• 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 the Korean Society of Food Science and Nutrition
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• v.33 no.8
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• pp.1359-1366
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• 2004

Ultra high temperature treated (UHT) skim milk and colloidal calcium phosphate-free skim milk were treated with microbial transglutaminase (TGase), ultracentrifuged at various rates, lyophilized, and observed for morphological properties with a scanning electron microscope (SEM). UHT skim milk showed small holes of associated micelles at lower centrifugal rates, and became thick and irregular, and fine particles were associated regularly at higher centrifugal rates. When UHT skim milk with TGase was incubated for 1 hour, casein micelles aggregated and broadened as centrifugation rate increased. When UHT skim milk with TGase was incubated for 8 hours, casein micelles were associated irregularly to large aggregates and widened. Colloidal calcium phosphate-free skim milk with TGase incubated for 1 hour and separated by two-step centrifugation showed aggregated lump, while the milk incubated for 8 hours with TGase was associated with broadened, compact, and regular layers as the centrifugation rate increased. Such phenomena were caused by heat treatment, protein crosslinking reaction catalyzed by TGase and conformational changes of casein molecules, and could be dependent on reaction time, temperature and ultracentrifugation rate.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.21 no.1
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• pp.53-66
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• 1995

The gene for ${\gamma}$-casein, a milk protein, is a member of a family of casein gene which is expressed in mammary glands of the animal during the late gestation and lactation periods binder the influence of various hormones. In order to elucidate tile mechanisms b)'which hormones regulate the coordinate induction of milk protein genes, the mouse ${\gamma}$-casein gene was isolated and characterized. The ${\gamma}$-casein gene was screened from a mouse genomic library constructed in bacteriophage EMBL3 with the ${\gamma}$-casein CDNA used as probe and one clone was obtained. The ${\gamma}$-casein CDNA as probe was partially sequenced and contained ATG start codon and 5'-noncoding region. The cloned genomic DNA was digested with Sal I restriction enzyme, by which the insert DNA can be isolated from EMBL3 vector. Three DNA bands were observed and the size of DNAs was approximately 28kb, 14kb and 9Kb, respectively Accordingly the size of the insert DNA was calculated with approximately 23Kb. The result of Southern blot analysis, however, showed that the cloned genomic DNA was not hybridized with the synthetic oligonucleotides (40 mer) of cDNA 5'-end region, but it was hybridized with the y -casein CDNA. This means that tile cloned y -casein gene may not contain its promoter region. The ${\gamma}$ -casein genomic DNA containing the promoter region has been screening from mouse genomic library with oligonucleotides of CDNA 5'-end region as probe, and twenty-nine clones was obtained.

• Journal of the Korean Geotechnical Society
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• v.35 no.1
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• pp.31-42
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• 2019

About 3% of Casein is included in milk and it accounts for 80% of milk's protein. It has an adhesive property when mixed with calcium hydroxide and sodium hydroxide solutions. It has been usually used to bond woods under dry condition but becomes weak when exposed to moisture. Such weakness is very critical when casein is applied for soil cementation under groundwater condition. Therefore, this study was aimed to protect such weakness by changing or adding certain ingredients of casein adhesive. Two types of cemented specimens were prepared with Nakdong river sand and tested for unconfined compressive strength and durability. Each specimen was mixed with casein or cement. Ingredients of casein binder suggested by the University of Wisconsin, which is called a standard casein recipe, was also prepared. This study tried 6 different types of casein binder recipe. Among them, one with 30% hydroxide calcium increase and 50% hydroxide sodium decrease compared with the standard casein was most effective. Based on the most effective casein recipe, cemented sand with 1-4% of casein ratio was prepared and tested. The unconfined compressive strength and durability index were 6,253kPa and 92% for the specimen with 4% of casein ratio and 1,500kPa and 62% for the one with 8% of cement ratio. Therefore, casein cemented sand showed better performance. In addition, over 3% of casein cemented sand had over 80% durability index.

• Food Science of Animal Resources
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• v.23 no.4
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• pp.350-355
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• 2003

Raw skim milk and colloidal calcium phosphate-free skim milk were treated with microbial transglutaminase (TGase), ultracentrifuged at varying rates and were observed to contain textural properties using a scanning electron microscope (SEM). Skim milk showed irregular signs of conformation at lower centrifugal rate, and associated regular (10,000 ${\times}$g) and thin with broad holes (20,000 ${\times}$g). The associated texture became thick and irregular (40,000 ${\times}$g), and fine particles were regularly associated (100,000 ${\times}$g). When skim milk was incubated for 1 hr with TGase, casein micelles aggregated and broadened as centrifugation rate increased. When skim milk was incubated for 8 hrs with TGase, casein micelles associated to large widened aggregates, and were associated regularly which then became irregular (100,000 ${\times}$g). When colloidal calcium phosphate-free skim milk incubated for 1 hr with TGase showed no sediment, the milk incubated for 8 hrs with TGase associated together, yielding broadened and regular layers as the centrifugation rate increased. It is assumed that such phenomena could be caused by protein crosslinking reaction with TGase and conformational change of casein molecules, as well as dependencies on reaction time, temperature and ultracentrifugation rate.

• Korean Journal of Food Science and Technology
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• v.32 no.6
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• pp.1433-1436
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• 2000

The effect of addition of pectin on the stability of casein solution was studied to apply casein-pectin mixture to apple juice. The solubility of 0.1% casein solution was below 20% at pH 3-5. However, the solubility of 0.1% casein-0.1% pectin mixtures was over 70% at pH 2-10. The increase in the concentration of casein-pectin mixture showed adverse effect on the solubility. The apple juice (pH 3.4), containing 0.1-0.5% casein-pectin mixtures, remained stable without the precipitation of casein. The stability of apple juice including casein-pectin mixture was maintained upon heating at $100^{\circ}C$ for 10 minutes or refrigerating for a week. This study suggested the possibility of protein fortification to acidic beverages since casein-pectin mixture maintained stability in apple juice.

• Korean Journal of Food Science and Technology
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• v.30 no.5
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• pp.1035-1039
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• 1998

Phase separation is the typical phenomenon in protein-polysaccharide mixtures because of thermodynamic incompatibility between two macromolecules. Phase separations of casein-alginate-water systems were investigated by using phase diagram under varying pH (6, 8 and 10) and NaCl concentrations (0, 0.25 and 0.5 M). Incompatibility decreased with increasing pH and decreasing NaCl concentration. Molecular weight of alginates did not significantly affect the phase diagram of casein-alginate-water systems. The results strongly suggested that compatibility of casein and alginate involved electrostatic interactions.

• Journal of the Korean Applied Science and Technology
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• v.29 no.4
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• pp.618-625
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• 2012

In this study, prepared synthesis waterborne acrylic resin and water soluble milk casein resin. And than extent of casein contents in acrylic resin. We measured property of these samples by Lamb leather which is coated by acrylic-casein resins. According to measure data for solvent resistance, WAR resin and Hybrid resins had good property. Among this result knew that increase of casein constant did not influence to big change of hybrid resin property. As test of tensile strength, WAR had lowest strength($1.399kg_f/mm^2$) and WAC-3 had highest strength($1.426kg_f/mm^2$). Also we knew that best property of abrasion was WAC-3(69.774 mg.loss). In elongation case, WAR had best property(820%) in this experiment.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2005.10a
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• pp.177-181
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• 2005

근원섬유 단백질에 카제인염을 첨가함으로써 유화안정성이나 보수력을 증진시킬 수 있으나 가제인염은 열에 안정성이 떨어지는 단점을 가지고 있다. TGase가 이러한 카제인염의 단점을 보완해주는지 알아보기 위해 열량분석기와 전기영동을 이용하여 단백질의 변화를 측정하였다. 열량분석기의 경우 근원섬유 단백질과 카제인 염 단백질의 상호교차결합을 TGase의 첨가유무에 따라 실시하였으며 그 결과 TGase의 첨가는 각 단백질 열량변화가 나타나는 온도를 변화시켰으며 배양시간을 증가할수록 각 단백질별 열량변화의 차이를 보였고 peak의 크기에도 차이를 보였다. 또한 전기영동의 경우 MFP, SC, MFP:SC의 1:1 혼합액을 각각을 TGase 첨가한 것과 하지 않은 것을 비교한 결과, TGase의 첨가는 고분자 polymer를 만들어줌으로써 두 단백질간의 상호작용에 촉매제로써 작용한다는 것을 확인하였다.

• Journal of Animal Science and Technology
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• v.44 no.4
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• pp.483-490
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• 2002

The aim of this study was to determine if a low-molecular weight casein hydrolysate has an anti- hypertensive effect in spontaneously hypertensive rats (SHR). Prior to the in vivo experiment, the casein hydrolysate was confirmed to be resistant to gastrointestinal digestion by confirming the retention of its potency as an inhibitor of angiotensin I-concerting enzyme after incubation with pepsin, trypsin, or chymotrypsin. The in vivo anti-hypertensive effect of the hydrolysate was determined by the tail cuff method. Following an oral administration of the hydrolysate solution, the systolic blood pressure (SBP) decreased by 12.9% (－28.9mmHg; P<0.05) at 3 h after the administration at a dose of 500mg/kg body weight. When the hydrolysate was administered as an emulsion with 30% egg yolk, its anti-hypertensive effect was even more greater at the same dose(－30.8mmHg or －15.9%; P<0.01). In a 50-day long-term trial where the casein hydrolysate was administered once a day, the SBP-lowering effect of the hydrolysate was apparent (P<0.05) from day 35 through the end. Moreover, organ weights and plasma glutamate oxaloacetate transaminase and glutamate pyruvate transaminase activities of the administered SHR were not significantly different from those of controls at the end of the long-term trial.