Using proteomics to characterise storage-induced aggregates in acidic whey protein isolate drinks

Le, Thao T.; Nielsen, Søren; Villumsen, Nanna Stengaard; Kristiansen, Gitte; Nielsen, Lene Nørby; Nielsen, Søren Achim; Hammershøj, Marianne; Larsen, Lotte Bach

doi:10.1016/j.idairyj.2016.01.028

Cited by 27 publications

(20 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…α S1 -CN was the most susceptible to the heat-induced hydrolysis and ĸ-CN was the most resistant. Indications of acid-induced hydrolysis of whey proteins, in combination with deamidation, have also been reported recently (Le et al, 2016).…”

Section: Proteolysismentioning

confidence: 78%

“…According to Holland et al (2012), the variant A has Asp in place of Gly, therefore the Asn 63 -Asp 64 motif is unlikely to be a non-enzymatic deamidation site. In a recent study, however, deamidation occurred at position Asn 63 in both variants A and B of β-Lg in acidic whey protein isolate drinks during storage, as assessed by 2-DE and MALDI-TOF-MS (Le et al, 2016). This means the Asn 63 -Asp 64 motif could be a potential deamidation site in acidic conditions where direct hydrolysis of the side chain amide generates aspartate.…”

Section: Deamidationmentioning

confidence: 91%

“…-A reduction in nutritional values due to blocked lysines requires quantitative estimation of the modification degree of each protein (Meltretter, 2013(Meltretter, , 2014. Ebner et al, 2016;Larsen et al, 2010b;Le et al, 2016;McGrath et al, 2016;Wedholm et al, 2008-McGrath et al (2016 presented 11 abundant peptides released from N-and C-terminal regions of the caseins in caseinate heated at 130 °C, pH 7 for 120 min. κ-CN was more resistant to heat-induced proteolysis than the other caseins.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Proteomics of major bovine milk proteins: Novel insights

Deeth

Larsen

2017

International Dairy Journal

Self Cite

View full text Add to dashboard Cite

Milk proteomics covers the identification, characterisation and quantification of milk proteins. Its applications vary from the basic composition of milk proteins to their post-translational modifications (PTMs), occurring naturally or via processing and storage. Through the combination of liquid chromatography or two-dimensional gel electrophoresis with advanced mass spectrometry, milk proteomics has revealed PTMs that affect milk protein structural and functional properties. This review discusses detection by proteomics-based methods with special emphasis on natural and process induced PTMs in the major bovine milk proteins. The review covers the importance of milk proteomics in determining PTMs, especially those formed by heat treatment and during storage, and highlights some breakthroughs in PTM studies. Furthermore, aspects and applications of quantitative proteomics on milk proteins and bioinformatics are covered. ___________________________________________________________________________________ 1998). Milk from other species have been included in other reviews (Cunsolo, Muccilli, Saletti & Foti, 2011; El-Salam, 2014) and will not be included here. Overall, bovine milk proteins and related peptides can be classified into four different groups: caseins (α S1-, α S2-, βand κ-caseins), serum proteins [αlactalbumin (α-La), β-lactoglobulin (β-Lg), bovine serum albumin (BSA), immunoglobulins (Igs) and a range of other minor whey proteins], proteose peptones (low molecular weight peptides derived from caseins and well as proteose peptone component 3, called PP3) and membrane [mostly milk fat globule membrane (MFGM)] proteins (Table 1).

show abstract

Section: Proteolysismentioning

confidence: 78%

Section: Deamidationmentioning

confidence: 91%

mentioning

confidence: 99%

See 1 more Smart Citation

Proteomics of major bovine milk proteins: Novel insights

Deeth

Larsen

2017

International Dairy Journal

Self Cite

View full text Add to dashboard Cite

show abstract

“…Digested peptides after both gastric and gastrointestinal digestion were identified by LC‐ESI‐MS/MS using the method of Le et al . Digested samples from the control and glycated samples were mixed with 0.2% (v/v) formic acid in a 1:1 ratio prior to filtration through a 10 kDa cut‐off filter (14 000 × g , 4 °C for 15 min).…”

Section: Lc‐esi‐ms/msmentioning

confidence: 99%

“…Digested peptides after both gastric and gastrointestinal digestion were identified by LC-ESI-MS/MS using the method of Le et al 27 Digested samples from the control and glycated samples were mixed with 0.2% (v/v) formic acid in a 1:1 ratio prior to filtration through a 10 kDa cut-off filter (14 000 × g, 4 ∘ C for 15 min). Then, 10 μL solution was loaded on to an Aeris Peptide C18 column (250 mm × 2.1 mm, 3.6 μm; Phenomenex, Torrance, CA, USA) in an Agilent LC 1200 directly connected to an HCT Ultra ion trap (Bruker Daltonics, Billerica, MA, USA).…”

Section: Lc-esi-ms/msmentioning

confidence: 99%

Digestibility of glycated milk proteins and the peptidomics of their in vitro digests

Zhao

et al. 2019

J Sci Food Agric

View full text Add to dashboard Cite

BACKGROUND Milk proteins are widely used in food production and are often glycated by reducing sugar. Although many studies have reported the digestibility of glycated milk protein, most have focused on measuring degree of hydrolysis (DH), showing sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS‐PAGE) image of digests. Detailed information on the changes in peptide composition of digests has seldom been revealed. Therefore, in addition to measuring the DH and showing the SGS‐PAGE images of digests, we also analyzed the peptidomics in digests using liquid chromatography–electrospray ionization–tandem mass spectrometry (LC‐ESI‐MS/MS) and Mascot database in this work to further reveal the influence of glycation on protein nutrition. RESULTS Compared with β‐lactoglobulin and bovine serum albumin (BSA), DH of β‐casein was suppressed to a lesser extent by glycation in both gastric and intestinal stages. Aggregates of glycated BSA were less sensitive to the action of digestive enzymes throughout gastrointestinal digestion according to SDS‐PAGE images. Changes in the peptide composition of digests induced by glycation were distinctly displayed, showing both absence of peptides and occurrence of new peptides, based on the results obtained from LC‐ESI‐MS/MS. CONCLUSIONS Glycation can greatly change the peptide composition in digests of milk protein. The nutritional impact of the change in the peptide composition requires further investigation, and the impact of MRPs in unabsorbed digests on the gut flora should be an interesting field for further studies. © 2018 Society of Chemical Industry

show abstract

Analytical Methods

2017

High Temperature Processing of Milk and Milk Products

View full text Add to dashboard Cite

Using proteomics to characterise storage-induced aggregates in acidic whey protein isolate drinks

Cited by 27 publications

References 23 publications

Proteomics of major bovine milk proteins: Novel insights

Proteomics of major bovine milk proteins: Novel insights

Digestibility of glycated milk proteins and the peptidomics of their in vitro digests

Analytical Methods

Contact Info

Product

Resources

About