• Korean Journal of Food Science and Technology
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• v.20 no.2
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• pp.170-175
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• 1988

This experiment was carried out to study the properties of casein micelles obtained from colostral skim milk. As lactation was progressed from parturition until 240h after calving, the content of total protein decreased while the proportion of casein to whey protein increased. Fractionaltion according to the site of casein micelle was done by ultracentrifugation at 100,000 x g for 10 minutes(pellet 1), 30 minutes(pellet 2) and 60 mintes(pellet 3) and the serum casein was prepared by acid precipitation of final supernatant at pH 4.6. During the lactation period, the relative amount of pellet 1(large size) decreased, that of pellet 2(middle size) maintained nearly constant level except for pllet from parturition, that of pellet 3(small size) increased, and the serum casein showed almost constant level. The relative amounts of ${\alpha}_{s1}-casein\;and\;{\alpha}_{s2}-casein\;and\;{\beta}-casein-5P$ in the pellets decreased and that of x-casein increased markedly with decreasing micelle size, but the relative amounts of ${\beta}-casein-1P$(f 29-209), (f 106-209) and (f 108-209) showed little change. The composition of the serum casein was different from that of the skim milk casein.

• Food Science of Animal Resources
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• v.24 no.3
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• pp.273-276
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• 2004

The objective of this study was to investigate the microstructure of folic acid-contained yogurt. Folic acids (25 and 50%) were added to milk preparation prior to pasteurization, then starter culture was added. The microstructure of yogurt containing folic acid was determined by the size of cluster of casein micelle using scanning electron microscopy and transmission electron microscopy. The cluster of casein micelle in yogurt containing folic acid were showed larger size than in control (p<0.05). In addition of 50% of folic acid, cluster of casein micelle per unit area was exhibited the highest number among tested yogurts. From these results, folic acid concentration of yogurt may be affected by mouth-feel of yogurt texture as well as the aggregation of casein micelle.

• Applied Biological Chemistry
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• v.38 no.3
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• pp.254-258
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• 1995

Various artificial casein micelle systems were prepared from dephosphorylated whole casein, ${\beta}$- or ${\kappa}$-casein and their stabilities towards ethanol were assessed. Ethanol stability was lower in the micelle systems with dephesphorylated whole casein as compared to the artificial micelles prepared from native whole casein, and the stability decreased with the extent of dephosphorylation. The casein micelles with partially dephosphorylated ${\kappa}$-casein had a lower ethanol stability than those with native ${\kappa}$-casein. Ethanol stability of the micelle system with dephosphorylated ${\beta}$-casein decreased as the degree of dephosphorylation increased. Progressive dephosphorylation of caseins in skim milk system resulted in a decrease of the stability towards ethanol. The decrease was less than that in the system with dephosphorylated individual caseins. Increase in pH of the artificial casein micelle systems in the range of $6.3{\sim}7.2$ led to an increased ethanol stability manifesting that the presence of serine phosphates contributes significantly to the stability towards ethanol.

• Journal of Dairy Science and Biotechnology
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• v.2 no.1
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• pp.6-16
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• 1982

• Korean Journal of Food Science and Technology
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• v.16 no.3
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• pp.279-284
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• 1984

Microstructure of milk powder and cheese made from milk powder were observed by electron microscope. Freeze dried milk powder showed apple-like appearance. The cheese made from freeze dried milk powder had relatively flat surface and homogenous deposit in compare with classical processed cheese. Imported milk powder also indicated similar surface as well as freeze dried milk powder, however, the cheese made from imported milk powder had somewhat coarse surface structures with the spaces between casein matrix and deposit. Commericial milk powder showed irregular shape in size and coagulum which were possibly denatured in the course of drying. The cheese made from commercial powder indicted irregular and small deposit and porous structure. The porousity of the cheese seemed to be influenced by the degree of heat treatment. Denatured protein would be less dispersive than native in presence of polyphosphates. Fat globule and protein micelle of cheese made from skim milk powder get very adjacent to each other and showed compactness of micelles. It is thought that melting mechanism of skim milk powder was different from the melting of typical processed cheese.

• Bulletin of the Korean Chemical Society
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• v.25 no.7
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• pp.1031-1035
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• 2004

The adsorption kinetics of ${\beta}$-casein on a hydrophobic surface has been studied by means of the quartz crystal microbalance (QCM). The self assembled monolayer of 1-octadecanethiol on a gold coated quartz crystal was used as a hydrophobic surface for adsorption. The adsorption kinetics was monitored in different solution conditions. Formation of monolayer is observed in most cases. At high concentration of protein, micelle formation which is interrupted by high ionic strength of solution is observed. Casein binding cations such as $Ca^{2+},\;Ba^{2+}\;and\;Al^{3+}$ increase the hydrophobicity of the protein and the multiple layer adsorption occurs. The strong and weak points of the QCM method in the study of protein adsorption are discussed.

• Korean Journal of Agricultural Science
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• v.38 no.3
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• pp.459-464
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• 2011

A simplified model for the colloidal calcium phosphate (CCP) nanocluster was developed from an active role of phosphate in the precipitation of casein (CN)/Ca mixtures and the composition of casein micelles (CM). The possible shape of the CCP nanocluster was selected as a tetrahedron, and we estimated that 4 CN molecules were involved in crosslinking a single CCP nanocluster. Similar values were obtained for the number of CN molecules involved in stabilizing the nanocluster when the number of CNs attached onto each nanocluster surface was deduced from the composition of CM. If one phosphoserine cluster consisted of 3 phosphoserine residues, the theoretical molecular weight and volume for the nanocluster were estimated to be 4,898 g/mol and 2.88 $nm^3$, respectively. It was also shown that the position of Ca present in our model were reasonably located to accommodate the serine phosphate in CN molecule.

• Korean Journal of Food Science and Technology
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• v.19 no.1
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• pp.61-65
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• 1987

The milk protein portion contains sialic acid which may be used as an index for k-casein. In comparison with non fat dry milk (NFDM) and calcium caseinate, the solubility of NFDM protein isolates at the various pH was inferior. Another consideration for the low solubility relates to the possibility that k-casein may have been extracted or possibly modified by the action of alcohol. The k-casein is the principal stabilizing fraction for casein micelle and any changes which result in its destruction or removal would be expected to have potent results. During solvent treatment, 16.5% of sialic acid was extracted in the first extraction solvent, whereas the second treatment caused only a 4.0% loss, based on sialic acid analysis. A study was conducted on the effect of concentration of methanol on loss of sialic acid. The loss of sialic acid decreased as the concentration of methanol increased to above 62% in both the first and second extracted solvent. It appears that loss of sialic acid is attributed to the water fraction rather than the methanol fraction. The effect of addition of the dried extracted solids on solubility was investigated. Protein solubility of NFDM protein isolates was sharply increased by 10% addition of the extracted solids and, thereafter, decreased. Efforts to restore solubility by feeding-back the extracted material supported the concept that removal of surface k-casein may have been a possible factor.

• Food Science of Animal Resources
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• v.30 no.4
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• pp.551-559
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• 2010

Among the food constituents, proteins differ in coagulation properties as compared to other constituents in food system. Especially milk protein coagulate through different pathways thus this coagulability can be used for manufacture of various dairy products or as a determinant of dairy product analysis. These milk coagulation methods include organic solvent, isoelectric point, trichloroacetic acid, Ca-sensitive casein, heavy metal ion and rennet coagulation. The coagulation experiment was performed using above parameters at $0^{\circ}C$ and $25^{\circ}C$ to find the dehydration conditions before coagulating for precheese powder making. After different chemical treatments, there was no coagulation at $0^{\circ}C$ rather at $25^{\circ}C$ whatever the mode of coagulation methods was. The appearance of precipitate with coagulation methods was quite different from above mentioned methods of coagulation illustrated by scanning electron microscope. These powders were used for fabrication of camembert cheese by renneting coagulation at $0^{\circ}C$, showing the possibility of cheese materials and of food additives for fabrication of products.

• Journal of Dairy Science and Biotechnology
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• v.35 no.4
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• pp.270-285
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• 2017

Among milk proteins, caseins are not subjected to chemical changes during heat treatment of milk; however, whey proteins are partially denatured following heat treatment. The degree of whey protein denaturation by heat treatment is decreased in the order of high temperature short time (HTST) > low temperature long time (LTLT) > direct-ultra-high temperature (UHT) > indirect-UHT. As a result of heat treatment, several changes, including variations in milk nitrogen, interactions between beta-lactoglobulin and k-casein, variations in calcium sulfate and casein micelle size, and delay of milk coagulation by chymosin action, were observed. Lysine, an important essential amino acid found in milk, was partially inactivated during heat treatment. Therefore, the available amount of lysine decreased slightly (1~4% decrease) after heat treatment, However, the influence of heat treatment on the nutritional value of milk was negligible. Nutritional value and nitrogen balance did not differ significantly between UHT and LTLT in milk. In conclusion, our results showed that heat treatment of milk did not alter protein quality. Whey proteins denatured to a limited extent during the heat treatment process, and the nutritional value and protein quality were unaffected by heat treatment.