• Journal of the Korean Society of Food Culture
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• v.22 no.1
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• pp.97-103
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• 2007

In this study, physicochemical properties and the antioxidative activity of whey protein isolate(WPI) for com germ oil were measured. The pH of WPI was 6.26, and the titrable acidity was 0.18%. The WPI’s moisture content was 5.2% and each of the other element content such as lactose, crude protein, crude ash and crude fat was found to be 0.8%, 90.7%, 2.7% and 0.6%, respectively. The amounts of active SH group in WPI 9 ${\mu}$ M-g and total colony counts of bacteria was 5.9 ${\times}$ 10$^3$ CFU-g. ${\alpha}$-Lactalbumin, ${\beta}$-lactoglobulin and bovine serum albumin(BSA) were shown in WPI as major protein by electrophoresis. The antioxidative effect of WPI and other antioxidants on com germ oil used as substrate was determined by peroxide value(POV) and conjuqated dienoic acid value(CDV). By these results, the order of antioxidative effects could be defined as BHT 0.02%>ascorbic acid 0.1%>WPI 0.1%>WPI 0.02%>ascorbic acid 0.02%>control>tocopherol 0.02%>tocopherol 0.1%, respectively. Also the induction period of com germ oil added with WPI was longer by 1.6 times than that of control(none added any antioxidant). Therefore the fact suggested that WPI could be utilized as a good antioxidative agents.

• Food Science of Animal Resources
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• v.24 no.2
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• pp.171-175
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• 2004

Insulin-like growth factor-I (IGF-I) rich fraction, which was obtained molecules ranged between 30 kDa and 1 kDa, was fractionated by ultrafiltration from bovine colostral whey with 30 kDa and 1 kDa membrane. IGF-I included in fractionated IGF-I rich fraction was confirmed by SDS-PAGE and western blotting and then the quantity of IGF-I was measured by ELISA. IGF-I concentration in IGF-I rich fraction was 10ng/mg protein. Effect of IGF-I rich fraction on in vitro proliferation of several cells was tested. IEC-6 cell proliferation rate was increased 60％. 53％, 30％, and 20％ at l0ng, 1ng, 0.1ng and IGF-I of IGF-I, respectively, compared to control group which was not supplemented by IGF-I rich fraction. IGF-I rich fraction stimulated in vitro proliferation of IEC-6 cell in a dose dependent manner by increasing cell number. Detroit 551 cell proliferation was enhanced 56％ and 26％ at 10ng and 1ng level of IGF-I, respectively, compared to control group. EL-4 cell and L6 cell proliferation was increased 53％ and 46％ at 10ng of IGF-I, respectively, compared to control group.

• Korean Journal of Animal Reproduction
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• v.16 no.2
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• pp.87-102
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• 1992

A rapid, sensitive, and specific enzyme-linked immuno-sorbent assay (ELISA) for bovine casein was developed. Biotinylated casein and peroxidase-conjugated avidin were used in the assay with antibody separated from yolks of immunized hens. Caseins were biotinylated with sulfo-N-hydroxy succinimido biotin and peroxi-dase-conjugated avidin bound the biotinylated casein which became bound to immobilized anti-body on a microplate. The antibodies were specific for bovine $\alpha$- and $\beta$-caseins, and their cross-reactivities with whey proteins, IgG, and serum albumin from bovine were not detectable by ELISA and Western blot. Various sensitivities ranging from 2ng/ml to 20${\mu}\textrm{g}$/ml of casein were achieved, and were controlled by adding vanous concentrations of the biotinylated casein. Parallelism was observed between standard and sample curves. The coefficients of variation of intra-assays and inter-assays from the most sensitive assay were 5.5 and 5.7%, respectively, at the 50% displacement. Casein contents of peripaturient milk samples showed that casein secretion rapidly increased 3d prepartum.

• Journal of Animal Science and Technology
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• v.48 no.5
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• pp.719-726
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• 2006

Bovine whey protein are rich in cysteine, which is the rate limiting amino acid for synthesis of antioxidant glutathione(GSH). Some strains of Lactobacillus caseihas been reported to contain high level of GSH in cell extracts. The objective ofthis study was to determine whether enzymatically hydrolyzed whey protein isolate(WPI) and cell extract of Lb. casei HY2782 could increase intracellular GSH concentrations and protect against oxidant induced cell death in human prostate epithelial cell line (designated as RWPE1, and PC3MMM2 cells). Treatment of RWPE1 cellsandPC3MMM2 cells with hydrolyzed WPI (500g/ml) significantly increased GSH by28.2% and38.4% respectively. Compared with control cells receiving no hydrolyzed WPI(P<0.05). hydrolyzed WPI and Lb casei HY2782 cell extracts significantly protected RWPE1 and PC3MMM2 cellsfrom oxidant induced cell death compared with controls receiving no WPI. DNA damage associated with oxidant treatment was demonstrated by single cell gel (SCG) electrophoresis.

• Journal of Dairy Science and Biotechnology
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• v.31 no.1
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• pp.75-83
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• 2013

Mare milk is gaining importance because of its nutritional characteristics and therapeutic properties, which enable its use as part of the diet of the elderly, convalescents, and newborn infants. This review describes the functional and bioactive components of mare milk, such as proteins, carbohydrates, and lipids, and the characteristics such as acidification and released free amino acids of fermented mare milk. The protein profile of mare milk differs from that of bovine milk but is similar to that of human milk. The salt and lactose content in mare's milk is similar to that in human milk, but mare's milk has a significantly lower content of fat. Whey protein concentration is higher and casein content is much lower in mare milk than in bovine milk. These health-promoting properties indicate that mare milk and its derivatives could become valuable foods for elderly consumers in the form of probiotic beverages. Protein allergies related to and the potential industrial applications of mare milk have also been discussed in comparison with those of bovine milk. Although mare milk has diverse advantages if used as a nutritional food and has positive effects on health, further studies are required to enable its use as a complete substitute for human milk or as a health food.

• Food Science and Biotechnology
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• v.17 no.2
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• pp.241-246
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• 2008

A nutritional supplement was developed aiming at correcting the most common nutrient and caloric deficiencies encountered in elderly people (${\geq}60$ years old). The protein source was a mixture of whey protein isolates (WPI) and bovine collagen hydrolysate (BCH) with high nutritional and functional qualities making up 12% of the formulation. The carbohydrate fraction was composed of sucrose, inulin (soluble fiber), and fructo-oligosaccharide (prebiotic). The most commonly deficient essential minerals and vitamins were also included. Acceptance of the product was good according to both an elderly panel and a laboratory panel composing of both sexes and various ages. The stability of the formulations was evaluated and the estimated shelf life at room temperature (ca. $27^{\circ}C$) was approximately 4 months.

• Preventive Nutrition and Food Science
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• v.12 no.1
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• pp.1-6
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• 2007

Colostrum basic proteins (CBP) (MW 1$\sim$30 kDa) were isolated from bovine colostrum using a series of ultrafiltration processes and their effects on osteoblast cell proliferation and bone metabolism were investigated in cell line and animal models. Treatments with CBP (1, 10, 100 $\mu$g/mL) dose-dependently increased cell proliferation of osteoblastic MC3T3 cells. Alkaline phosphatase activity, a marker of osteoblastic phenotype, in the cells was also increased after treatments with CBP in a dose-dependent manner. Significant increases in bone density were observed in femur of ovariectomized rats which were fed a diet with 1% and 10% CBP, compared to rats fed a normal diet. These results suggest that CBP may increase bone mass and density and be useful for the prevention of bone-related diseases.

• Korean Journal of Food Science and Technology
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• v.32 no.3
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• pp.564-569
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• 2000

An enzyme-linked immunosorbent assay(ELISA) was developed for the detection of milk proteins in processed foods. The ${\alpha}_{s1}-casein({\alpha}_{s1}-CN)$, a heat stable major milk protein, was immunized into rabbits to produce specific antibodies. When competitive indirect ELISA(ciELISA) using $anti-{\alpha}_{s1}-CN$ antibodies was established, its detection limit was $0.1\;{\mu}g/mL$. The reactivities of the specific antibodies toward ${\alpha}_{s1}-CN$, skim milk, ${\beta}-CN$ and whey protein isolate(WPI) were 100, 37, 0.14 and 0.04%, respectively, as determined by ciELISA. However $anti-{\alpha}_{s1}-CN$ antibodies did not have any reactivity to other milk proteins such as ${\beta}-lactoglobulin,\;{\alpha}-lactalbumin$, bovine serum albumin, and isolated soy protein. When sandwich ELISA was established, its detection limit was $0.01\;{\mu}g/mL$ which was 10 times more sensitive than that of ciELISA. In the spike test which was performed by adding 1-10% of whole CN to market milk, mean assay recovery as determined by sandwich ELISA was 94.8%(CV, 8.2%). Food stuffs and dairy products were assayed by sandwich ELISA to show 29, 0.13, 0.25, and 6.9% of whole CN in skim milk powder, WPI, semi-solid yoghurt, and processed cheese, respectively.

• Food Science of Animal Resources
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• v.22 no.1
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• pp.72-76
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• 2002

Bovine serum albumin(BSA), $\alpha$-lactalbumin($\alpha$-LA), $\beta$-lactoglobulin($\beta$-LG) and bovine immunoglobulin G (IgG) were investigated the cytotoxicity on tumor cell lines. $\alpha$-LA was showned a tendency of dose dependaent on cytotoxicity using WiDr. The growth of WiDr was inhibited 82% by 1mg/ml of $\alpha$-LA. However, IgG, BSA and $\beta$-LG were not shown the cytotoxicity on WiDr. When $\alpha$-LA was purified by using high pressure liquid chromatography(HPLC), the main component($\alpha$-LA) was eluted at 33.057 min and extremely small quantities eluted at 32.310 min. The cytotoxicity of main component (eluted at 33.057 min peak) was lower than commercial $\alpha$-LA. And the cytotoxic activity of hydrolyzed $\alpha$-LA and $\alpha$-LA treated with EDTA were lower than commercial $\alpha$-LA on tumor cells.

• Journal of the Korean Society of Food Science and Nutrition
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• v.30 no.3
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• pp.505-509
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• 2001

This study was carried out to evaluate the application of food irradiation technology as a method for reducing milk allergies. Bovine $\alpha$-casein, $\beta$-casein, $textsc{k}$-casein, $\alpha$-lactalbumin(ALA), $\beta$-lactoglobulin (BLG) and serum albumin (BSA) were used as model allergens of milk proteins and the proten solution (2.0 mg/mL) with 0.01 M phosphate buffered saline (pH 7.4) was irradiated at 3, 5 and 10 kGy. Using milk-hypersensitive patients IgE (MHP-IgE), the changes of binding ability to irradiated proteins were observed by competitive indirect enzyme-linked immunosorbent assay (Ci-ELISA). Affinity of MHP-IgE to milk proteins was higher in ALA and BLG than that of other proteins. Standard curve to each non-irradiated protein could be made with MHP-IgE for quantifying milk allergens. Binding abilities of MHP-IgE to the irradiated proteins, however, decreased with different slopes of the standard curves. Sensitivity of gamma irradiation was higher in ALA and BLG than of other proteins. These results indicated that irradiation technology can be used to reduce the milk hypersensitivity.