Identification of bioactive peptides and quantification of β-casomorphin-7 from bovine β-casein A1, A2 and I after ex vivo gastrointestinal digestion

Asledottir, Tora; Le, Thao T.; Petrat-Melin, Bjørn; Devold, Tove Gulbrandsen; Larsen, Lotte Bach; Vegarud, Gerd Elisabeth

doi:10.1016/j.idairyj.2017.03.008

Cited by 63 publications

(27 citation statements)

References 51 publications

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“…After the harmonization of the static digestion protocol, several studies have been performed using the INFOGEST protocol to study the bioaccessibility and the bioactivity of milk and dairy proteins and peptides. The digestion, hydrolysis, and peptide profile from casein was investigated by Asledottir et al (2017Asledottir et al ( , 2018 in digestates from casein and from ex vivo gastrointestinal digestion. In our research group, we digested a selection of whey, casein, and plant proteins in vitro and found an increase in angiotensin I-converting enzyme (ACE) inhibitory activity after in vitro dairy protein digestion (Fekete et al, 2016a;Giromini et al, 2017).…”

Section: Static Models To Study Dairy Bioactivesmentioning

confidence: 99%

Invited review: Dairy proteins and bioactive peptides: Modeling digestion and the intestinal barrier

Giromini

Cheli

Rebucci

et al. 2019

Journal of Dairy Science

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Dairy products are one of the most important sources of biologically active proteins and peptides. The healthpromoting functions of these peptides are related to their primary structure, which depends on the parent protein composition. A crucial issue in this field is the demonstration of a cause-effect relationship from the ingested protein form to the bioactive form in vivo. Intervention studies represent the gold standard in nutritional research; however, attention has increasingly been focused on the development of sophisticated in vitro models of digestion to elucidate the mechanism of action of dairy nutrients in a mechanistic way and significantly reduce the number of in vivo trials. On the other hand, the epithelial intestinal barrier is the first gate that actively interacts with digestion metabolites, making the intestinal cells the first target tissue of dairy nutrients and respective metabolites. An evolution of the in vitro digestion approach in the study of dairy proteins and derived bioactive compounds is the setup of combined in vitro digestion and cell culture models taking into consideration the endpoint to measure the target organism (e.g., animal, human) and the key concepts of bioaccessibility, bioavailability, and bioactivity. This review discusses the relevance and challenges of modeling digestion and the intestinal barrier, focusing on the implications for the modeling of dairy protein digestion for bioactivity evaluation.

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Section: Static Models To Study Dairy Bioactivesmentioning

confidence: 99%

Invited review: Dairy proteins and bioactive peptides: Modeling digestion and the intestinal barrier

Giromini

Cheli

Rebucci

et al. 2019

Journal of Dairy Science

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“…() showed that β‐casein‐derived peptides, such as XPP and XP, were especially resistant to the digestive action of intestinal proteases in vivo . Many investigations are focused on the in vitro , in vivo , or ex vivo digestibility of food proteins and the bioactivity and bioavailability of peptides obtained during the enzymatic hydrolysis process (González‐Montoya et al ., ; Sanchón et al ., ; Jakubczyk et al ., ; Zielińska et al ., ; Egger et al ., ; Asledottir et al ., ; Wada & Lönnerdal, ; Karaś et al ., ). These models are suitable for evaluation of the influence of gastrointestinal digestion protein on the release of bioactive peptides or susceptibility of peptides to digestion (Minekus et al ., ; Udechukwu et al ., ).…”

Section: Digestion and Absorption Of Protein And Peptidesmentioning

confidence: 99%

Influence of physiological and chemical factors on the absorption of bioactive peptides

Karaś

2018

Int J of Food Sci Tech

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Food-derived bioactive peptides can be released during digestion and have a potentially beneficial effect on human health. It is known that the penetration of peptides across the small intestine can take place in several ways. The research related to the bioavailability of peptides develops dynamically, but still raises many doubts. Since there are many barriers to absorption of peptides, there is still a need to carry out in vitro and in vivo investigations on the bioavailability of these compounds. Moreover, there are few in vivo studies regarding the absorption and activity of peptides in organs, hence the lack of unequivocal and reliable information about this process. Therefore, this review discusses the current research on in vitro and in vivo absorption of these compounds and factors that play a key role in this process and provides better understanding of the in vitro and in vivo bioavailability and bioaccessibility of peptides.

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“…Multiple or selected reaction monitoring (MRM or SRM) has been applied to the quantification of lactosylated milk proteins, mostly at relative concentration ( Le et al., 2013 ). Nevertheless, there have been a number of studies published on absolute quantification of either milk bioactive peptides ( Asledottir et al., 2017 ; Asledottir et al., 2018 ), human milk proteins ( Chen et al., 2016 ) or cow's milk proteins in processed dairy products ( Lutter et al., 2011 ). Recently, the application of MRM for the absolute and simultaneous quantification of twenty bovine milk proteins was reported ( Bär et al., 2019 ).…”

Section: Introductionmentioning

confidence: 99%

Quantitative LC-MS/MS analysis of high-value milk proteins in Danish Holstein cows

Poulsen

Kristiansen

et al. 2020

Heliyon

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High-value milk proteins, which can be obtained by optimized fractionation procedures, are ideal ingredients in many food applications. Thus, a simple and robust analytical method is required for the identification and quantification of these individual milk proteins. Here, we present a liquid chromatography–tandem mass spectrometry (LC-MS/MS) method using multiple reaction monitoring (MRM) to simultaneously detect and measure target peptides of two major milk proteins, α-lactalbumin (α-LA) and β-casein (β-CN), in raw milk samples from 662 Danish Holstein cows. The MRM quantification of α-LA and β-CN was achieved with limit of detection (LOD) of 0.14 and 0.16 g/L, respectively and reproducibility of the assay <15%. By this newly established MRM-based method, the concentration of α-LA and β-CN in an individual cow's milk ranged from 0.5 to 1.9 (average 1.1) g/L, and from 7.5 to 23.4 (average 15) g/L, respectively. There was no significant effect of parity, whereas significantly increasing concentrations of α-LA and β-CN were observed through lactation (P < 0.001). This shows a considerable biological variation of these two ingredient milk proteins, providing potential varying outputs of fractionation in the dairy streams.

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Identification of bioactive peptides and quantification of β-casomorphin-7 from bovine β-casein A1, A2 and I after ex vivo gastrointestinal digestion

Cited by 63 publications

References 51 publications

Invited review: Dairy proteins and bioactive peptides: Modeling digestion and the intestinal barrier

Invited review: Dairy proteins and bioactive peptides: Modeling digestion and the intestinal barrier

Influence of physiological and chemical factors on the absorption of bioactive peptides

Quantitative LC-MS/MS analysis of high-value milk proteins in Danish Holstein cows

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