Caseinomacropeptide influences the functional properties of a whey protein concentrate

Svanborg, Sigrid; Johansen, Anne-Grethe; Abrahamsen, Roger K.; Schüller, Reidar Barfod; Skeie, Siv

doi:10.1016/j.idairyj.2015.12.007

Cited by 16 publications

(14 citation statements)

References 43 publications

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“…The pI of sialylated gCMP has previously been reported to be 3.1 as a result of the high degree of sialylation and the low pK a of NeuAc (2.2; Farías et al, 2010). The aCMP is less acidic, and has a pI of approximately 4.0 to 4.15 (Kreuß et al, 2009b;Svanborg et al, 2016). Previous studies have shown that pI decreases 0.07 to 0.31 for each NeuAc residue cleaved off (Barrabés et al, 2010).…”

Section: Short Communicationmentioning

confidence: 97%

Short communication: Application of proteomics for characterization of caseinomacropeptide isoforms before and after desialidation

Sunds

Poulsen

Larsen

2019

Journal of Dairy Science

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Caseinomacropeptide (CMP) is an important polypeptide found in cheese whey that has various biological activities and functional properties. Because sialylations play an important role in the functional properties of CMP, the aim of the present work was to characterize CMP isoform heterogeneity in a commercial glycosylated CMP (gCMP) isolate using liquid chromatography-and gel-based proteomics before and after desialidation. Using 2-dimensional gel electrophoresis (2-DGE), we observed a shift in isoelectric point (pI) after enzymatic desialidation, indicating that sialylated gCMP were located at pI 3.0 to 3.1, but desialylated gCMP had repositioned to pI 3.7 to 3.9. We used liquid chromatography/mass spectroscopy (LC-ESI/MS) for further analysis of the glycan chains of gCMP. In total, we identified 19 CMP isoforms, of which 13 were glycosylated and 6 were nonglycosylated. We also detected 3 genetic variants (A, B, and E), with up to 3 glycosylations attached per gCMP. Further, we identified up to 4 isomers, reflecting different sites of glycosylation in the peptide backbone of these isoforms. The dominating gCMP isoform of genetic variant E appeared to contain 4 N-acetyl-neuraminic acid (NeuAc) residues, whereas the dominating gCMP isoforms of variants A and B appeared to contain 2 NeuAc. The identification revealed conversions of isoforms containing different combinations of genetic variants and degrees of glycosylation, sialylation, and phosphorylation to various desialylated counter-isoforms. The content of sialylated gCMP relative to the total CMP content was 37% (wt/ wt), which decreased to 1.5% after sialidase treatment, indicating 96% effectivity of the desialidation. This approach can be valuable for future functionality studies specifically addressing the importance of NeuAc.

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Section: Short Communicationmentioning

confidence: 97%

Short communication: Application of proteomics for characterization of caseinomacropeptide isoforms before and after desialidation

Sunds

Poulsen

Larsen

2019

Journal of Dairy Science

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“…For example, spherical nanoparticles of CMP and lactoferrin, an iron-binding glycoprotein, can be formed during heating, based on the electrostatic attraction of these two proteins at pH 5.0 (Bourbon et al, 2015); heating CMP or lactoferrin separately produced more branched particles rather than spherical particles. Other authors have shown that a complexation between CMP and the whey proteins occurs during heating, affecting the gelation behaviour and the strength of whey protein gels formed (Martinez, Farías, & Pilosof, 2010;Svanborg, Johansen, Abrahamsen, Schüller, & Skeie, 2016). This interaction depended on the pH of heating and the ratio of CMP to whey proteins.…”

Section: Introductionmentioning

confidence: 93%

Influence of chaperone-like activity of caseinomacropeptide on the gelation behaviour of whey proteins at pH 6.4 and 7.2.

et al. 2021

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“…The caseinomacropeptide or glycomacropeptide (f 106-169) segment of j-CN is composed of glycan chains and has been reported to be resistant to hydrolysis in many studies (Svanborg et al, 2016). The resistance has been attributed to the presence of hydrophilic amino acids and their negative charges which cause increased electrostatic repulsion (Zahraa et al, 2010).…”

Section: Determination Of In Vitro Ace Inhibitory (Acei) Activity In Low Molecular Weight (Lmw) Peptidesmentioning

confidence: 99%

Antihypertensive peptides from whey proteins fermented by lactic acid bacteria

Daliri

Lee

Park

et al. 2018

Food Sci Biotechnol

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In this study, whey proteins were fermented with 34 lactic acid bacteria for 48 h at 37°C and their ability to inhibit angiotensin 1-converting enzyme (ACE) activity were compared. All the lactic acid bacteria displayed varying proteolytic abilities in whey. Their fermentates also displayed varying abilities to inhibit ACE in vitro. Seven fermentates showed strong ACE inhibitory abilities between 84.70 ± 0.67 and 52.40 ± 2.1% with IC 50 values between 19.78 ± 1.73 and 2.13 ± 0.7 mg/ml. Pediococcus acidilactici SDL1414 showed the strongest ACE inhibitory activity of 84.7 ± 0.67% (IC 50 = 19.78 ± 1.73 lg/ml). Mass spectrometry revealed that more than half (57.7%) of the low molecular weight peptides (\ 7 kDa) in the P. acidilactici SDL1414 fermented samples were ACE inhibitory peptides. Our results show that P. acidilactici SDL1414 could be used as a starter culture in the dairy industry to develop antihypertensive functional foods for hypertension management.

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Caseinomacropeptide influences the functional properties of a whey protein concentrate

Cited by 16 publications

References 43 publications

Short communication: Application of proteomics for characterization of caseinomacropeptide isoforms before and after desialidation

Short communication: Application of proteomics for characterization of caseinomacropeptide isoforms before and after desialidation

Influence of chaperone-like activity of caseinomacropeptide on the gelation behaviour of whey proteins at pH 6.4 and 7.2.

Antihypertensive peptides from whey proteins fermented by lactic acid bacteria

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