In vitro digestibility of bioactive peptides derived from bovine β-lactoglobulin

Roufik, Samira; Gauthier, Sylvie F.; Turgeon, Sylvie L.

doi:10.1016/j.idairyj.2005.03.010

Cited by 76 publications

(63 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…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

View full text Add to dashboard Cite

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.

show abstract

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

View full text Add to dashboard Cite

show abstract

“…An in vitro study demonstrated that heptapeptides (fr. 142-148) can be hydrolysed by chymotrypsin during digestion [Roufi k et al 2006]. Otte et al [2011] analysed peptide profi les of fermented milk products containing Lactobacillus helveticus and Lacctococcus lactis strains.…”

Section: Research Into Bioactive Peptides In Dairy Productsmentioning

confidence: 99%

Milk proteins-derived bioactive peptides in dairy products: molecular, biological and methodological aspects

Dziuba

2014

Acta Sci Pol Technol Aliment

View full text Add to dashboard Cite

Proteins are one of the primary components of the food, both in terms of nutrition and function. They are main source of amino acids, essential for synthesis of proteins, and also source of energy. Additionally, many proteins exhibit specifi c biological activities, which may have effect on functional or pro-health properties of food products. These proteins and their hydrolysis products, peptides, may infl uence the properties of food and human organism. The number of commercially available food products containing bioactive peptides is very low, apart from that milk proteins are their rich source. It could be supposed that number of available products with declared activity will rise in near future because of observed strong uptrend on interest in such products. Molecular and biological properties of milk proteins, as precursors of bioactive peptides was characterised in the work. Therefore, the strategy of research and obtaining of such peptides both in laboratory and industrial scale, as well as the range of their commercial application, was presented. Several examples of research efforts presenting high potential to develop new products containing bioactive peptides from milk proteins and predetermined as nutraceuticals was described.

show abstract

“…The structure and bioactivity of short-chain peptides are more easily preserved through gastrointestinal passage than those of their long-chain counterparts [272] -whereas sequences containing Pro residue(s) are generally more resistant to degradation by digestive enzymes [273]. Furthermore, peptides absorbed following digestion may accumulate in specific organs, and then exert their action in a systematic and gradual manner [274,275].…”

Section: Bioavailabilitymentioning

confidence: 99%

“…However, the degree of hydrolysis of a given peptide depends not only on its size and nature, but also on the presence of other peptides in its vicinity [272] -which would make it difficult to test the required number of possibilities in a rather limited experimental program. Several in vitro studies were carried out that show the importance of digestion upon formation and degradation of ACEinhibitor peptides [107,272,[278][279][280]284]. In these studies, peptides were subjected to two stages of hydrolysis that mimic digestion in the body.…”

Section: Bioavailabilitymentioning

confidence: 99%

“…In vitro simulated digestion is in fact not entirely reliable; the degree of hydrolysis depends on the size, nature and neighborhood of the peptide [272], so in vivo studies (with laboratory animals and human volunteers) are eventually necessary to ascertain in full the behavior of the peptide. Another example is the release of potent ACE-inhibitory peptides from WPC brought about by aqueous extracts from the plant C. cardunculus.…”

Section: Bioavailabilitymentioning

confidence: 99%

See 1 more Smart Citation

Whey Proteins as Source of Bioactive Peptides Against Hypertension

Tavares¹,

Malcata²

2013

Bioactive Food Peptides in Health and Disease

View full text Add to dashboard Cite

In vitro digestibility of bioactive peptides derived from bovine β-lactoglobulin

Cited by 76 publications

References 36 publications

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

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

Milk proteins-derived bioactive peptides in dairy products: molecular, biological and methodological aspects

Whey Proteins as Source of Bioactive Peptides Against Hypertension

Contact Info

Product

Resources

About