• Food Science of Animal Resources
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• v.18 no.1
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• pp.9-18
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• 1998

This study was performed to obtain a large quantity of $\alpha$-lactalbumin ($\alpha$-LA) from milk by an improved separation and purification method. Functional properties-solubility viscosity, emulsifying activity, foamability surface hydrophobicity and gelation-of the purified $\alpha$-LA were investigated, $\alpha$-LA was purified in a large quantity by DEAE-Sephacel chromatography using 0.15M NaCl in 20mM Tris-HCl buffer(pH 7.2), as an eluent. The yield and purity of the purified $\alpha$-LA were 23.6%, 92.5%, respect-ively. The solubility viscosity and emulsifying activity of the purified $\alpha$-LA were 92.2$\pm$2% 3.46$\pm$0.19 cP and 345$\pm$5.0m^2$-/g respecively. The foamability of $\alpha$ -LA was 762 after 5min whipping which was lower than that of WPC and showed decreasing tendency with whipping time. The relative surface hydrophobicity of the $\alpha$-LA was formed when a 10% $\alpha$-LA solution containing 100mM NaCl and 20 mM $CaCl_2$ was heated at 92$^{\circ}C$for 40min. The $\alpha$-LA gel showed 31.5 as hardness and showed low springiness and cohesiveness.

• Korean Journal of Food Science and Technology
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• v.30 no.4
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• pp.988-991
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• 1998

Plasma proteins were obtained from bloods of slaughtered bovine and porcine and analyzed by Fast Protein Liquid Chromatography (FPLC). Serum albumin content decreased in the following order: Porcine Plasma Protein (PPP)> Bovine Plasma Protein (BPP)> Whey Protein Concentrate (WPC). Protein contents of BPP, PPP, and WPC determined by Kjeldahl method were 85.79%, 82.30%, and 84.38%, respectively. Compared to WPC, plasma proteins had higher emulsifying activity index (EAI) below 2% protein concentration and slightly lower EAI above 4% protein concentration. Plasma proteins had higher EAI in the acidic pH range and more dependence on NaCl than WPC. Also, EAI of plasma proteins with NaCl was higher in the acidic range than that of WPC. These results indicated that plasma protein can be utilized as a raw material for emulsifier.

• 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.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.32 no.5
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• pp.556-562
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• 1999

The increasing price of surimi has affected the economical benefits of surimi based food industry, To maintain gel strength in low grade surimi, the optimum formulation adding functional proteins to low grade surimi is required. The objective of this study was to develop the optimum formulation of ingredients in making gels in low grade surimi on the addition of functional non-muscle proteins to low grade surmi by measuring rheological properties of the gels. The rheological qualities of the cooked gels made with A and RA grade surimi on the effects of adding five kinds of starches (potato, wheat, waxy maize, corn and modified corn) and four kinds of functional proteins (bovine plasma protein, dehydrated egg white, soy protein isolate and whey protein concentrate) to the gels were evaluated, The gel styengths at cooking with A and RA grade surimi were decreased with increasing the added starches. The kind of starches added affected little the gel strengths in Rh grade surimi, while potato and corn starches decreased at the least in gel strengths of the gel made with A grade surimi with increasing the concentration of starches. The bovine plasma protein (BPP) significantly increased the gel strength, especially in RA grade surimi, but BPP decreased the whiteness of the gel. Therefore, the optimum content of BPP was up to $2\%$ because of the whiteness of the gels in RA grade surimi, The optimum formulation for the gel with RA grade surimi to satisfy the gel strength of 1000$\times$g and $78\%$ moisture was $40.9\%$ surimi, $9.1\%$ dehydrated egg white (DEW) and $0.9\%$ starch, while that with A grade surimi under the same condition was $37.9\%$ surimi, $6.6\%$ DEW and $3,4\%$ starch.

• Food Science and Biotechnology
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• v.14 no.6
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• pp.752-757
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• 2005

Changes in milk quality during storage of extended shelf life milk (ESL milk) and non-ESL milk were evaluated. No significant differences were observed between ESL and typical ultra high temperature-treated (UHT) milk in physicochemical properties including non-casein nitrogen (NCN) content, whey protein nitrogen index (WPNI), and L-ascorbic acid content. Low temperature and long time-treated milk (LTLT milk) had significantly higher NCN content and WPNI than those of UHT milk. In terms of microbial quality, yeast, molds, coliforms, and other bacteria were not detected in ESL milk during entire storage (21 days after expiration date) period at 4 and $25^{\circ}C$, while LTLT milk was more susceptible to microbial infection. Rats fed ESL milk resulted in significantly higher body weight, average daily gain, and feed efficiency than those given UHT milk. These results suggest ESL milk maintains better microbial quality than typical UHT milk, particularly during storage under extended refrigeration and at high temperature.

• Journal of Dairy Science and Biotechnology
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• v.23 no.1
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• pp.1-8
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• 2005

The purpose of this study was to demonstrate biochemical properties and antibacterial activity of lactoferrin(Lf) obtained from the colostrum of Korean native cow. Lactoferrin was isolated from the colostrum of Korean native cow by purification steps using batch extraction, ion exchange chromatography, gel filtration chromatography, affinity chromatography. Other whey protein components that is similar molecular weight and affinity to lactoferrin were gradually removed from crude Korean Native cow's lactoferrin during the purification steps. The molecular weight of the purified Korean native cow's Lf(K-Lf) was 81 kDa, the isoelectric point was 9, and the content of iron was 0.56mg/g, which is indicated that iron saturation of the K-Lf was 40.6%. Amino acid composition and a-helix content were different K-Lf from bovine Lf(B-Lf). Antibacterial activity of E. coli O111 by K-Lf was lower than that of B-Lf. A minimal inhibitory concentration(MIC) of K-Lf and B-Lf was 2.75mg/ml and 1.5mg/ml respectively.

• Food Science of Animal Resources
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• v.30 no.3
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• pp.443-448
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• 2010

Casein phosphopeptide (CPP) enhances calcium absorption in humans. Lactic acid bacteria (LAB) are capable of synthesis of cell-surface proteinase, which can hydrolyze milk protein and release several types of peptides in the medium. This study was conducted to characterize proteinase of LAB and to evaluate the CPP production from bovine milk. The content of CPP of milk produced by cell-free extract of LAB was determined based on the quantity of decomposed peptide from casein using the O-phthaldialdehyde (OPA) method. The proteolytic activity of LAB was assayed using fluorescein isothiocyanate (FITC)-labeled casein. Casein appeared to be a better substrate than whey proteins for extracellular proteinases of LAB. During fermentation, milk proteins were hydrolyzed by extracellular proteinase of LAB, resulting in an increase in the amount of free $NH_3$ groups. Overall, the results presented here indicate that CPP produced by LAB may be a promising material for novel applications in the dairy industry.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.4
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• pp.390-397
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• 1992

This study was carried out to analyze the physicochemical properties of bovine milks, which were heated with LTLT, HTST, UHT pasteurization and UHT sterilization methods and to compare the heat intensity among the heating methods and samples. The mean HMF values per liter milk were measured as 0.66~1.62 $\mu$M (LTLT), 0.9~1.78$\mu$M (HTST), 3.53$\mu$M(UHT pasteurized) and 7.43~8.97$\mu$M (UHT sterilized) in samples, re- sportively. The available Iysine contents per 100ml milk showed 293.2 mg (Raw), 289.2~291.2 mg (LTLT), 298.4~292.4mg (HTST), 272.4~261.6mg (UHT pasteurized) and 279.0mg (UHT sterilized), respectively. The rates of whey protein denaturation were 9.5~11.4% (LTLT), 9.5~17.1% (HTST), 89.3~95% (UHT pas-tsterilized) and 62.7% (UHT sterilized), respectively. The contents of SH groups per g protein were determined as 2.86$\mu$M (Raw) and 2.95~3.15$\mu$M (LTLT), 3.08~3.18$\mu$M (HTST), 3.26~3.42$\mu$M (UHT Pasteurized) and 3. 36$\mu$M (UHT sterilized), respectively, The SS groups Contents per g protein were 28.93$\mu$M (Raw), 25.72~26. 51 $\mu$M (LTLT), 26.93~26.79$\mu$M (HTST), 23.65~23.04 $\mu$M (UHT pasteurized) and 24.69$\mu$M (UHT sterilized), respectively. The ascorbic acid contents per liter milk were measured 6.05mg (Raw), 1.47~1.65mg (LTLT), 2.50~3.85mg (HTST), 2.87~3.69mg (UHT pasteurized) and 4.50mg (UHT sterilized). The changes of some in-dices in milk samples depend on the heating temperature and time ; the HMF values, SH groups, whey protein denaturation rates increased, while the available lysine contents and SS groups decreased in LTLT, HTST, UHT pasteurized and UHT sterilized milks. No remarkable differences were found in heating indicators between LTLT and UHT milks.

• 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.

• Korean Journal of Food Science and Technology
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• v.20 no.2
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• pp.170-175
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• 1988

This experiment was carried out to study the properties of casein micelles obtained from colostral skim milk. As lactation was progressed from parturition until 240h after calving, the content of total protein decreased while the proportion of casein to whey protein increased. Fractionaltion according to the site of casein micelle was done by ultracentrifugation at 100,000 x g for 10 minutes(pellet 1), 30 minutes(pellet 2) and 60 mintes(pellet 3) and the serum casein was prepared by acid precipitation of final supernatant at pH 4.6. During the lactation period, the relative amount of pellet 1(large size) decreased, that of pellet 2(middle size) maintained nearly constant level except for pllet from parturition, that of pellet 3(small size) increased, and the serum casein showed almost constant level. The relative amounts of ${\alpha}_{s1}-casein\;and\;{\alpha}_{s2}-casein\;and\;{\beta}-casein-5P$ in the pellets decreased and that of x-casein increased markedly with decreasing micelle size, but the relative amounts of ${\beta}-casein-1P$(f 29-209), (f 106-209) and (f 108-209) showed little change. The composition of the serum casein was different from that of the skim milk casein.