation of Endogenous Peptides in Human Milk

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