Disorder in Milk Proteins: Formation, Structure, Function, Isolation and Applications of Casein Phosphopeptides

Naqvi, Muhammad Ali; Irani, Kimia Anaraki; Katanishooshtari, Maryam; Rousseau, Dérick

doi:10.2174/1389203717666151201191658

Cited by 10 publications

(4 citation statements)

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“…In the 90th minute, high molecular peptide fractions are absent ( Figure 6). Similar results with a large number of various low molecular weight phosphopeptides are described in other scientific researchs [21,22]. Figure 6.…”

Section: Gel Filtration and Electrophoresis Of Proteolysis's Productssupporting

confidence: 88%

Characteristics of proteolytic processes during the isolation of natural casein phosphopeptides

Yukalo¹,

Krupa²

2019

Ukr. food j.

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Introduction. The aim of this work is studying of the proteolytic processes features in the production of natural phosphopeptides of the milk casein complex. Materials and methods. Casein substrate was isolated by isoelectric sedimentation from skimmed milk. Proteolysis was performed using pancreatin. The degree of proteolysis was determined spectrophotometrically by the absorption of low molecular weight products of proteolysis at λ = 280 nm. The yield of phosphopeptides was determined gravimetrically after precipitation with ethanol in the presence of calcium ions. Electrophoresis of phosphoproteins of the substrate and products of proteolysis was carried out in an alkaline system of homogeneous polyacrylamide gel in the presence of urea. Results and discussion. Natural phosphopeptides were obtained by proteolysis of the phosphoproteins of the casein complex with pancreatin (E:S = 1:100) under physiological conditions (37° C, pH 7.9). At different stages of proteolysis, the yield of phosphopeptides and peptides soluble in 10% trichloroacetic acid was determined. Degree of proteolysis has increased monotonically throughout the studied period. The yield of phosphopeptides reaches its maximum in the 90th minute of proteolysis and then decreases continuously. The yield of phosphopeptides is lower than it was used proteolytic preparations of microbial origin. The results obtained by gel filtration and electrophoresis in a polyacrylamide gel indicate that a decrease in the yield of phosphopheptides after the 90th minute of proteolysis may be caused by the phosphopeptide's molecular weight decrease. Most of phosphopeptides obtained in the 90th minute of proteolysis have a molecular weight up to 2000 Da, which is characteristic for the already known biologically active phosphopeptides. Conclusions. During the proteolysis of casein with pancreatin in physiological conditions, the total yield of proteolysis products increases monotonously. The yield of phosphopeptides has maximum. Gel filtration and electrophoresis data indicate that this is due to a decrease in the molecular mass.

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Section: Gel Filtration and Electrophoresis Of Proteolysis's Productssupporting

confidence: 88%

Characteristics of proteolytic processes during the isolation of natural casein phosphopeptides

Yukalo¹,

Krupa²

2019

Ukr. food j.

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“…Gaucheron et al 31 estimated that cations are bound to α-casein and β-casein in the following affinity order: Fe > Zn > Ca. Zinc was found with 3 CPP (casein phosphopeptide) and the fraction containing α-casein and the 3 CPPs containing amino acids (glutamic acid, serine and phosphoserine), showing the Zn-complexes formation 23,32 . Moreover, the Zn distribution between casein, whey and other components may be affected by pH, heat and other cations present in the diet.…”

Section: Samples / Kdamentioning

confidence: 97%

“…Naqvi et al 23 reported that it was also possible to observe that Ca, Fe, Mg and Zn were mainly associated with colloidal calcium phosphate in casein micelles. For soybeans, 80% of the extracted proteins are βconglycine (7S) and glycine (11S).…”

Section: Gel Electrophoresismentioning

confidence: 99%

Zinc fractionation in cow, goat, sheep and soybean milk samples using gel-electrophoresis and determination by electrothermal atomic absorption spectrometry (ETAAS)

et al. 2021

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A screening method for zinc levels in different milk samples (raw cow, raw sheep, UHT cow, UHT goat and soybean milk base) was performed to establish the Zn levels’ differences in protein samples. The samples were digested in a cavity microwave oven and the total Zn levels in the extracts were determined by flame absorption atomic spectrometry (FAAS). The protein separation was performed by urea polyacrylamide gel electrophoresis (UREA-PAGE). Protein bands were digested in the cavity microwave oven and Zn-protein analysis was further conducted by electrothermal atomic absorption spectrometry (ETAAS). The results showed that Zn is mainly bound to 32 kDa (β-casein) protein (17.0 ± 2.0%) in UHT cow and 24 kDa (α-casein) protein (9.0 ± 0.6%) in raw sheep milk. This method provided quantitative information regarding Zn species present in the protein fractions of the milk samples. The accuracy was evaluated using certified reference material (whole milk powder, NIST 8435) with statistically equivalent concentrations (Student’s t-test) for total Zn and by addition and recovery experiments applied to measure Zn-protein. The recovered values were in the 92-110% range.

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“…This is why the NaCasstabilized emulsion can be formed and broken within 1 min. Furthermore, the phosphoserine clusters can dynamically bind to the positive ions to form a positively charged layer around the localized micelles, serving as a vehicle for capturing ions, [33][34][35] providing theoretical support for strong salt tolerance, and thus contributing to the indenitely reversible pH-responsive cyclability ( Fig. S7 †) that cannot be found in other common proteins.…”

Section: Andmentioning

confidence: 99%

Sodium caseinate as a particulate emulsifier for making indefinitely recycled pH-responsive emulsions

Liu

Jiang

et al. 2020

Chem. Sci.

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Disorder in Milk Proteins: Formation, Structure, Function, Isolation and Applications of Casein Phosphopeptides

Cited by 10 publications

References 0 publications

Characteristics of proteolytic processes during the isolation of natural casein phosphopeptides

Characteristics of proteolytic processes during the isolation of natural casein phosphopeptides

Zinc fractionation in cow, goat, sheep and soybean milk samples using gel-electrophoresis and determination by electrothermal atomic absorption spectrometry (ETAAS)

Sodium caseinate as a particulate emulsifier for making indefinitely recycled pH-responsive emulsions

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