• 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.