• Preventive Nutrition and Food Science
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• v.2 no.4
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• pp.281-284
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• 1997

Heat-induced gelation is an important functional property of whey proteins. Preheating of calcium reduced whey was reported to increase gel strength. 5% whey-protein solutions were preheated at pH7 and at various temperatures(60~8$0^{\circ}C$) for 15 minutes. The amount of soluble aggregates and denaturation enthalpy of preheated whey proteins were measured. Preheating temperature was negatively correlated with denaturation enthalpy($R^2$=0.857, P=0.08) and positive with the amount of soluble aggregates($R^2$=0.921, P=0.002). Denaturation enthalpy was negatively correlated with gel strength($R^2$=0.93, P=0.002). Soluble aggregates and gel strength were positively correlated($R^2$=0.972, P=0.0003). The formation of three dimensional gel network requires controlled protein denaturation and aggregation. Since preheating leads to the partial denaturation of proteins and the formation of soluble aggregates, preheated whey proteins have a higher gel strength than non-preheated one.

• 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.

• 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.

• Applied Biological Chemistry
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• v.29 no.1
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• pp.83-89
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• 1986

To investigate effectors on the colloidal stability of whey and soybean proteins, characteristics of tofu-gel formation, effects of heat treatment and salt composition on the colloidal stability, and effects of heat treatment on storage stability were analyzed. When experimental tofus were made from the mixture of whey and soybean, the calcium in the whey precipitated the soy proteins, and disrupted the gel formation, which resulted in the curd of poor texture. In the heat treatment at $60{\sim}100^{\circ}C$, whey and the whey proteins dialyzed against distilled water were readily preciptated at over $70^{\circ}C$, but the mixture of whey and soy extract as well as soy extract were stable at the range of temperature. The proteins of soy extract, whey dialyzed against sodium phosphate buffer, and the mixture were stable at the same heat treatment, and this suggested that phosphates in the soy extract stabilize specialty the whey proteins. Soy proteins were easily destabilized by adding $CaCl_2(0.05{\sim}0.07M)$ at $80{\circ}C$ and $70{\sim}85%$ of the proteins in soy extract and the mixture were preciptated, while only $30{\sim}55%$ of the proteins in whey dialyzed against distilled water were destabilized at the same conditions. Storage stability at $4^{\circ}C$ of the mixture was increased when the mixture was treated at $63^{\circ}C$ and lower temperature.

• Membrane and Water Treatment
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• v.7 no.2
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• pp.155-173
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• 2016

The present work has been focused on the development of polysulfone (PSf) ultrafiltration membrane via blending by sulfonated polyethersulfone (SPES) in order to permeability enhancement for ultrafiltration of cheese whey. In this regards, sulfonation of polyethersulfone was carried out and the degree of sulfonation was estimated. The effect of blend ratio on morphology, porosity, permeation and fouling of PSf / SPES membranes was investigated. Filtration experiments of whey were conducted for separation of macromolecules and proteins from the lactose enrichment phase. The morphology and performance of membranes were evaluated using different techniques such SEM, AFM, and contact angle measurements. The contact angle measurement showed that the hydrophilicity of membrane was increased by adding SPES. According to AFM images, PSf / SPES membranes exhibited lower roughness compared to neat PSf membrane. The water and whey flux of these membranes were higher than neat membrane. However, flux was decreased when the PSf / SPES blend ratio was 0/100. It can be attributed to pore size and morphology changes. Further, fouling parameters of PSf membrane were improved after blending. The blend membranes show a great potential to be used practically in proteins separation from cheese whey.

• Food Science of Animal Resources
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• v.44 no.2
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• pp.299-308
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• 2024

Proteins in whey have prebiotic and antimicrobial properties. Whey protein comprises numerous bioactive proteins and peptides, including glycomacropeptide (GMP), a hydrophilic casein peptide that separates with the whey fraction during cheese making. GMP has traditionally been used as a protein source for individuals with phenylketonuria and also has prebiotic (supporting the growth of Bifidobacterium and lactic acid bacteria) and antimicrobial activities. GMP supplementation may help positively modulate the gut microbiome, help treat dysbiosis-related gastrointestinal disorders and improve overall health in consumers.

• Journal of Food Hygiene and Safety
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• v.5 no.4
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• pp.219-228
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• 1990

Whey proteins in milk were analyzed by polyacrylamide gel electrophoresis and compared with respect to electrophoregrams, densitograms and concentrations of whey proteins in raw and market milk classified according to 3 kinds of pasteurization by low temperature long time. high temperature short time and ultra-high temperature short time. Relative composition of major whey protein constituents such as bovine serum albumin, ${\alpha}\;-\;lactalbumin\;and\;{\beta}-lactoglobulin$ in raw milk were 3.71:11.44:84.85 and not affected by low temperature long time and high temperature short time pasteurization, even though there were the tendencies of some declining in the actual concentrations. But by ultra-high temperature short time pasteurization compositions of whey protein were changed to 0: 64.75: 35 in which reflected the disapprearance of bovine serum albumin and the extensive decrease of ${\beta}-lactoglobulin$. Storage of low temperature pasteurized milk at $5^{\circ}C$ resulted in a slight decrease of ${\alpha}\;-\;lactalbumin\;a\;{\beta}-lactoglobulin$, but storage at $25^{\circ}C$ did not make any changes until3rd days of storage. Most of whey proteins in high temperature short time pasteurized milk were not affected during storage at $5^{\circ}C\;and\;25^{\circ}C$, but bovine serum albumin and ${\alpha}\;-lactalbumin$ diminished in 2-3 days of storage. Whey proteins of milk treated with ultra-high temeperature were not affected during storage at $5^{\circ}C\;and\;25^{\circ}C$ except a slight decrease of ${\alpha}\;-lactalbumin$ in 2nd day of storage at $5^{\circ}C$.

• Food Science of Animal Resources
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• v.35 no.3
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• pp.350-359
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• 2015

This review focuses on the enhanced functional characteristics of enzymatic hydrolysates of whey proteins (WPHs) in food applications compared to intact whey proteins (WPs). WPs are applied in foods as whey protein concentrates (WPCs), whey protein isolates (WPIs), and WPHs. WPs are byproducts of cheese production, used in a wide range of food applications due to their nutritional validity, functional activities, and cost effectiveness. Enzymatic hydrolysis yields improved functional and nutritional benefits in contrast to heat denaturation or native applications. WPHs improve solubility over a wide range of pH, create viscosity through water binding, and promote cohesion, adhesion, and elasticity. WPHs form stronger but more flexible edible films than WPC or WPI. WPHs enhance emulsification, bind fat, and facilitate whipping, compared to intact WPs. Extensive hydrolyzed WPHs with proper heat applications are the best emulsifiers and addition of polysaccharides improves the emulsification ability of WPHs. Also, WPHs improve the sensorial properties like color, flavor, and texture but impart a bitter taste in case where extensive hydrolysis (degree of hydrolysis greater than 8%). It is important to consider the type of enzyme, hydrolysis conditions, and WPHs production method based on the nature of food application.

• Asian-Australasian Journal of Animal Sciences
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• v.24 no.2
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• pp.272-278
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• 2011

Bovine whey protein expression patterns of colostrum are much different from that of milk. Moreover, bovine colostrum is an important source of protective, nutritional and developmental factors for the newborn. However, to our knowledge, no research has been performed to date using a comparative proteomic method on the changes in the bovine whey proteome during the transition from colostrum to milk. This study therefore separated whey protein of days 1, 3, 7 and 21 after calving using two dimension electrophoresis. Differentially expressed proteins at different collection times were identified using high-performance liquid chromatography in tandem with mass spectrometry (LC/MS) and validated by enzyme-linked immunosorbent assay (ELISA) in order to understand the developmental changes in the bovine whey proteome during the transition from colostrum to milk. The expression patterns of whey protein of days 1 and 3 post-partum were similar except that immunoglobulin G was down-regulated on day 3, and four proteins were found to be down-regulated on days 7 and 21 compared with day 1 after delivering, including immunoglobulin G, immunoglobulin M, albumin, and lactotransferrin, which are involved in immunity and molecule transport. The results of this study confirm the comparative proteomic method has the advantage over other methods such as ELISA and immunoassays in that it can simultaneously detect more differentially expressed proteins. In addition, the difference in composition of milk indicates a need for adjustment of the colostrum feeding regimen to ensure a protective immunological status for newborn calves.

• Food Science and Biotechnology
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• v.14 no.1
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• pp.131-136
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• 2005

The selective extraction behavior of lactoferrin (Lf) from whey protein mixture was examined using reverse micelles formed by the cationic surfactant, cetyldimethylammonium bromide (CDAB). The major whey proteins, including ${\beta}$-lactoglobulin, ${\alpha}$-lactalbumin and bovine serum albumin, were solubilized from aqueous phase to organic phase while Lf was recovered in the aqueous phase. The solubilization behaviors of the proteins were manipulated by the process parameters such as the pH and salt concentration of the aqueous phase and the surfactant concentration in the organic phase. Efficient forward extraction was achieved with sodium borate buffer (50 mM, pH 9) containing 50 mM KCl and organic phase containing 100 mM CDAB. Based on SDS-PAGE and densitometry, about 96% of the initial Lf remained in the aqueous phase after forward extraction. The dialyzed Lf fully maintained its bacteriostatic activity against E. coli O157:H7.