• Korean Journal of Ichthyology
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• v.27 no.4
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• pp.293-299
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• 2015

The feeding experiment was conducted to investigate the effects of one experimental diet (EDP) and five different commercial diets (CEPs) on growth and body composition for juvenile parrot fish, Oplegnathus fasciatus. An EDP was formulated to contain 50% crude protein (CP) from fishmeal, casein, zein and wheat flour and 15% crude lipid (CL) from squid liver oil. Five CEPs for seawater fish were two domestic E commercial diet (DECD) and C commercial diet (DCCD), three imported H commercial diet (IHCD), L commercial diet (ILCD) and O commercial diet (IOCD) containing 53.1~66.6% CP and 10.7~14.6% CL, respectively. Each diet was fed to triplicate groups of juvenile parrot fish initially weighing $1.14{\pm}.01g/fish$ (mean${\pm}$SD) in a flow-through seawater system with a water temperature of $19.0{\sim}25.0^{\circ}C$. Weight gain (WG) and feed efficiency (FE) were significantly greatest in fish fed the DCCD and IOCD; intermediate responses were observed for fish fed the ILCD, while the IECD, IHCD, and the EDP produced the lowest WG and FE values. Survival with no significant difference approached 100% for fish fed the all six diets in this experiment. Whole-body moisture, protein, lipid and ash contents were not affected by the different type of diets. Therefore, type of diets appeared to be important factor in influencing WG and FE of juvenile parrot fish; the best diets for juvenile parrot fish was determined to be the domestic commercial C and the imported commercial O diets containing high protein (61.3, 66.6%) and lipid (14.6, 13.0%) in natural seawater based on highest WG, and FE, respectively. This study indicates that the two commercially formulated diets containing two highest proteins and lipids used in this experiment could be practical diets for juvenile parrot fish; these differences of growth performance between experimental diet and commercial diets may be reason for different dietary protein and lipid levels.

• Journal of the Korean Society of Food Science and Nutrition
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• v.38 no.11
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• pp.1506-1515
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• 2009

This study was performed to investigate the effect of chongkukjang intake on lipid metabolism and liver function in alcoholic fatty liver rats. Thirty-five 7-weeks old Spargue-Dawley male rats were used as experimental animals. After inducing alcoholic fatty liver, rats were divided into two groups and fed ethanol＋casein diet (ECD) or ethanol＋chongkukjang diet (EChD). At 10th, 20th and 30th days of the feeding experimental diet, rats were sacrificed to get blood and liver samples for analysis of blood lipids, lipid peroxides, antioxidative enzymes and biochemical indices of liver function. The mean food intake was not significantly different between ECD and EChD groups. Daily weight again of EChD group was significantly higher than that of ECD group at days 20 and 30. Serum total lipid, triglyceride and total cholesterol of ECD group were significantly higher than those of EChD group, while HDL-cholesterol was significantly higher in EChD group. Liver TBARS level of ECD group was significantly higher than that of EChD group. However, liver conjugated diene level was significantly higher in ECD group only at day 10. SOD, CAT and GPx activities of EChD group were significantly higher than those of ECD group at days 20 and 30. In the indices of liver function, GOT and GPT of ECD group were significantly higher than those of EChD group at day 10. LDH was significantly higher in ECD group. γ-GTP was significantly higher in ECD group only at day 20. Serum alcohol concentration of ECD group was significantly higher than that of EChD group at day 30. ADH and ALDH activities of EChD group were significantly higher than those of ECD group at day 30. Therefore, chongkukjang intake seems to give a beneficial effect on improving lipid metabolism and liver function by increasing HDL-cholesterol level, antioxidative enzyme activites, alcohol enzyme activities and decreasing serum lipids, liver TBARS and conjugated diene.

• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.3
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• pp.470-486
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• 1995

Mammary epithelial cells contain a subpopulation of cells with a large proliferativ potential which are responsible for the maintenance of glandular cellularity and are the progenitor cells of mammary cancer. These clonogens give rise to multicellular clonal alveolar or ductal units(AU or DU) on transplantation and hormonal stimulation. To isolate putative mammary clonogens, enzymatically monodispersed rat mammary epithelial cells from organoid cultures and from intact glands are sorted by flow cytometry according to their affinity for FITC labeled peanut lectin(PNA) and PE labeled anti-Thy-1.1 antibody(Thy-1.1) into four subpopulations : cells negative to both PNA and Thy-1.1(B-), PNA+cells, Thy-1.1+cells, and cells positive to both reagents(B+). The in vivo transplantation assays indicate that the clonogenic fractions of PNA+cells from out-growths of organoids in primary cultures for three days in complete hormone medium(CHM) are significantly higher than those of cells from other subpopulations derived from cultrues or from intact glands. Extracellular matrix(ECM) is a complex of several proteins that regulated cell function ; its role in cell growth and differentiation and tissue-specific gene expression. It can act as a positive as well as a negative regulator of cellular differentiation depending on the cell type and the genes studied. Regulation by ECM is closely interrelated with the action of other regulators of cellular function, such as growth factors and hormones. Matrigel supports the growth and development of several different multicellular colonies from mammary organoids and from monodispersed epithelial cells in culture. Several types of colonies are observed including stellate colonies, duct-like structures, two- and three-dimensional web structures, squamous organoids, and lobulo-duct colonies. Organoids have the greatest proliferative potential and formation of multi-cellular structures. Phase contrast micrographs demonstrate extensive intracellular lipid accumulation within the web structures and some of duct-like colonies. At the immunocytochemical and electron micrograph level, casein proteins are predominantly localized near the apical surface of the cells or in the lumen of duct-like or lobulo-duct colonies. Squamous colonies are comprised of several layers of squamous epithelium surrounding keratin pearls as is typical fo squamous metaplasia(SM). All-trans retinoic acid(RA) inhibits the growth of SM. The frequency of lobulo-ductal colony formation increased with the augmentation of RA concentration in these culture conditions. The current study models could provide powerful tools not only for understanding cell growth and differentiation of epithelial cells, but also for the isolation and characterization of mammary clonogenic stem cells.

• Korean Journal of Food Science and Technology
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• v.7 no.4
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• pp.229-237
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• 1975

An attempt was made to utilize the enzyme produced by Asp. oryzae as meat tenderizer. The production, purification, and various properties of proteinase produced by Asp. oryzae were investigated. Results obtained are as follow; 1. A strain which had the highest proteolytic activity was selected among 9 Aspergillus species. 2. Culture medium consisted of wheat bran 10g, 2% glucose, 0.03% urea and 0.1% $MgSO_4$ (pH 6.5). Mold was incubated at $30^{\circ}C$ for 3 days. 3. Enzyme extract from culture medium were fractionated with ammonium sulfate and purified by Sephadex G-75 column chromatography. 4. When pH of reaction mixture was controlled, maximal activity of proteinase by Asp. oryzae was obtained at pH 3, pH 6.6, $8.4{\sim}8.5$ and pH 10.0 to 10.5. Those results were interpreted to show that enzyme consists of acid proteinase, neutral proteinase and alkaline proteinase. Enzyme was stable at pH 6 to 10. 5. Opt. temperature for proteinase activity was $50^{\circ}C$, but enzyme was stable up to $40^{\circ}C$. 6. The proteinase was inhibited by $Ag^+$. It was also inhibited by EDTA. 7. When myofibrillar proteins were treated by proteinase from Asp. oryzae, ATPase activities of myofibrillar proteins changed remarkably. Accordingly, it was concluded that proteinase produced by Asp. oryzae were able to be used as meat tenderizer.

• Journal of Dairy Science and Biotechnology
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• v.14 no.2
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• pp.157-164
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• 1996

This study aimed increase the quality during ripening of Cheddar cheese made with proteinase-negative mutant of Streptococcus lactis KCTC 1913 selected by curing. The degradation of protein during cheese ripening were investigated by electrophoresis and chromatography. The results were summarized as follow ; 1. The number of lactic acid bacteria decreased with the ripening stage, and that of the control cheese decreased faster than that of the cheese made with mutant. 2. Polyacrylamide gel electrophoretic analysis of cheese caseins revealed no difference between the cheese made with mutant and the control cheese, but differences along with the ripening stage were evident. 3. On Sephadex G-25 column chromatography, the extracts of bitter components from the green cheese and 3 month ripended cheese were fractionated into 3 fractions. With the progress of ripening, bitter peptides were degraded to rather small peptides or free amino acids. 4. Sensory evaluation of the 3 month ripended Cheddar cheese found no significant differences in color but the cheese made with mutant evidenced higher palatability in flavor and better texture than the control cheese. 5. The yields of the cheddar cheese made with mutant was 0.14% higher than that of the control cheese.

• Journal of Dairy Science and Biotechnology
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• v.32 no.2
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• pp.131-139
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• 2014

The aim of this study was to manufacture Cutting-Gouda cheese and to investigate the change in physicochemical properties of Cutting-Gouda cheese made with Lactobacillus rhamnosus_p1. Lactic acid bacteria were isolated from Gouda cheese ripened for more than 1 year. They were identified as 2 strains of L. rhamnosus, Lactobacillus casei, Lactobacillus curvatus, and Staphylococcus saprophyticus by 16S rDNA sequencing and named L. rhamnosus_p1, L. casei_p2, L. curvatus_p3, L. rhamnosus_p4 and S. saprophyticus_p5. The proteolytic activities of isolated strains against casein were measured using prepared skim milk agar plates. L. rhamnosus_p1 showed the highest proteolytic activity. Cutting-Gouda cheese was made with L. rhamnosus_p1, and its physicochemical properties (moisture, protein, fat, ash and free amino acid content) were measured during ripening periods. Because of the modified atmosphere packaging ($N_2{^-}$), there was no change in moisture, protein, fat, and ash in the experimental group. The total amount of free amino acids in the control and experimental group gradually increased during ripening periods. The sensory evaluation showed that the experimental group was preferable to the control group. This result suggests that L. rhamnosus_p1 has potential to be developed as a new starter for Gouda cheese.

• Journal of Dairy Science and Biotechnology
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• v.30 no.2
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• pp.93-109
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• 2012

This study was performed to investigate the effects of added whey protein concentrates (WPC) and whey powder (WP) on the quality and shelf life of Tofu, a traditional food in Korea. Combined whey powder and whey protein concentrates were obtained at drainage after the casein was separated by using rennet enzyme or acidification of milk. We manufactured whey Tofu and evaluated its nutritional quality by testing, the general composition for yield, moisture, pH, crude protein, crude fat, carbohydrate, rheology, sensory properties, and change during storage. 1. The general compositions of WPC and WP were as follows: (a) WPC: moisture, 5.9%; crude protein, 56.2%; crude fat, 0.1%; carbohydrate, 32.6%; ash, 5.2%; and pH 5.93 and (b) WP: moisture, 3.7%; crude protein, 13.2%; crude fat, 1.6%; carbohydrate, 74.4%; ash, 7.1%; and pH, 6.65. 2. The yield of Tofu was as follows: (a) in WPC, the content was $CaCl_2$:GDL=6:4 > $CaCl_2$:GDL=9:1 > $CaCl_2$:GDL=7:3 > $CaCl_2$:GDL=8:2 and (b) in WP, 2% addition was the highest (265%) at $13.3g/cm^2$, but with 4% addition WP was the lowest (184%) at $22.2g/cm^2$. 3. The moisture content of Tofu was as follows: (a) in WPC, the content was $CaCl_2$:GDL = 6:4 > $CaCl_2$:GDL=9:1 > $CaCl_2$:GDL=7:3 > $CaCl_2$:GDL=8:2 and (b) in WP, 2% addition was the highest at 79.82% ($13.3g/cm^2$), but 4% was the lowest at 75.18% ($22.2g/cm^2$). 4. The pH of Tofu was as follows: (a) in WPC, the value was WPC 6% > WPC 4% > WPC 2% > control and $CaCl_2$:GDL=6:4 > $CaCl_2$:GDL=8:2 > $CaCl_2$:GDL=9:1 > $CaCl_2$:GDL=7:3 and (b) in WP, WP 4% > WP 2% > control. 5. The ash content of Tofu was as follows: (a) in WPC, the content was $CaCl_2$:GDL=8:2 > $CaCl_2$:GDL=7:3 > $CaCl_2$:GDL=6:4 > $CaCl_2$:GDL=9:1 and (b) in WP, there was no difference between 2% and 4% addition. 6. The crude protein content of Tofu was as follows: (a) in WPC, the content was $CaCl_2$:GDL=8:2 > $CaCl_2$:GDL=7:3 > $CaCl_2$:GDL=9:1 > $CaCl_2$:GDL=6:4 and (b) in WP, there was no difference between 2% and 4% addition. 7. The crude fat content of Tofu was as follows: (a) in WPC, the content was $CaCl_2$:GDL=8:2 > $CaCl_2$:GDL=7:3 > $CaCl_2$:GDL=9:1 > $CaCl_2$:GDL=6:4 and (b) in WP, values decreased with increasing pressed weight. 8. The carbohydrate content of Tofu was as follows: (a) in WPC, the content was $CaCl_2$:GDL=8:2 > $CaCl_2$:GDL=7:3 > $CaCl_2$:GDL=6:4 > $CaCl_2$:GDL=9:1 and (b) in WP, values increased with increasing pressed weight. 9. The rheology test results of Tofu were as follows: (a) in WPC, hardness and brittleness was highest with $CaCl_2$:GDL=8:2 and 6% added WPC. Cohesiveness was highest with $CaCl_2$:GDL=6:4 and 2% added WPC. Elasticity was the highest with $CaCl_2$:GDL=7:3 and the added WPC control. (b) in WP, hardness was the highest with $22.2g/cm^2$ and added WP control. Cohesiveness was the highest with $17.8g/cm^2$ and added WP 2%. Elasticity was the highest with $17.8g/cm^2$ and added WP 4%. Brittleness was the highest with $17.8g/cm^2$ and added WP control. 10. The sensory test results of Tofu were as follows: (a) in WPC, the texture, flavor, color, and smell were the highest with $CaCl_2$:GDL=6:4 and 6% added WPC. (b) in WP, the texture was the highest in the control with $22.2g/cm^2$. Flavor and smell were the highest in WP 2% and $22.2g/cm^2$. Color was the highest in WP 2% and $17.8g/cm^2$. 11. The quality change of Tofu during storage was as follows: (a) in WPC, after 60 h, all samples began to get spoiled and their color changed, and mold began to germinate. (b) in WP, the result was similar, but the rate of spoilage was more rapid than that in the control.

• Journal of Life Science
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• v.19 no.11
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• pp.1529-1537
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• 2009

To elucidate further the antitumor effects of a natural L-arginine analogue, L-canavanine, the mechanism underlying apoptogenic activity of L-canavanine and its modulation by protein tyrosine kinase $p56^{lck}$ was investigated in human Jurkat T cells. When the cells were treated with 1.25 to 2.5 mM L-canavanine for 36 h, several apoptotic events including mitochondrial membrane potential (${\Delta\Psi}m$) loss, activation of caspase-9, -3, -8, and -7, poly (ADP-ribose) polymerase (PARP) degradation, and DNA fragmentation were induced without alteration in the levels of Fas or FasL. These apoptotic changes were more significant in $p56^{lck}$-deficient Jurkat clone JCaM1.6 than in $p56^{lck}$-positive Jurkat clone E6.1. The L-canavanine-induced apoptosis observed in $p56^{lck}$-deficient JCaM1.6 cells was significantly reduced by introducing $p56^{lck}$ gene into JCaM1.6 cells by stable transfection. Treatment of JCaM1.6/lck cells with L-canavanine caused a transient 1.6-fold increase in the kinase activity of $p56^{lck}$. Both FADD-positive wild-type Jurkat T cell clone A3 and FADD-deficient Jurkat T cell clone I2.1 exhibited a similar susceptibility to the cytotoxicity of L-canavanine, excluding involvement of Fas/FasL system in triggering L-canavanine-induced apoptosis. The L-canavanine-induced apoptotic sub-$G_1$ peak and activation of caspase-3, -8, and -7 were abrogated by pan-caspase inhibitor (z-VAD-fmk), whereas L-canavanine-induced activation of caspase-9 was not affected. These results demonstrated that L-canavanine caused apoptosis of Jurkat T cells via the loss of ${\Delta\Psi}m$, and the activation of caspase-9, -3, -8, and -7, leading to PARP degradation, and that the $p56^{lck}$ kinase attenuated the ${\Delta\Psi}m$ loss and activation of caspases, and thus contributed as a negative regulator to L-canavanine-induced apoptosis.