• 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.

• Asian-Australasian Journal of Animal Sciences
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• v.11 no.4
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• pp.422-427
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• 1998

The gene and genotypic frequencies of ${\kappa}$-casein (${\kappa}$-CN), ${\beta}$-lactoglobulin (${\beta}$-LG), growth hormone (bGH) and prolactin (bPRL) loci in Korean cattle were investigated using PCR-RFLP analyses. Genomic DNA samples were obtained from 290 cows and 30 AI bulls. In both cows and bulls, the most predominant genotypes of ${\kappa}$-CN, ${\beta}$-LG, bGH and bPRL loci were AB, BB, AA and AA, respecitively. The frequencies of A and B alleles for ${\kappa}$-CN locus were .612 and .388 for cows and .567 and .433 for bulls. The respective frequencies of A and B alleles for ${\beta}$-LG locus were .153 and .847 in cows and .217 and .783 in bulls. The frequencies of A and B alleles for bGH locus were .769 and .231 in cows and .784 and .216 in bulls, respectively. The frequencies of A and B alleles for bPRL locus were .678 and .322 for cows and .767 and .233 for bulls. Differences in frequencies of these alleles were not significant between cows and bulls at all loci examined. If the DNA polymorphisms of these candidate genes are associated with economically important traits, they could serve as genetic markers for genetic improvement in future marker-assisted selection programs in Korean cattle.

• Bulletin of the Korean Chemical Society
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• v.32 no.4
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• pp.1315-1320
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• 2011

Whey protein (WP) is a mixture of proteins, and is of high nutritional values. WP has become an important source of functional ingredients in various health-promoting foods. In this study, size-exclusion chromatography (SEC) and asymmetrical flow field-flow fractionation (AsFlFFF) were used for separation and analysis of whey proteins. It was found that a lab-prepared WP from raw milk is mostly of ${\beta}$-lactoglobulin with small amount of higher molecular weight components, while a commercial whey protein isolate (WPI) powder contains relatively larger amount of components other than ${\beta}$-lactoglobulin, including IgG and protein aggregates. Results suggest that AsFlFFF provides higher resolution for the major whey proteins than SEC in their normal operation conditions. AsFlFFF could differentiate the BSA and Albumin, despite a small difference in their molecular weights, and also was able to separate much smaller amount of aggregates from monomers. It is noted that SEC was able to show the presence of low molecular weight components other than the major whey proteins in the WP samples, which AsFlFFF could not show, probably due to the partial loss of those low molecular weight species through the membrane.

• Animal cells and systems
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• v.1 no.4
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• pp.603-608
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• 1997

Analysis of the 5'-regulatory sequence of the caprine ${\beta}$-lactoglobulin (BLG) gene promoter revealed that two different types of activation were mediated by discrete regions, from -740 to -470 and from -205 to 109, in cultured mammary HC11 cells. Activation mediated by the proximal region was observed regardless of cell growth status. Distal activation, however, was observed only after confluent growth of the cells and was enhanced by the lactogenic hormones. This activation was accompanied by appearance of binding activity of proteins to these regions in the mammary HC11 cells. The binding motifs were broadly distributed over the upstream regulatory sequence. Comparison of the binding regions and mutation analysis suggest that a binding motif homologous to the ${\gamma}$-interferon responsive element (${\gamma}$-IRE) is responsible for transcriptional activation by hormonal induction in the mammary HC11 cells. The multiple ${\gamma}$-IRE homologous motifs seem to play a significant role in enhancing mammary cell-specific activation of the caprine BLG gene.

• Food Science of Animal Resources
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• v.22 no.2
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• pp.179-182
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• 2002

Using differential scanning calorimetry (DSC), changes underwent by a mixture of $\alpha$-lactalbumin ($\alpha$-La) and $\beta$-lactoglobulin ($\beta$-Lg) during heat treatment were studied, yielding useful information for the dairy industry. Results of the DSC showed that the heat denaturation temperature of the hobo-$\alpha$-La was higher than that of apo-$\alpha$-La, suggesting hole-$\alpha$-La‘s greater stability. The denaturation temperature of a mixture of holo-$\alpha$-La and $\beta$-Lg was also slightly lower than that of holo-$\alpha$-La alone. The denaturation temperature of an apo-$\alpha$-La and $\beta$-Lg mixture was higher than that of holo-$\alpha$-La and $\beta$-Lg, suggesting that the heat stability of apo-$\alpha$-La was increased by $\beta$-Lg. Based on these results, it is possible to conclude that a mixture of holo-$\alpha$-La and $\beta$-Lg is more intensively affected by an increase in temperature than other samples, and that free sulphydryl groups seem to take part in this heat-induced denaturation.

• Food Science of Animal Resources
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• v.22 no.1
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• pp.59-65
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• 2002

This study was carried out to evaluate the effect of whey protein concentrate-80%(WPC-80) and whey protein isolate(WPI) on the growth of B. bifidum Bb-11. Whey proteins($\alpha$-lactalbumin, $\beta$-lactoglobulin) were digested with trypsin, then their hydrolyzates were separated into three fractions (>10,000Da, 3,000∼10,000Da, <3,000Da) by two-step ultrafiltration process with Centriprep 10 and Centricon-30. These three fractions by molecular weight were evaluate growth-promoting effects for the B. bifidum Bb-11. The results obtained were summarized as follows; The growth rate of B. bifidum Bb-11 tended to increase by supplementation of WPC-80 to basal medium, but decreased by supplementation of WPI. Two whey proteins were hydrolyzed by trypsin at 40$\^{C}$ for 6 hrs, and three fractions were collected by UF treatment and concentrated by Centricon-30. Collected concentrations of protein of F-I and F-II and F-III from $\alpha$-lactalbumin were 11.53mg, 7.79mg, and 5.21 mg and those of protein from $\beta$-lactoglobulin were 4.13mg, 5.30mg, and 9.351mg, respectively. Three fractions of $\alpha$-lactalbumin hydrolyzates promoted the growth rate of B. dbifidum Bb-11. Growth promoting activities of hydrolyzates(F-I and F-II) with molecular weight below 10,000Da were stronger than that of hydrolyzate(F-III) above 10,000Da. However, there was no significant difference between the hydrolyzate F-I and F-II. Three fractions of $\beta$-lactoglobulin hydrolyzates improves the growth rate of B.bifidum Bb-ll. The growth of B.bifidum Bb-ll was decreased after 24 hr incubation by supplementation of either F-II or F-III fraction compared to basal Whey medium, but maintained the enhancement by supplementation of F-I.

• Food Science of Animal Resources
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• v.37 no.6
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• pp.940-947
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• 2017

Goat milk has a protein composition similar to that of breast milk and contains abundant nutrients, but its use in functional foods is rather limited in comparison to milk from other sources. The aim of this study was to prepare a goat A2 ${\beta}$-casein fraction with improved digestibility and hypoallergenic properties. We investigated the optimal conditions for the separation of A2 ${\beta}$-casein fraction from goat milk by pH adjustment to pH 4.4 and treating the casein suspension with calcium chloride (0.05 M for 1 h at $25^{\circ}C$). Selective reduction of ${\beta}$- lactoglobulin and ${\alpha}_s$-casein was confirmed using sodium dodecyl sulphate-polyacrylamide gel electrophoresis and reverse-phase high-performance liquid chromatography. The hypoallergenic property of A2 ${\beta}$-casein fraction was examined by measuring the release of histamine and tumor necrosis factor alpha from HMC-1 human mast cells exposed to different proteins, including A2 ${\beta}$-casein fraction. There was no significant difference in levels of both indicators between A2 ${\beta}$-casein treatment and the control (no protein treatment). The A2 ${\beta}$-casein fraction is abundant in essential amino acids, especially, branched-chain amino acids (leucine, valine, and isoleucine). The physicochemical properties of A2 ${\beta}$-casein fraction, including protein solubility and viscosity, are similar to those of bovine whole casein which is widely used as a protein source in various foods. Therefore, the goat A2 ${\beta}$-casein fraction may be useful as a food material with good digestibility and hypoallergenic properties for infants, the elderly, and people with metabolic disorders.

• Korean Journal of Human Ecology
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• v.5 no.1
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• pp.75-80
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• 1996

The immunogenecity of low molecular weight ($MW{\le}30,000$) immunogens in laying hens was investigated. Immunogens were insulin derivatives and ${\beta}$-lactoglobulin(${\beta}-Lg$). Insulin derivatives were reduced- carboxymethylated(RCM) insulin, and RCM-A and RCM-B chain of insulin. The yolk antibodies against RCM-A chain of insulin appeared after the first immunization. The yolk antibodies against RCM-B chain of insulin were elicited 5 weeks after the third booster injection. Although the anti-RCM-B chain yolk antibodies recognized native insulin, the anti-RCM-A chain yolk antibodies didn't native insulin. The anti-RCM insulin yolk antibodies were induced after the second booster injection and showed cross-reactivities with native insulin. On the other hand, ${\beta}-Lg$ showed stronger immunogenecity than insulin derivatives. The $anti-{\beta}-Lg$ yolk antibodies were produced after the second booster injection and the peak titer was reached 3 weeks after the third booster injection.

• Preventive Nutrition and Food Science
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• v.3 no.2
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• pp.143-151
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• 1998

Protein -surfactant interactions have been investigate by measuring ζ-potential of $\beta$-lactoglobulin-coated emulsion droplets and $\beta$-lactoglobulin in solution in the rpesenceof surfactant, with particular emphasis on the effect of protein heat treatment(7$0^{\circ}C$, 30min). When ionic surfactant (SDS or DATEM) is added to the protein solution, the ζ-potential of the mixture is found to increase with increasing surfactant concentration, indicating surfactant binding to the protein molecules. For heat-denatured protein,it has been observed that the ζ-potential tends to be lower than that of the native protein. The effect of surfactant on emulsions is rather complicated .With SDS, small amounts of surfactant addition induce a sharp increase in zeta potential arising from the specific interaction of surfactant with protein. With further surfacant addition, there is a gradual reductio in the ζ-potential, presumably caused by the displacement of adsorped protein (and protein-surfactant complex) from the emulsion droplet surfac by the excess of SDS molecules. At even higher surfactant concentrations, the measured zeta potential appears to increase slightly, possibly due to the formation of a surfactant measured zeta potential appears to increase slightly, possibly due to the formation of surfactant micellar structure at the oil droplet surface. This behaviour contrastswith the results of the corresponding systems containing the anionic emulsifier DATEM, in which the ζ-potential of the system is found to increase continuously with R, particularly at very low surfactant concentration. Overall, such behaviour is consisten with a combination of complexation and competitive displacement between surfactant and protein occurring at the oil-water interface. In addition, it has also been found that above the CMC, there is a time-dependent increase in the negative ζ-potential of emulsion droplets in solutions of SDS, possibly due to the solublization of oil droplets into surfactant micelles in the aqueous bulk phase.

• Asian-Australasian Journal of Animal Sciences
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• v.30 no.8
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• pp.1175-1182
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• 2017

Objective: To create genetically modified goat as a biopharming source of recombinant human lacotoferrin (hLF) with transcription activator-like effector nucleases. Methods: TALENs and targeting vector were transferred into cultured fibroblasts to insert hLF cDNA in the goat beta-lactoglobulin (BLG) locus with homology-directed repair. The gene targeted efficiency was checked using sequencing and TE7I assay. The bi-allelic gene targeted colonies were isolated and confirmed with polymerase chain reaction, and used as donor cells for somatic cell nuclear transfer (SCNT). Results: The targeted efficiency for BLG gene was approximately 10%. Among 12 Bi-allelic gene targeted colonies, five were used in first round SCNT and 4 recipients (23%) were confirmed pregnant at 30 d. In second round SCNT, 7 (53%), 4 (31%), and 3 (23%) recipients were confirmed to be pregnant by ultrasound on 30 d, 60 d, and 90 d. Conclusion: This finding signifies the combined use of TALENs and SCNT can generate biallelic knock-in fibroblasts that can be cloned in a fetus. Therefore, it might lay the foundation for transgenic hLF goat generation and possible use of their mammary gland as a bioreactor for large-scale production of recombinant hLF.