• Applied Biological Chemistry
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• v.31 no.4
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• pp.361-370
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• 1988

To investigate the interaction between whey and soybean protein, thermal changes of component proteins were analyzed by column chromatography and gel electrophoresis. In the Sephadex G-200 chromatography of the mixture treated at above $80^{\circ}C$, the amount of low molecular weight proteins and high molecular aggregates were increased. This implicated that dissociation of 1ls globulin into subunits and the formation of soluble aggregates between these subunits and whey proteins that contain thiol and disulfide groups. These interaction between soy proteins and ${\beta}-lactoglobulin$, ${\alpha}-lactalbumin$, and proteose-peptone 3 were confirmed by gel electrophoresis. Bovine serum albumin, Immunoglobulin-G(H), Lactoferrin, 1ls-subunits(basic and acidic), and subunit of 7s globulin were also considered to interact each other depending on the condition of the salt solutions.

• 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.30 no.6
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• pp.923-929
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• 2010

Colostral whey prepared from colostrum (pooled from first six post-partum milkings) was heated for 10 min at $100^{\circ}C$ Heated colostral whey was incubated with 1% enzymes (protein equivalent basis) for 15, 30, 60, 90, and 120 min at $50^{\circ}C$. Papain, pepsin, trypsin, and alcalase produced different degrees of hydrolysis (DH), 10.66%, 12.42%, 10.83%, and 25.31%, respectively, at an incubation time of 120 min. The SDS-PAGE reveals that significant amounts of bovine serum albumin (BSA), ${\beta}$-lactoglobulin (${\beta}$-LG), and ${\alpha}$-lactalbumin (${\alpha}$-LA) survived papain digestion. In contrast, pepsin completely removed BSA but not ${\beta}$-LG present in heated colostral whey. Alcalase completely eliminated BSA, ${\beta}$-LG, and ${\alpha}$-LA. This differential hydrolysis was confirmed by reversed-phase HPLC analysis. Using ion-exchange chromatography, fraction-1 (F-1) was obtained from alcalase hydrolysate at a NaCl gradient concentration of 0.25 M. Reversed-phase HPLC chromatograms of alcalase F-1 showed numerous small peaks, which probably indicate that a variety of new peptides were produced. Iron content of alcalase F-1 was 28.94 ppm, which was the highest among all enzyme fractions, whereas iron content of colostral whey was 36.56 ppm. Main amino acids contained in alcalase F-1 were Thr (15.45%), Glu (14.12%), and Ser (10.39%). Therefore, alcalase can be used to generate good iron-binding peptides in heated colostral whey, and the resulting iron-binding peptides could be suitable as a value-added food ingredient for food supplements.

• Journal of Dairy Science and Biotechnology
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• v.16 no.2
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• pp.106-118
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• 1998

Whey is a natural product obtained during cheese production. With the advent of new technology, whey protein concentrates and whey fractions have become readily available and versatile food ingredients. Whey protein concentrates are highly functional ingredients that have gelling, emulsifying, whipping, water-binding and fat-replacement properties. New fractions derived from whey (such as alpha-lactalbumin, lactoferrin, lactoperoxidase and peptides) attract considerable interest worldwide because of their bioactive or health-enhancing properties. Some of these fractions also find new uses as natural antibiotic, natural preservative and immunity-enhancing agents. With the growth of the functional foods industry sector, an increasing number of manufacturers take advantage of whey's nutritional and functional benefits to develop successful new products. The United States is the world's largest single producer and exporter of whey products. In 1997, more than 1 million metric tons of whey products were manufacturers in the U.S.

• Asian-Australasian Journal of Animal Sciences
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• v.27 no.6
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• pp.886-897
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• 2014

The aim of the present study was to get a total physical and chemical characterization and comparison of the principal components in Bangladeshi buffalo (B), Holstein cross (HX), Indigenous cattle (IC) and Red Chittagong Cattle (RCC) milk. Protein and casein (CN) composition and type, casein micellar size (CMS), naturally occurring peptides, free amino acids, fat, milk fat globule size (MFGS), fatty acid composition, carbohydrates, total and individual minerals were analyzed. These components are related to technological and nutritional properties of milk. Consequently, they are important for the dairy industry and in the animal feeding and breeding strategies. Considerable variation in most of the principal components of milk were observed among the animals. The milk of RCC and IC contained higher protein, CN, ${\beta}$-CN, whey protein, lactose, total mineral and P. They were more or less similar in most of the all other components. The B milk was found higher in CN number, in the content of ${\alpha}_{s2}-$, ${\kappa}$-CN and ${\beta}$-lactalbumin, free amino acids, unsaturated fatty acids, Ca and Ca:P. The B milk was also lower in ${\beta}$-lactoglobulin content and had the largest CMS and MFGS. Proportion of CN to whey protein was lower in HX milk and this milk was found higher in ${\beta}$-lactoglobulin and naturally occuring peptides. Considering the results obtained including the ratio of ${\alpha}_{s1}-$, ${\alpha}_{s2}-$, ${\beta}$- and ${\kappa}$-CN, B and RCC milk showed best data both from nutritional and technological aspects.

• 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.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.2
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• pp.208-214
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• 1993

Ginseng-whey beverages were prepared with rennet whey, ginseng, sweetener, honey and Japanese apricot, inoculated with different strains of lactic acid bacteria or unfermented partly. The samples were stored at 4$^{\circ}C$ or 30$\pm$1$0^{\circ}C$ and then physicochemical and microbiological properties were investigated. The yield of whey was 78.8%. The pH-values reduced and acidities increased during the storage period. The contents of solid-substances, ash and lipid in ginseng-whey beverages were 7.90~8.20%, 0.62~0.66% and 0.16%, respectively. The protein contents of ginseng-whey beverages were 0.42~0.56% and the contents were not changed during the storage period. The lactose contents of fermented beverages were higher than those of unfermented beverages. During the storage period (1~5 weeks), the ranges of D(-) - and L(+)- lactic acid contents in fermented ginseng-whey beverages (17.3~156.1 mg/100g, 347.3~1894.2mg/100g) were higher than those of unfermented ginseng-whey beverages (6.2~82.8mg/100g, 7.1~885.5mg/100g). The contents of total saponin in unfermented sample and fermented sample (Lac. casei sub-sp. casei+Str. salivarius sub-sp. thermophilus) were increased during the storage period. But, those of the fermented sample(Lac. acidophilus+Lac. delbrueckii sub-sp. bulgaricus) were reduced. In the electrophoretic results of ginseng-whey beverages, an $\alpha$-lactalbumin and a $\beta$-lactoglobulin bands were shown apparently and there were no changes observed during the storage period. During the storage period (1~3 week) the coliform was not detected and total plate counts and psychrotrophs were increased according to the storage period.

• 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.

• Korean Journal of Agricultural Science
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• v.47 no.3
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• pp.459-470
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• 2020

This study investigated the effects of the proteolytic hydrolysates of α-lactalbumin (LA), β-lactoglobulin (LG) and bovine serum albumin (BSA) by alcalase on inflammatory cytokines. The proteolytic hydrolysates were separated into two fraction of peptides, ≤ 10,000 Da and > 10,000 Da, respectively, because various low molecular weight peptides were generated during the hydrolysis reaction time. Among the hydrolysate peptides, BSA (all types), β-LG (> 10,000 Da), and α-LA (> 10,000 Da) showed an inhibitory activity against thymic stromal lymphopoietin (TSLP) mRNA expression in lipopolysaccharide-induced RAW264.7 murine macrophages. α-LA (> 10,000 Da), β-LG (hydrolysates), and BSA (> 10,000 Da) showed an inhibitory activity against tumor necrosis factor (TNF)-α expression. α-LA (all types), β-LG (hydrolysates, > 10,000 Da), and BSA (> 10,000 Da) showed an inhibitory activity against interleukin-6 (IL-6) expression. α-LA (> 10,000 Da), β-LG (> 10,000 Da), and BSA (all types) showed an inhibitory activity against inducible nitric oxide synthase (iNOS) expression. α-LA (> 10,000 Da), β-LG (> 10,000 Da), and BSA (all types) showed an inhibitory activity against cyclooxygenase (COX)-2 expression. The lowest level of TNF-α production was measured with α-LA (> 10,000 Da) and β-LG (> 10,000 Da) for all types, and a similar low level was measured for all types of BSA. The highest level of IL- 6 production was measured with α-LA (≤ 10,000 Da) among α-LA, β-LG, and IL-6. The low level of NO production was similar with α-LA, β-LG, and BSA but not with α-LA (≤ 10,000 Da). These potential peptides from whey protein hydrolysates could be used for food, medicinal, and industrial applications.