Semi‐preparative isolation of phosphopeptides derived from bovine casein and dephosphorylation of casein phosphopeptides

Goepfert, A.; Meisel, Hans

doi:10.1002/food.19960400503

Cited by 9 publications

(8 citation statements)

References 13 publications

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“…A three‐step procedure consisting of solid phase extraction (anion exchange cartridges, QMA), RP‐HPLC (C18) and anion exchange chromatography (QMA) was used to isolate casein phosphopeptide f(1–25)4P from a tryptic hydrolysate of bovine casein as described in [17]. An immobilized alkaline phosphatase (F7m column, Mobitec) was used for the preparation of the dephosphorylated fragment [17].…”

Section: Methodsmentioning

confidence: 99%

“…An immobilized alkaline phosphatase (F7m column, Mobitec) was used for the preparation of the dephosphorylated fragment [17]. Purity of the isolated peptides was checked by analytical RP-HPLC (C18) and amino acid analysis [17], as well as by determination of the N-terminal group by the dansyl chloride method according to [18].…”

Section: Preparation and Puri¢cation Of The Native And Dephosphorylatedmentioning

confidence: 99%

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Post‐translational phosphorylation affects the IgE binding capacity of caseins

et al. 2000

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IgE response specific to those molecular regions of casein that contain a major phosphorylation site was analyzed using native and modified caseins and derived peptides. This study included (i) the naturally occurring common variants A1 and A from L L-and K Ks2-caseins, respectively, which were purified in the native form and then dephosphorylated, (ii) a purified rare variant D of K Ks2-casein which lacks one major phosphorylation site, and (iii) the native and dephosphorylated tryptic fragment f(1^25) from L L-casein. Direct and indirect ELISA using sera from patients allergic to milk showed that the IgE response to caseins is affected by modifying or eliminating the major phosphorylation site.z 2000 Federation of European Biochemical Societies.

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Section: Methodsmentioning

confidence: 99%

Section: Preparation and Puri¢cation Of The Native And Dephosphorylatedmentioning

confidence: 99%

Post‐translational phosphorylation affects the IgE binding capacity of caseins

et al. 2000

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“…Starting from CN, the overall preparation process gave 16% CPP (Figure 10), less than the theoretical yield of 23% (Ytheor =22.8%), which means approximately 20% yield on the basis of weight, a yield higher than that obtained by other researchers [138][139][140]. In their production The example of 2000 L Na-caseinate solution containing 180 kg protein and 1 kg trypsin yielded 29 kg of calcium-enriched CPP, corresponding to a yield of ~16% (w/w) [141].…”

Section: Examples Of Industrial Methods For Cpp Preparationmentioning

confidence: 71%

Bioactive Casein Phosphopeptides in Dairy Products as Nutraceuticals for Functional Foods

Pinto¹,

Caira²,

Cuollo³

et al. 2012

Milk Protein

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“…Because of this sequence, these CCPs are hardly retained on IEC column and can be present in the peak of SerP. Most of them are probably dephosphorylated by attack of alkaline phosphatase as recently reported by Goepfert and Meisel [26] for tryptic CPPs. As a consequence, the peptides can be fully hydrolysed by the pool of enzymes, causing increase of the values of Ser and Glu and disappearence of the peak of SerP.…”

Section: Enzymatic Hydrolysis Of Caseinmentioning

confidence: 78%

About presence of free phosphoserine in ripened cheese and in enzymatic hydrolysate of casein

Noni

Pellegrino

Resmini

et al. 1997

Nahrung

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Occurrence of free phosphoserine (SerP) in ripened cheeses was investigated to clarify whether this amino acid can be directly released from casein by enzymatic attack. Free amino acids extracted from cheese were separated by IEC or RP-HPLC and the peak of SerP always eluted close to unretained material and acidic components. Presence of these interferences suggests that the content of free SerP (from 0.8 to 16.4 mmoleskg cheese) could be highly overestimated. These figures were dramatically lowered (up to 100 times) after a purification step of the cheese extract on cationic column, but the chromatographic separation of SerP was not yet interference-free. However, these values of free SerP are not significant on the basis of the total amount of free amino acids (~0.06%). The interfering compounds were characterized in Grana Padano cheese by FAB-MS and several low-MW peptides were found, the most abundant of which was the casein phosphopeptide (CPP) p( 16-22)3P. In vitro enzymatic hydrolysis of casein confirmed that accumulation of short-chain CPPs having the common structure X-SerP-SerP-SerP-Glu-Glu-X occurs, explaining incomplete recovery of the amino acids. The recovery increased from 89% up to 96% and the content of Ser and Glu approached the theoretical value when the enzymatic hydrolysis was performed in presence of alkaline phosphatase.These data are consistent with splitting of Ser and not of SerP from casein by enzymatic attack and with accumulation of only free Ser in cheese ripening. Because of the accumulation of "enzyme-resistant" CPPs, in vitro enzymatic hydrolysis of casein can be completed when alkaline phosphatase is included in the pool of enzymes.

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Semi‐preparative isolation of phosphopeptides derived from bovine casein and dephosphorylation of casein phosphopeptides

Cited by 9 publications

References 13 publications

Post‐translational phosphorylation affects the IgE binding capacity of caseins

Post‐translational phosphorylation affects the IgE binding capacity of caseins

Bioactive Casein Phosphopeptides in Dairy Products as Nutraceuticals for Functional Foods

About presence of free phosphoserine in ripened cheese and in enzymatic hydrolysate of casein

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