• Korean Journal of Food Science and Technology
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• v.25 no.5
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• pp.521-525
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• 1993

To elucidate adsorption of proteins and examine the molecular behavior of protein molecules at interfaces, various proteins at the air-water interface were studied. The adsorption data of bovine serum albumin intermediates indicated that the conformational state of a protein played an important role in adsorption of proteins at interfaces. The adsorption behavior of succinylated beta-lactoglobulin indicated that the increase in the net negative charge of the protein significantly inflenced both the kinetics and thermodynamics of adsorption. The adsorption kinetics of beta-casein showed that the salt that induced break-down of water structure decreased the rate of adsorption.

• Asian-Australasian Journal of Animal Sciences
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• v.9 no.6
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• pp.685-693
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• 1996

A total of 3,610 Ayrshire and 1,711 Jersey cows were phenotyped for the genetic variants of ${\alpha}_{s1}$-casein, ${\beta}$-casein, $\chi$-casein, ${\beta}$-lactoglobulin and ${\alpha}$-lactalbumin. Least squares analyses showed possible associations between milk protein phenotypes and lactational production traits. Depending on lactation number, ${\beta}$-casein phenotypes in Ayrshires were associated with milk production ($A^2A^2$ > $A^1A^2$ > $A^1A^1$), and with milk protein content. In the third lactation, Ayrshire cows with ${\beta}$-casein $A^1A^1$ produced milk with 3.43% fat compared to 3.37% fat for ${\beta}$-casein $A^2A^2$. In Ayrshire, $\chi$-casein phenotypes affected the protein content during the three lactations (BB > AB > AA) and ${\beta}$-lactoglobulin phenotypes significantly influenced the milk fat during the first lactation (4.06% for AA and 3.97% for BB). In Jerseys, protein content of milk was influenced by phenotypes of ${\alpha}_{s1}$-casein(3.98% for CC v/s 3.86% for BB in the first lactation). In the third lactation, $\chi$-casein AA of Jersey milk contained 5.35% fat compared to 4.82% for phenotype BB. The effects of ${\beta}$-lactoglobulin phenotypes on protein content were apparent in Jerseys during the second lactation with the A variant being superior to the B (4.00% for AA v/s 3.87% for BB).

• BMB Reports
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• v.33 no.2
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• pp.133-137
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• 2000

To elucidate the effect of oxygen radicals on the molecular properties of proteins, the secondary and tertiary structure and molecular weight size of BSA and ${\beta}$-lactoglobulin were examined after irradiation of proteins at various doses. Gamma-irradiation of protein solutions caused the disruption of the ordered structure of protein molecules as well as degradation, cross-linking, and aggregation of the polypeptide chains. As a model system, BSA and ${\beta}$-lactoglobulin were used as a typical ${\alpha}$-helical and a ${\beta}$-sheet structure protein, respectively. A circular dichroism study showed that the increase of radiation decreased the ordered structure of proteins with a concurrent increase of aperiodic structure content. Fluorescence spectroscopy indicated that irradiation quenched the emission intensity excited at 280 nm. SDS-PAGE and a gel permeation chromatography study indicated that radiation caused initial fragmentation of proteins resulting in a subsequent aggregation due to cross-linking of protein molecules.

• Journal of Animal Science and Technology
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• v.44 no.6
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• pp.801-808
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• 2002

Proteolytic activities of some commercial milk clotting enzymes(rennet, trypsin, pepsin, papain W-40, neutrase 1.5 and protease S) in bovine skim milk containing 0.02% $CaCl_2$ were determined by measuring DH(Degree of Hydrolysis), NPN(Non Protein Nitrogen) and by comparing patterns of SDS-PAGE(Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis). The DH of microbial enzymes(neutrase 1.5 and protease S) and trypsin in bovine skim milk were higher than those of pepsin and papain W-40. The amounts of NPN in the milk treated with trypsin and the other animal enzymes(rennet and pepsin) showed the highest and lowest degrees of proteolysis, respectively. SDS-PAGE showed that trypsin and protease S hydrolyzed $\alpha$-lactalbumin and papain W-40 hydrolyzed $\beta$-lactoglobulin slightly, while neutrase 1.5 hydrolyzed both $\alpha$-lactalbumin and $\beta$-lactoglobulin after treating for 90 min. Trypsin and protease S easily hydrolyzed ${\alpha}_s$-casein and $\beta$-casein, which were not hydrolyzed by rennet. Papain W-40 hydrolyzed $\kappa$-casein more than rennet as shown in SDS-PAGE. Based on the results of the experiments, the DH and NPN of trypsin, neutrase 1.5 and protease S were shown to be higher than those of the other enzymes. The SDS-PAGE patterns of papain W-40 and neutrase 1.5 were similar with that of rennet.

• Journal of the Korean Applied Science and Technology
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• v.17 no.3
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• pp.158-166
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• 2000

A conductimetric study of foam formed from mixture of the protein, ${\beta}-lactoglobulin$, and the nonioinc surfactant, SML, revealed that their stability was reduced at concentrations of SML in the range $3{\sim}10mM$. The interaction of SML with ${\beta}-lactoglobulin$ was investigated by fluorimetry and a dissociation constant of $0.2{\mu}M$ was calculated for the complex. Surface tension studies confirmed the presence of interaction between the two components and provided evidence for the progressive displacement of ${\beta}-lactogloblin$ from the air/water interface with increasing SML concentration. Experiments using air-suspended microscopic thin liquid films revealed transitions in the chainage characteristics and thickness of the film at SML concentrations below that which resulted in destabilization of the foam. However, measurements of surface mobility of fluorescent-labeled ${\beta}-lactoglobulin$ by a photobleaching method identified that a transition to a mobile system occurred at a SML concentration which correlated with the onset of instability in the disperse phase. The results would indicate that maintenance of the viscoelastic properties of the surface is paramount importance in determining the stability of interfaces comprising mixtures of protein and surfactant.

• 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 $80^{\circ}C$.

• Asian-Australasian Journal of Animal Sciences
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• v.15 no.5
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• pp.732-739
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• 2002

Milk samples with different phenotype combination of $\{kappa}$-casein and ${\beta}$-lactoglobulin and different preheating temperatures of 30, 70, 75 and $80^{\circ}C$ were used for cheesemaking under laboratory conditions. For the 853 batches of cheese, mean composition was 59.64% total solids, 30.24% fat and 23.66% protein, and the whey contained 6.93% total solids, 0.30% fat and 0.87% protein. Least squares analysis of the data indicated that heating temperature of the milk and ${\kappa}$-CN/${\beta}$-LG phenotypes had significant effects on cheese and whey compositions. The total solids, fat and protein contents of cheese were negatively correlated with preheating temperatures of milk. Cheese from BB/BB phenotype milk had the highest and those from AA/AA phenotype milk had the lowest concentrations of total solids, fat and protein. Mean recoveries of milk components in the cheese were 53.71% of total solids, 87.15% of fat, and 80.32% of protein. For the 10 different types of milk, maximum recoveries of milk components in cheese occurred with preheating temperature of $70^{\circ}C$ or $75^{\circ}C$ and lowest recoveries occurred at $80^{\circ}C$. The whey averaged 6.94% total solids, 0.30% fat and 0.87% protein. Losses of milk components in the whey were lowest for milk preheated at $80^{\circ}C$ and for milk containing the BB/BB phenotype.

• Korean Journal of Food Science and Technology
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• v.19 no.4
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• pp.285-289
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• 1987

The partition behavior or proteins in an aqueous two-phase system of poly (ethyleneglycol)-potassium phosphate buffer (PEG/PPB) was investigated. The proteins of different surface hydrophobicity, i.e. Bovine serum albumin (BSA), ${\beta}-lactoglobulin$, ovalbumin. moved to the PPB-rich bottom phase in a PEG(12%)/PPB (12%) two-phase system resulting in very low partition coefficients. When the concentration of PPB increased to 15% level. the electric potential of bottom phase changed from +50 mV to zero and the partition coefficient tended to increase. The change In the molar ratio of $K_2HPO_4/KH_2PO_4$ in PPB from 1.43 to 9.55 caused the volume ratio of top to bottom phase $(V_t/V_b)$ to be decreased and protein partition coefficient increased. When the concentration of PPB was elevated from 14% to 26%, the $V_t/V_b$ decreased from 1.5 to 0.39 and the partition coefficient of proteins increased drastically; ${\beta}-lactoglobulin$ 74 fold. BSA 32 fold, ovalbumin 12 fold and lysozyme 5 fold.

• Animal cells and systems
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• v.1 no.2
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• pp.345-350
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• 1997

The ${\beta}$-Lactoglobulin (BLG) gene expression is differentially regulated during development of the mammary tissues. Such differential regulation of the BLG gene expression can be reiterated in the cultured mammary HC11 cells. In the growing non-confluent HC11 cells, the BLG promoter activity was shown to be partially repressed by the upstream regulatory sequence. The repression was gradually diminished and switched to activation as the cells grew confluent. The differential regulation of the BLG promoter was controlled by the 5'-regulatory sequence located at the upstream of 205 bp. Electromobility shift assay showed that nuclear extract from HC11 cells differentially bound on the regulatory sequence, depending on the cell confluency, which was in accordance with the differential transcriptional activity. DNase I foot-print assay, however, revealed that all nuclear extracts presented the same foot-prints, regardless of confluency of HC11 cells. These results suggest that differential regulation BLG gene expression by the 5'-regulatory sequence may be accomplished by competitive and/or cooperative binding of differential regulatory factors on the same regulatory element.

• Asian-Australasian Journal of Animal Sciences
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• v.15 no.3
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• pp.326-329
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• 2002

A population of exotic Holstein Friesian, Jersey, their crossbreds and the indigenous Murrah breed of buffalo bulls (n=486), used in artificial insemination breeding program were screened for the allelic distribution of the ${\kappa}$-casein and ${\beta}$-lactoglobulin genotypes. The preferred "B" allele frequency was highest in Murrah buffalo bulls followed by Jersey and Holstein Friesian. The increase in this particular allele frequency in the Holstein Friesian crossbred bulls was more when compared to their Jersey counterparts. Hardy-Weinberg's equilibrium was maintained albeit with some deviations, which was higher in crossbreds than in purebreds. The feasibility of using such large-scale molecular diagnostic tools in the field and their significance with regards to the dairy economy is discussed.