• Title/Summary/Keyword: kappa-casein

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Study on the Analysis of β-lactoglobulin and κ-casein Genotypes of Cattle using Polymerase Chain Reaction (PCR 기법을 이용한 축우의 β-lactoglobulin 및 κ-casein 유전자형 분석에 관한 연구)

  • Sang, Byung Chan;Ryoo, Seung Heui;Lee, Sang Hoon;Song, Chi Eun;Nam, Myung Soo;Chon, Byung Soon
    • Korean Journal of Agricultural Science
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    • v.25 no.2
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    • pp.216-224
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    • 1998
  • This study was performed to offer the basic and applicable data for improvement of Korean cattle and dairy cattle, according to finding the genetic construction obtained from analysis of genetic polymorphisms of ${\beta}$-lactoglobulin and ${\kappa}$-casein loci related Korean cattle and Holstein cows using PCR-RFLP. Genomic DNA used in this study was prepared from the blood of 253 individuals of Korean cattle in Korean Native Cattle Improvement Center, NLCF, and the blood of 113 individuals of Holstein cows in National Livestock Research Institute. The results obtained are summarized as follows : 1. This study confirmed amplified products of 530bp and 262bp fragments obtained from the amplification of ${\beta}$-lactoglobulin and ${\kappa}$-casein loci in Korean cattle and Holstein breed by PCR. 2. The ${\beta}$-lactoglobulin AA genotype showed 153bp and 109bp fragments, and ${\beta}$-lactoglobulin AB genotype showed 153bp, 109bp, 79bp and 74bp fragments, and BB genotype showed 109bp, 79bp and 74bp fragments in amplified products of ${\beta}$-lactoglobulin loci with the restricted enzyme digestion of Hae III. 3. The ${\kappa}$-casein AA genotype showed a 530bp fragment, and ${\kappa}$-casein AB genotype showed 530bp, 344bp and 186bp fragments, and BB genotype showed 344bp and 186bp fragments in amplified products of ${\kappa}$-casein loci with the restricted enzyme digestion of Taq I. 4. On ${\beta}$-lactoglobulin genotypes and gene frequencies, Korean cattle were 6.72%, 26.09% and 67.19% for AA, AB and BB genotypes, and ${\beta}$-lactoglobulin A and B alleles were 0.197 and 0.803, and Holstein were 35.40%, 56.64% and 7.96% for AA, AB and BB genotypes, and ${\beta}$-lactoglobulin A and B alleles were 0.637 and 0.363, respectively. 5. On ${\kappa}$-casein genotypes and gene frequencies, Korean cattle were 46.25%, 39.13% and 14.62% for AA, AB and BB genotypes, and ${\kappa}$-casein A and B alleles were 0.658 and 0.342, and Holstein were 60.18% and 38.94% and 0.88% for AA, AB and BB genotypes, and ${\kappa}$-casein A and B alleles were 0.796 and 0.204, respectively. 6. As a consequence, the gene frequency was 0.197 and 0.803 for ${\beta}$-lactoglobulin A and B alleles, and 0.658 and 0.342 for ${\kappa}$-casein A and B alleles in Korea cattle, but was 0.637 and 0.363 for ${\beta}$-lactoglobulin A and B alleles, and 0.796 and 0.204 for ${\kappa}$-casein A and B alleles in Holstein, respectively.

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Effect of Casein Dephosphorylation on Stability of Casein Micelles towards Ethanol (카제인의 탈인산화가 카제인 미셀의 에탄올 안정성에 미치는 영향)

  • Shin, Weon-Sun;Moon, Tae-Wha
    • 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.

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Effects of Genetic Variants of κ-casein and β-lactoglobulin and Heat Treatment on Coagulating Properties of Milk

  • Choi, J.W.;Ng-Kwai-Hang, K.F.
    • Asian-Australasian Journal of Animal Sciences
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    • v.16 no.8
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    • pp.1212-1217
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    • 2003
  • Fifty-two Holstein cows with different phenotypes of $\kappa$-casein ($\kappa$-CN) and $\beta$-lactoglobulin ($\beta$-LG) were selected to provide weekly milk samples for heating at 30, 70, 75 and $80^{\circ}C$ for 2 min. Coagulating properties of heated milk samples measured as rennet clotting time, rate of curd firming and curd firmness at cutting were determined by a Formagraph. Milk samples were analysed for fat and casein. Least squares analyses of data, after adjustments were made for effect of milk casein and fat contents, indicated that although an increase in heating temperatures resulted in less desirable coagulating properties, the effect of milk types was inherent irrespective of heating temperatures. The shortest rennet clotting time (6.06 min), fastest rate of curd firming (5.61 min) and firmest curd (38.05 mm) were obtained from milk with the B variant for $\kappa$-CN and B variant for $\beta$ -LG when preheated at $30^{\circ}C$. It appears that milk bearing $\kappa$-CN B is more resistant to heat perturbation. All milk samples having the $\kappa$-casein AA (milk types AA/AA, AA/AB, AA/BB) did not have a measurable K20 value when preheated at $70^{\circ}C$. This effect was observed for $\kappa$-casein AB (milk types AB/AA, AB/AB, AB/BB) at $75^{\circ}C$ and $\kappa$-casein BB (milk types BB/AA, BB/AB, BB/BB) at $80^{\circ}C$.

The effects of human milk proteins on the proliferation of normal, cancer and cancer stem like cells

  • Kang, Nam Mi;Cho, Ssang-Goo;Dayem, Ahmed Abdal;Lee, Joohyun;Bae, Seong Phil;Hahn, Won-Ho;Lee, Jeong-Sang
    • Analytical Science and Technology
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    • v.31 no.6
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    • pp.232-239
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    • 2018
  • Human breast milk (HBM) provides neonates with indispensable nutrition. The present study evaluated the anti-cancer activity of diluted and pasteurized early HBM (< 6 weeks' lactation) on human breast cancer cell lines. The cell lines MCF7 and MDA-MB231 were exposed to 1 % HBM from the 1st, 3rd, and 6th weeks of lactation and exhibited reduced proliferation rates. As controls, breast cell lines (293T and MCF-10A), breast cancer cell lines (MCF-7 and MDA-MB-231), and $CD133^{hi}CXCR4^{hi}ALDH1^{hi}$ patient-derived human cancer stem-like cells (KU-CSLCs) were treated with prominent milk proteins ${\beta}$-casein, ${\kappa}$-casein, and lactoferrin at varying doses (10, 50, and $100{\mu}g$) for 24 or 48 hrs. The impact of these proteins on cell proliferation was investigated. Breast cancer cell lines treated with ${\kappa}$-casein and lactoferrin exhibited significantly reduced viability, in both a dose- and time-dependent manner. Interestingly, ${\kappa}$-casein selectively impacted only cancer (but not normal breast) cell lines, particularly the more malignant cell line. However, ${\beta}$-casein-exposed human breast cancer cell lines exhibited a significantly higher proliferation rate. Thus, ${\kappa}$-casein and lactoferrin appear to exert selective anti-cancer activities. Further studies are warranted to determine the mechanisms underlying ${\kappa}$-casein- and lactoferrin-mediated cancer cell-selective cytotoxic effects.

The Relationship between Milk Protein Phenotypes and Lactation Traits in Brown Swiss and Canadienne

  • Kim, S.;Ng-Kwai-Hang, K.F.;Hayes, J.F.
    • Asian-Australasian Journal of Animal Sciences
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    • v.11 no.3
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    • pp.311-317
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    • 1998
  • A total of 1033 Brown Swiss and 610 Canadienne cows were phenotyped for the genetic variants ${\alpha}_{s1}$-casein, ${\beta}$-casein, ${\kappa}$-casein, ${\beta}$-lactoglobulin and ${\alpha}$-lactalbumin. In Brown Swiss, frequency distributions were: 97.3% B and 2.7% C variant of ${\alpha}_{s1}$-casein; 31.6% $A^1$, 51.8% $A^2$, 0.5% $A^3$ and 16.1% B variant of ${\beta}$-casein; 70.4% A, 29.3% B, and 0.3% C variant of ${\kappa}$-casein; 41.7% A and 58.3% B variant of ${\beta}$-lactoglobulin; and 100% B variant of ${\alpha}$-lactalbumin. Corresponding frequencies in Canadienne for those five milk proteins were: 98.6 and 1.4%;58.5, 33.5, 0.08 and 7.9%; 78.8, 21.1 and 0.1%, 42.4 and 57.6%; and 100%. Analysis of variance by least squares showed possible association between milk protein phenotypes and some lactational production traits. There were no significant association of phenotypes of ${\alpha}_{s1}$-casein, ${\beta}$-casein and ${\beta}$-lactoglobulin with milk yield, fat yield, protein yield, fat percentage and protein percentage in both breeds during the three lactations. In the Brown Swiss, ${\kappa}$-casein phenotype was associated with 305-day fat yield and protein yield during the first lactation. ${\kappa}$-Casein AB was associated with higher milk, fat and protein yield during the second lactation. During the third lactation, ${\beta}$-lactoglobulin AA in Canadienne cows was associated with higher protein content in the milk (3.70%) when compared to phenotypes AB (3.54%) and BB (3.64%).

MILK PROTEIN POLYMORPHISMS AS GENETIC MARKER IN KOREAN NATIVE CATTLE

  • Chung, E.R.;Han, S.K.;Rhim, T.J.
    • Asian-Australasian Journal of Animal Sciences
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    • v.8 no.2
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    • pp.187-194
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    • 1995
  • Genetic variants of ${\alpha}s_1$-casein, ${\beta}$-casein, ${\kappa}$-casein and ${\beta}$-lactoglobulin were investigated by starch urea gel electrophoresis in milk samples of 280 Korean native cattle. A new ${\beta}$-casein variant, designated ${\beta}$-casein $A^4$, was found in milk samples of Korean native cattle. It has a much slower electrophoretic mobility than the ${\beta}$-casein $A^3$ variant in acid gel. This new variant appeared together with either ${\beta}$-casein $A^1$, $A^2$ or B variant. Gene frequencies and genotypic frequencies were estimated. Gene frequencies of four milk protein loci in Korean native cattle were compared with those of imported cattle breeds raised in Korea and Japanese brown cattle. Gene frequencies were ${\alpha}s_1$-casein B .846, ${\alpha}s_1$-casein C .154; ${\beta}$-casein $A^1$ .216, ${\beta}$-casein $A^2$ .666, ${\beta}$-casein $A^4$ .048, ${\beta}$-casein B .070; ${\kappa}$-casein A .648, ${\kappa}$-casein B .352; ${\beta}$-lactoglobulin A .148, ${\beta}$-lactoglobulin B .852. The population was in Hardy-Weinberg equilibrium at all milk protein loci. Gene frequencies of Korean native cattle were very similar to those of Japanese brown cattle. Interestingly, a new variant, ${\beta}$-casein $A^4$, was found only in Korean native cattle and Japanese brown cattle. These results support the hypothesis that Korean native cattle were used in the development of the Japanese brown cattle.

Characterization of Equine Milk and Cheese Making

  • Chang, O.K.;Humbert, G.;Gaillard, J.L.;Lee, B.O.
    • Food Science of Animal Resources
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    • v.26 no.3
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    • pp.368-374
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    • 2006
  • We have studied on characterization and cheese making like mineral contents, protein composition and coagulation pattern on equine milk. At first, for contents of mineral on equine milk, It was lower in equine than bovine milk Contents of Na, Mg, P, Ca and K the major minerals, were indicated as 18.3 mg, 0.4 mg, 33.3 mg, 80.9 mg and 134.9 mg respectively by 100 g. In the distribution of nitrogen, the ratio NPN to Nt was indicated as 9.8% while that of bovine milk was 7%. And In NCN, its percentage was indicated as 45.6% shelving that Equine casein was lower than bovine. From these results, equine milk could not be applicable to cheese production since there are no coagulable nitrogen fraction such as ${\kappa}$-casein, as there aye with bovine milk. Equine milk will be more acceptable if we accept that the phylogenic affinity is near to human. It is the same as equine from the view points that monogastric, which did not contain ruminant's casein. For the rennet coagulation, equine milk was different than bovine milk. Equine milk did not coagulated by rennet after the addition of $Ca^{2+}$. But when bovine ${\kappa}$-casein was added in the presece of rennet, and $Ca^{2+}$ to equine milk, coagulation occurred. Such phenomenon was also observed by the use SEM. Verification of ${\kappa}$-casein by SDS-PACE did not existed in equine milk. The Casein of equine milk(54.4%) is similar to human milk in that casein/whey is about 1. For equine milt this can be explained because distance between casein and Ca is great, casein being lower, which result in reaction of casein with $Ca^{2+}$ because it could not activated which lasting time of coagulation is too long.

Angiotensin I-Converting Enzyme Inhibitory Activity of the ${\kappa}-Casein$ Fragments Hydrolysated by Chymosin, Pepsin, and Trypsin (${\kappa}-Casein$의 Chymosin, Pepsin 및 Trypsin 가수분해물에 대한 안지오텐신 변환효소 저해효과의 탐색)

  • Oh, Se-Jong;Kim, Sae-Hun;Kim, Sang-Kyo;Baek, Young-Jin;Cho, Kyung-Hyun
    • Korean Journal of Food Science and Technology
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    • v.29 no.6
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    • pp.1316-1318
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    • 1997
  • The isolated ${\kappa}-Casein$ on gel permeation chromatography was hydrolyzed by chymosin, trypsin, and pepsin. The 3% TCA soluble portion of the hydrolysates were dialyzed on the angiotensin-I converting enzyme (ACE) inhibition rate (%,) and inhibitory activity $(IC_{50})$ were determined. The trypsin hydrolysate exhibited the highest ACE inhibition rate while the chymosin hydrolysation showed the lowest activity. The hydrolysate was dialyzed using dialysis membrane with various molecular cut-offs, and $IC_{50}$ was determined. As the pore size of the dialysis tubing increased, the ACE inhibitory activity decreased.

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Physiochemical characteristics and fermentation ability of milk from Czech Fleckvieh cows are related to genetic polymorphisms of β-casein, κ-casein, and β-lactoglobulin

  • Kyselova, Jitka;Jecminkova, Katerina;Matejickova, Jitka;Hanus, Oto;Kott, Tomas;Stipkova, Miloslava;Krejcova, Michaela
    • Asian-Australasian Journal of Animal Sciences
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    • v.32 no.1
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    • pp.14-22
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    • 2019
  • Objective: The aim of the study was to find a possible association between the ${\beta}-$ and ${\kappa}-casein$ and ${\beta}-lactoglobulin$ genotypes and important milk physiochemical and technological characteristics such as acidity, alcohol stability, the contents of some minerals and the parameters of acid fermentation ability (FEA) in Czech Fleckvieh Cattle. Methods: Milk and blood samples were collected from 338 primiparous Czech Fleckvieh cows at the same stage of lactation. The genotypes of individual cows for ${\kappa}-casein$ (alleles A, B, and E) and ${\beta}-lactoglobulin$ (alleles A and B) were ascertained by polymerase chain reaction-restriction fragment length polymorphism, while their ${\beta}-casein$ (alleles $A^1$, $A^2$, $A^3$, and B) genotype was determined using melting curve genotyping analysis. The data collected were i) milk traits including active acidity (pH), titratable acidity (TA), alcohol stability (AS); calcium (Ca), phosphorus (P), sodium (Na), magnesium (Mg), and potassium (K) contents; and ii) yoghurt traits including active acidity (Y-pH), titratable acidity (Y-TA), and the counts of both Lactobacilli and Streptococci in 1 mL of yoghurt. A linear model was assumed with fixed effects of herd, year, and season of calving, an effect of the age of the cow at first calving and effects of the casein and lactoglobulin genotypes of ${\beta}-CN$ (${\beta}-casein$, CSN2), ${\kappa}-CN$ (${\kappa}-casein$, CSN3), and ${\beta}-LG$ (${\beta}-lactoglobulin$, LGB), or the three-way interaction between those genes. Results: The genetic polymorphisms were related to the milk TA, AS, content of P and Ca, Y-pH and Lactobacilli number in the fresh yoghurt. The CSN3 genotype was significantly associated with milk AS (p<0.05). The effect of the composite CSN2-CSN3-LGB genotype on the investigated traits mostly reflected the effects of the individual genes. It significantly influenced TA (p<0.01), Y-pH (p<0.05) and the log of the Lactobacilli count (p<0.05). Conclusion: Our findings indicate that the yoghurt fermentation test together with milk proteins genotyping could contribute to milk quality control and highlight new perspectives in dairy cattle selection.

The Changes of Casein of Cheese Base Treated with Enzyme during Ripening (Enzyme의 처리에 의한 Cheese Base의 숙성중 Casein의 변화)

  • Lee, Gang-Ik;Cha, Gwang-Jong;Yu, Je-Hyeon
    • Journal of Dairy Science and Biotechnology
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    • v.14 no.2
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    • pp.135-146
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    • 1996
  • This experiment was carried out to investigate the changes of casein of cheese base treated with substitute enzyme during ripening. The cheese base without enzyme treatment(control, D)and cheese base treated with only calf rennet(A), cheese base treated with mixed enzyme(calf rennet :porcine pepsin 1:1, B), cheese base treated with only porcine pepsin(C) were manufactured. The changes of casein were analyzed by means of HPLC and electrophoresis as experimental parameters during ripening. Gel filtration(HPLC) of casein by Superose 12 column in Cheddar cheese showed 5 fractions immediately after manufacturing and 8 fractions after six months ripening. Though D showed no difference in number of fraction(4 fraction) during 8 weeks ripening, A, B, C have represented the change of fraction number 4 to 5, 4 to 7, 4 to 8, respectively. As the mixing ratio of porcine pepsin increased, higher degradability of casein appeared. After 8 weeks ripening, electrophoresis of casein in cheese base showed three bands as an ${\alpha}$$_{s1}$casein from A and five bands from B, C. In case of D one major band and two minor bands were appeared as an ${\alpha}$$_{s1}$-casein. As the additional level of porcine pepsin increased the concentration of ${\beta}$-casein band decreased. however, that of ${\gamma}_1$ ${\gamma}_2$-casein band increased and para-${\kappa}$-casein band appeared from A, B, C, except D.

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