Effect of Dephosphorylation of Casein on Its Coagulation and Proteolysis by Chymosin

Yamauchi, Kunio; Yoneda, Yoshiki

doi:10.1080/00021369.1978.10863103

Cited by 4 publications

(4 citation statements)

References 8 publications

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“…A decrease in rennet curd strength was observed following partial dephosphorylation of AMM and the incorporation of dephosphorylated or partly dephosphorylated /?-casein into AMM. This supports the proposal by Yamauchi & Yoneda (1978) and Yun et al (1982) that the phosphate groups of casein, particularly those of /?-casein, contribute to the development of curd strength. In the current investigation, dephosphorylation was observed to affect both RCT and curd strength which is consistent with the observations of Reimerdes & Roggenbuck (1980).…”

Section: Discussionsupporting

confidence: 90%

“…Reimerdes & Roggenbuck (1980) observed an increase in RCT, but an even greater reduction in rennet curd strength following the partial dephosphorylation of casein micelles. Yamauchi & Yoneda (1978) on the other hand, prepared artificial milk by the method of Grindrod et al (1956) from native and dephosphorylated casein and found that the RCT were similar but that the curd strength was reduced following dephosphorylation. The reason for this variation is not clear, however it may in part be attributable to the different experimental systems used.…”

mentioning

confidence: 99%

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Effect of casein micelle composition and casein dephosphorylation on coagulation and syneresis

Pearse¹,

Linklater

Hall

et al. 1986

Journal of Dairy Research

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SUMMARYThe effect of varying the casein composition of artificial micelle milk on rennet coagulation time and syneresis was examined in order to determine whether either of these processes is dependent on the concentration of particular casein components. It was found that the levels of κ-and β-caseins had a significant effect on coagulation, whereas syneresis was only affected by the level of β-casein. Partial dephosphorylation of preformed micelles or the incorporation of dephosphorylated or partly dephosphorylated β-casein into artificial micelle milk was found to have an adverse effect on both coagulation and syneresis. It was concluded that the phosphate groups of casein, particularly those of β-casein, are directly involved in the micelle-micelle interactions which occur during coagulation and syneresis.

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Section: Discussionsupporting

confidence: 90%

mentioning

confidence: 99%

Effect of casein micelle composition and casein dephosphorylation on coagulation and syneresis

Pearse¹,

Linklater

Hall

et al. 1986

Journal of Dairy Research

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“…The determination of peak areas indicated that more 3% TCA-soluble peptides were obtained from dephosphorylated β-casein (30% increase). Plasminolysis accelerates with dephosphorylation as reported for chymosin and pepsin digestion [29,36]. The removal of phosphate groups from a peptide should increase its hydrophobicity and hence its retention time in reverse phase chromatography.…”

Section: Rp-hplc Of the 3% Tca-soluble Peptidesmentioning

confidence: 99%

Plasmin digestion of bovine ?-casein dephosphorylated with one protein phosphatase type 2A purified from Yarrowia lipolytica

Jolivet¹,

Macedo

Wu³

et al. 2000

Lait

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Bovine β-casein was dephosphorylated by the catalytic sub-unit of a type 2A protein phosphatase (PP2Ac) purified from the yeast Yarrowia lipolytica. Complete dephosphorylation was obtained after 24 to 30 h in Tris buffer (pH 7.5). On the contrary, the activity of PP2Ac was largely inhibited (80%) in the presence of 13 mmol⋅L-1 sodium citrate (pH 6.8). After dephosphorylation of β-casein, plasminolysis was increased and more 3% TCA-soluble peptides were obtained (30% increase). Dephosphorylation led to the disappearance of the f 29-105/107 peptide and to the appearance of a new non-phosphorylated 8 200 g. mol-1 peptide, suggested to be f 33-105/107 originated from the middle part of the β-casein sequence and obtained upon plasmin cleavage of the Lys 32-Phe 33 peptide bond. β-casein / dephosphorylation / protein phosphatase / Yarrowia lipolytica / plasmin Résumé-Hydrolyse par la plasmine de la caséine β bovine déphosphorylée par une protéine phosphatase de type 2A purifiée chez Yarrowia lipolytica. La caséine β peut être déphosphorylée par la sous-unité catalytique d'une protéine phosphatase de type 2A purifiée chez la levure Yarrowia lipolytica. La déphosphorylation complète est obtenue en 24 à 30 h en tampon Tris (pH 7.5). À l'inverse, elle est largement inhibée par le citrate de sodium 13 mmol. L-1 à pH 6.8 (80 % d'inhibition). Après déphosphorylation, la plasminolyse de la caséine β est augmentée puisque l'on observe une production supplémentaire de 30 % de peptides solubles dans le TCA à 3 %. La déphosphorylation se traduit par la disparition du peptide f 29-105/107 et l'apparition d'un nouveau peptide non phosphorylé de 8 200 g. mol-1. Il pourrait s'agir du peptide f 33-105/107 provenant de la partie centrale de la séquence protéique de la caséine β et obtenu par attaque de la liaison peptidique Lys 32-Phe 33. caséine β / déphosphorylation / protéine phosphatase / Yarrowia lipolytica / plasmine

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“…However, the importance of bound P, particularly organic P, in defining cheese characteristics has been studied to a lesser extent. Studies conducted on caseins have indicated that organic P is important for several functional interactions in food systems in which caseins are involved (Yamauchi and Yoneda, 1978;Van Hekken and Strange, 1993;Van Hekken et al, 1996). It appears that a hindrance in investigating the influence of organic P or bound Ca on cheese characteristics is the cumbersome analytical methods used for measuring these constituents in cheese.…”

Section: Introductionmentioning

confidence: 99%

Utilization of Fourier Transform Infrared Spectroscopy for Measurement of Organic Phosphorus and Bound Calcium in Cheddar Cheese

Upreti

Metzger

2006

Journal of Dairy Science

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The methods available for measuring organic P and bound Ca in cheese are either cumbersome or involve dilution of the cheese. Dilution of the cheese can lead to erroneous results, particularly in the case of bound Ca. Hence, the objective of this study was to evaluate the feasibility of Fourier transform infrared (FTIR) spectroscopy for direct measurement of organic P and bound Ca in Cheddar cheese. Two hundred sixteen samples of cheese were analyzed for protein-bound organic P, bound Ca using a water-extraction based method, and buffering curves. Additionally, the infrared spectra of the cheeses were collected between 4,000 and 650 cm(-1), at a resolution of 4 cm(-1), and 256 scans per sample. The spectral shifts in the infrared region from 1,050 to 900 cm(-1), in addition to the measured concentrations of organic P, bound Ca, and buffering peak area at pH 5.1, were used to develop calibration models using partial least squares (PLS) regression analysis. The spectral region of 956 to 946 cm(-1) correlated with the measured concentrations of organic P and the overall PLS model had a correlation (R2) of 0.76 between the predicted and measured concentrations. The spectral region at approximately 980 cm(-1) was correlated with the measured concentrations of bound Ca, and the overall PLS model had a correlation (R2) of 0.70 between the predicted and measured concentrations. A similar spectral region at approximately 980 cm(-1) was also correlated with the measured buffering peak areas and the overall PLS model had a correlation (R2) of 0.64 between the predicted and measured peak areas. A linear regression analysis between the bound Ca and buffering peak area demonstrated that bound Ca was correlated (R2 = 0.73) with buffering peak area. This study demonstrates that FTIR can be used to measure organic P in cheeses. It also has the potential to be used for measuring bound Ca in undiluted cheeses, and for prediction of the buffering capacity of cheese.

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Effect of Dephosphorylation of Casein on Its Coagulation and Proteolysis by Chymosin

Cited by 4 publications

References 8 publications

Effect of casein micelle composition and casein dephosphorylation on coagulation and syneresis

Effect of casein micelle composition and casein dephosphorylation on coagulation and syneresis

Plasmin digestion of bovine ?-casein dephosphorylated with one protein phosphatase type 2A purified from Yarrowia lipolytica

Utilization of Fourier Transform Infrared Spectroscopy for Measurement of Organic Phosphorus and Bound Calcium in Cheddar Cheese

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