• Journal of Dairy Science and Biotechnology
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• v.31 no.2
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• pp.127-131
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• 2013

The aim of this study was to investigate adulteration of caprine milk products by bovine milk using biomolecular techniques with bovine-specific primers for the mitochondrial cytochrome b gene. Polymerase chain reaction (PCR) and real-time PCR assays were applied to caprine milk products including infant formula, city milk, and fermented milk. The results indicated that six out of the eight caprine infant formula products tested contained bovine milk components. In addition, two of the three tested caprine city milk products and two caprine fermented milk products were shown to be adulterated with bovine milk. Conventional PCR results corroborated with results obtained by real-time PCR. This study demonstrates that DNA-based species identification procedures would be useful and applicable in routine examinations of the dairy industry to ensure the quality and safety of dairy foods.

• Food Science of Animal Resources
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• v.18 no.2
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• pp.185-191
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• 1998

Human milk and bovine milk in normal stage were fractionated four parts : whey, skimmilk membrane, and casein pellet. The specific activity (nmole / mim / mg protein) and distribution ratio(%) of suborganella marker enzymes in each separated milk fraction were determined. Especially, neutral $Ca^{2+}$-ATPase, acid $Ca^{2+}$-ATPase, NADH-cytochrome C reductase, and acid phosphatase were higher in human milk. However, both $Ca^{2+}$-ATPases were not detected in all fractions of bovine milk. On the other hand, 5'-nucleotidase, phosphodiesterase I, alkaline phosphatase, and $\gamma$-glutamyl transpeptidase activities in bovine milk were higher than in human milk. Most of the marker enzymes were highly distributed in cream fraction of either human milk or bovine milk, and their specific activities were high to 24 fold from 3 fold when compared with that of whole milk. These results suggest that marker enzymes in mammary epitherial cell are transfered into cream fraction by the membrane rearrangement, and different biochemical reaction between human and bovine exists for milk secretion in mammary gland.

• Journal of Food Hygiene and Safety
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• v.10 no.2
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• pp.61-64
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• 1995

The present study was conducted to examine the effect of recombinant bovine somatotrpin(${\gamma}$BST), which was administered to cow to promote milk production, on bST levels in milk. Fourteen cows were divided cows were divided into two groups: 1) control cows received neither ${\gamma}$bST nor vehicle, 2) treated cows were administered twice at two-week interval with 500 mg ${\gamma}$bST each cow byj after lst injection. Milk samples were taken on day 0 (prior to injection), day 7 (7 days after lst injection), day 21 (7 days after 2nd injection) and day 35 (21 days after 2nd injection). Milk bST concentration was measured by the radioimmunoassay method. There was no statistical difference(p<0.05) in milk bST levels between two groups showing bST levels in the range of 1.8 ng/m/ to 3.1 ng/m/. That is, ${\gamma}$bST administration did not increase bST levels in milk.

• 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.

• Asian-Australasian Journal of Animal Sciences
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• v.3 no.3
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• pp.247-252
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• 1990

Nine Holstein cows in mid lactation period were utilized to examine the effect of recombinant bovine somatotropin (BST) of tow companies (Company A, Company B) on milk production and milk composition under the feeding conditions of Korea. Treatments were 0 (Control), 25 mg BST/day from company A (BST A) and 25 mg BST/day from company B (BST B) injected subcutaneously, once daily beginning at $200{\pm}20$ days postpartum and continuing for 28 days. Cows were fed ad libitum a total mixed diet throughout the experimental period. BST treatments increased average 4% fat corrected milk yields and milk energy output over the 28-day treatment period. However, no differences were observed in dry matter intake, gross efficiency, energy intake and percent milk energy. Although there was a tendency for increased milk fat percent, there were no differences in milk composition and yields of major milk components except for milk fat yield with BST injection. Somatic cells of all groups were also characteristic of a well managed herd. Neither mean body condition score nor body weight was significantly (p <0.05) changed before and during BST treatment. BST concentration in milk remained in the range of control animals throughout the experimental period of BST treatment. Results indicate that short-term injection of recombinant bovine somatotropin from two companies to lactating dairy cow resulted in similar increased in milk yield without alteration of major milk components or feed intake.

• Korean Journal of Animal Reproduction
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• v.22 no.3
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• pp.237-244
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• 1998

To investigate the fidelity of transgene transmission and expression, we produced transgenic mice carrying bovine $\beta$-casein/bovine grwoth hormone(bGH) fusion gene and examined transmission efficiency and expression level of the transgene in the founders and their progeny. The transgene was composed of 1.8 kb bovine $\beta$-casein promoter and 2.1 kb bGH gene. Ten transgenic mice were produced. Milk and mammary gland were collected from eight transgenic lines at 10-day lactation and a, pp.ied to Western and Northern blot analyses. The bGH expression was detected in four of them. The concentrations of bGH in milk were highly variable from 4$\mu\textrm{g}$/ml to 600$\mu\textrm{g}$/ml depending on the lines. The bGH mRNA level in mammary gland was closely correlated with the bGH concentration in milk in each transgenic line. These results indicated that bGH transgene expression was a, pp.opriately regulated in the mammary gland and secreted into milk in transgenic mice. By using two transgenic lines(#2, #7) secreting a considerable amoung of bGH into their milk, the inferitance and maintenance of transgenic phenotype were assessed in successive four generations. The mean transmission frequencies of transgene in lines #2 and #7 were 34% and 40%, respectively. The bGH concentration in milk were 80, 240, 120, 60$\mu\textrm{g}$/ml in each G0(generation 0), G2, G3, G4 generation of line #2 and 600, 1600, 860, 900$\mu\textrm{g}$/ml in each G1. G2, G3, G4 generation of line #7. These results demonstrated that bovine $\beta$-casein/bGH gene was stably transmitted from generation to generation in a Menelian fashion in trasgenic mice and consistenly expressed in their milk throughout the generations, although there was a little variation in the transmission frequency and expression level of the transgene between generations.

• Food Science of Animal Resources
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• v.31 no.5
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• pp.631-640
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• 2011

Milk oligosaccharides are the complex mixture of six monosaccharides namely, D-glucose, D-galactose, N-acetyl-glucosamine, N-acetyl-galactosamine, L-fucose, and N-acetyl-neuraminic acid. The mixture is categorized as neutral and acidic classes. Previously, 25 oligosaccharides in bovine milk and 115 oligosaccharides in human milk have been characterized. Because human intestine lacks the enzyme to hydrolyze the oligosaccharide structures, these substances can reach the colon without degradation and are known to have many health beneficial functions. It has been shown that this fraction of carbohydrate can increase the bifidobacterial population in the intestine and colon, resulting in a significant reduction of pathogenic bacteria. The role of milk oligosaccharides as a barrier against pathogens binding to the cell surface has recently been demonstrated. Milk oligosaccharides have the potential to produce immuno-modulation effects. It is also well known that oligosaccharides in milk have a significant influence on intestinal mineral absorption and in the formation of the brain and central nervous system. Due to its structural resemblance, bovine milk is considered to be the most potential source of oligosaccharides to produce the same effect of oligosaccharides present in human milk. This review describes the characteristics and potential health benefits of milk oligosaccharides as well as the prospects of oligosaccharides in bovine milk for use in functional foods.

• Korean Journal of Agricultural Science
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• v.45 no.4
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• pp.635-643
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• 2018

Bovine milk is widely consumed by humans and is a primary ingredient of dairy foods. Proteomic approaches have the potential to elucidate complex milk proteins and have been used to study milk of various species. Here, we performed a proteomic analysis using 2-dimensional electrophoresis (2-DE) and matrix assisted laser desorption ionization-time of flight mass spectrometer (MALDI-TOF MS) to identify whey proteins in bovine milk obtained soon after parturition (bovine early milk). The major casein proteins were removed, and the whey proteins were analyzed with 2-dimensional polyacrylamide gel electrophoresis (2-D PAGE). The whey proteins (2 mg) were separated by pI and molecular weight across pH ranges of 3.0 - 10.0 and 4.0 - 7.0. The 2-DE gels held about 300 to 700 detectable protein spots. We randomly picked 12 and nine spots that were consistently expressed in the pH 3.0 - 10.0 and pH 4.0 - 7.0 ranges, respectively. Following MALDI-TOF MS analysis, the 21 randomly selected proteins included proteins known to be present in bovine milk, such as albumin, lactoferrin, serum albumin precursor, T cell receptor, polymeric immunoglobulin receptor, pancreatic trypsin inhibitor, aldehyde oxidase and microglobulin. These proteins have major functions in immune responses, metabolism and protein binding. In summary, we herein identified both known and novel whey proteins present in bovine early milk, and our sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis revealed their expression pattern.

• Proceedings of the Korean Society of Food Hygiene and Safety Conference
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• 1994.12a
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• pp.15-26
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• 1994

Bovine somatotropin(bST) or bovine growth hormone (bGH) is a protein of 191 amino acids produced by the anterior pituitary gland of cattle. Recombinant bovine somatotropin(rbST) is biosynthetic versions of the naturally occurring pituitary hormone in cows. The use of rbST in dairy cows promises to improve the efficiency of milk production around the world. Using recombinant DNA technology, bST can now be produced in commercial quantities. The recombinant bST(rbST) is biologically identical to the found in the bovine pituitary. Milk from rbST-treated cows has been found to have the same nutritional value and composition as milk from untreated cows. In November of 1993, rbST finally was approved by the FDA, nearly 10 years after filing a licence applica-tion. rbST has been one of the most extensively studied animal drug products to be reviewed by the agency. Three scientific facts will help to reassure the public about the safety of the milk suppy.: 1. rbST has no biological activity in humans when indigested orally or when given by intramuscular injection. 2. Insulin-like growth factor 1(IGF-1) is not orally active. Any changes in IGF-1 levels in milk are well within normal variation and are lower than those reported in human milk. 3. All cow's milk contains bST, and no significant change in bST levels in milk occurs as a result of giving cows supplemental bST. Based on the scientific evidence, the public can be confident that milk and meat from rbST-treated cows is safe to consumers.

• Korean Journal of Veterinary Research
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• v.47 no.1
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• pp.1-6
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• 2007

The importance of milk for the growth and health of a newborn offspring is well known. Milkcontains immunoglobulin G (Ig G), Ig A, lactoperoxidase, lactoferin, cytokines, and growth factors.Osteopontin, one of the multifunctional proteins, is secreted by macrophages, T cel, and epithelial cells.bovine milk have not been clarified. The aim of this study was to observe the expression of osteopontin,in bovine milk during the lactation period or bovine mamary glands..Western blot analysis detected thatosteopontin was expressed in bovine milk whey and mamary glands. The expression level of osteopontinin colostrum whey was higher than those in early milk and mature milk whey. Immunohistochemistryshowed that osteopontin was detected in the glandular epithelium and epithelial cels of intralobular ductof mamary glands. These findings suggest that osteopontin transiently shows high expression in colostrumand plays a potential role in the immunological development of breast-fed calves.