• 한국환경보건학회지
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• 제30권4호
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• pp.308-313
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• 2004

Native and acetylated soybean protein with acetylation percentage of $25\%$ were incubated with glucose to induce Maillard reaction. Acetylation of ${\varepsilon}$-amino group of lysine residues changed the conformation of soybean protein. The direct uv spectrum of native and acetylated soybean protein showed conformational changes with accessibility of tyrosine and tryptophan residues increased. Acetylation suppressed Maillard reaction between soybean protein and glucose. Acetylated soybean protein showed improved water sorption, fat binding, foam formation, and emulsion activity of the protein, but depressed brown pigment development and trypsin digestion. Thus aceylation prevented deterioration of certain functional characteristics that occurred during storage, besides causing functional characteristics to be improved on its own.

• 한국식품저장유통학회지
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• 제8권2호
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• pp.187-192
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• 2001

Amino acid composition of proteins in Italian millet, Common millet and sorghum were invstigated by HCI hydrolysis method. The optimum condition was obtained by hydrolysis at 110$\^{C}$ for 24hr. As major amino acids from protein hydrolyzate, the content of tyosine, arginine and phebylalanine were 7.06%, 6.79% and 6.44%, respectively. The content of glutamic acid in Common millet, Italian millet and Sorghum were 5.73%, 5.64% and 5.46%, respectively. Glycine content was about 2.93% in three samples. Contents of crude protein and pure protein in Italian millet, Common millet and sorghum were determined by micro-kjeldahl method. Crude protein contents were slightly higher than that of pure protein. Protein content of sorghum was higher than those of Italian millet and Common millet. For SDS-PAGE analysis, Italian millet showed more soluble proteins including 50kDa, 30kDa and smaller proteins than other cereals. In particular, Common millet and Sorghum only solubilized proteins less than 15kDa.

• Journal of Microbiology and Biotechnology
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• 제3권4호
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• pp.261-265
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• 1993

A sopA protein (41K) encoded by plasmid pXX288 was observed in the cytoplasm, whereas a sopB protein (37K) encoded by plasmid pXX157 was observed in the membrane fraction. Most of the sopB protein was solubilized from the crude membrane by treatment with Sarkosyl, which suggested that the protein may be located in the inner membrane. The sopA protein was precipitated at the concentration of 30 to 60% ammonium sulfate. The sedimentation profile of the crude membrane fraction showed a little difference according to culture media used, and the sopB protein existed in all fractions of inner membrane. The DNA of plasmids, pXX157, pXX300, and pXX167 co-sedimented with inner membrane fraction.

• Archives of Pharmacal Research
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• 제11권3호
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• pp.225-229
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• 1988

A ginseng protein fraction which has been reported to have radiation protective effect was purified from Korean ginseng and its effects on relative survival and chromosome aberration were studied in UV irradiated CHO-K1 cells. When the protein fraction $(100\;{\mu}g/ml)$ was added to the cells before UV irradiation at 4\;J/$m^2$,, the survival rates were increased to 53.8% from 40.6% in control. Addition of the protein $(100\;{\mu}g/ml)$ after UV irradiation at 4 and $8\;J/m^2$ raised the rates to 85.4 and 24.0% from 79.2 and 11.5% in control, respectively. When the ginseng protein $(800\;{\mu}g/ml)$ was added to the cells exposed to UV light at 10, 20, $30\;J/m^2$, the frequencies of chromosome aberration (CA) were reduced significantly to almost same level regardless of the UV dose increment and there was no significant difference between pre- and post-treatment. When the concentration of ginseng protein was increased from 200 to $800\;{\mu}g/ml$, at UV dose of 10, 20, $30\;J/m^2$ each, the CA frequencies were decreased consistently as the dose of ginseng protein increased, at all UV doses tested. Similar effects were observed in both cases of pre- and post-treatment. The data suggest that the protein may reduce cell damage caused by UV light, especially damage to DNA molecule, or play a role in repair processes of damaged DNA, to increase cell survival and reduce chromosome aberrations.

• Biotechnology and Bioprocess Engineering:BBE
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• 제8권2호
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• pp.76-82
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• 2003

An increased understanding of apoptosis makes anti-apoptosis engineering possible, which is an approach used to inhibit apoptosis for the purpose of therapeutic, or industrial applications in the treatment of the diseases associated with increased apoptosis, or to improve the productivity of animal cell cultures, respectively. Some known anti-apoptosis proteins are the Bcl-2 family, IAP (inhibitor of apoptosis) and Hsps (heat shock proteins), with which anti-apoptosis engineering has progressed. This article reviews anti-apoptosis engineering using known anti-apoptosis compounds, and introduces a 30 K protein, isolated from silkworm hemolymph, as a novel anti-apoptotic protein, that Shows no homology with other known anti-apoptotic proteins. The regulation of apoptosis, using anti-apoptotic proteins and genes originating from the silkworm, Bombyx mori, may provide a new strategy in this field.

• 한국작물학회지
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• 제35권5호
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• pp.440-448
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• 1990

참깨 품질 개량 육종을 위한 기초조사로써 작물시험장에서 수집 보존하고 있는 참깨 유전자원 품종중 임의로 114품종을 선정하여 생육특성 및 단백질 함량을 조사하였으며 유래별로 12품종에 대한 아미노산을 분석한 결과를 요약하면 다음과 같다. 1. 품종별로 20.6%-30.2%의 변이를 보였으며 평균함량은 24.72%였다. 미국 도입종인 PI158066이 30.2%의 최고치를 보여 고단백질 품종육성을 위한 귀중한 유전자원으로 평가되었다. 2. 품종의 유래별로는 한국재래종이 25.8%로 높았으며 일본 도입종과는 무려 2%의 단백질 함량 차이가 있었다. 3. 초장, 엽색, 화색, 착과습성 및 실방수에 따른 단백질 함량과는 직접 관련이 없는 것으로 보이나 종파조직이 매끄러운(smooth) 품종들의 함량이 0.8% 정도 높았고 종파색별로는 검은색 > 갈색 > 회색 > 백색순으로 높았다. 4. 참깨 단백질의 아미노산 조성은 FAO 권장량보다 높아서 그 우수성을 알 수 있었다. 총 마이노산 함량은 도입종인 PI 258372가 25.03%로 가장 높았으며 재래종인 부안종과 삼척종도 높은 편이었다. 5. 필수아미노산 비율은 FAO 권장치 32.3%보다 훨씬 높은 평균 42-58.2% 수준이었으며 다른 작물보다도 높은 편이었다. 6. 재래종인 삼척종은 필수아미노산 비율이 58.2%로 가장 높고 Tyrocin 및 Lysine 함량이 공시품종중 가장 높아 품질 개량 육종의 유망한 자원으로 평가되었다. 7. 육성종중 한섬깨는 Histidine, Valine 및 Lysine 등 필수아미노산 함량이 높아 양질 다수성 품종 육성에의 이용이 기대되었다. 8. 품종의 유래별로도 차이를 보여 한국재래종 > 도입종 > 육성종 순으로 아미노산의 함량이 많았으며 특히 재래종은 필수아미노산도 가장 높아 단연 품질의 우수성이 인정되었으며 향후 이들 자원을 이용한 고품질 품종육성의 가능성을 알 수 있었다.

• International Journal of Industrial Entomology and Biomaterials
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• 제30권2호
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• pp.50-57
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• 2015

Porcine circovirus type 2 (PCV2) is an important infectious swine virus causing postweaning multisystemic wasting syndrome (PMWS). PCV2 capsid protein, encoded by ORF2 has type-specific epitopes, is very immunogenic, and is associated with the induction of neutralizing antibodies. For the efficient production of capsid protein, recombinant Autographa californica nucleopolyhedroviruses were generated to express ORF2 fused with two forms of a partial polyhedrin. Recombinant capsid protein was produced successfully with the partial polyhedrin fusion form and the yield was high, as was shown by SDS-PAGE. Production of recombinant capsid proteins in insect cells was confirmed by Western blot analysis using anti-His monoclonal antibody, anti-ORF2 monoclonal antibody, and anti-PCV2 porcine serum. Fusion expression with amino acids 19 to 110 of the polyhedrin increased the production of recombinant capsid protein, but fusion with amino acids 32 to 85 did not. Additionally, PCV2 capsid protein is a glycoprotein; however, the glycosylation of recombinant protein was not observed. The results of an Enzyme-linked immunosorbent assay (ELISA) showed that recombinant capsid proteins could be utilized as antigens for fast, large-scale diagnosis of PCV2-infected pigs. Our results suggest that the fusion expression of partial polyhedrin is able to increase the production of recombinant PCV2 capsid protein in insect cells.

• Applied Biological Chemistry
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• 제36권1호
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• pp.11-16
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• 1993

미생물에 의한 균체외 단백질의 생산 및 그 분비조건에 관한 기초자료를 얻기 위해 토양으로 부터 단백질 생산균주 11주를 분리하여 그 중 단백질 생산능이 강한 WY-60 균주를 선정하여 동정한 결과, Bacillus sp.으로 확인되었다. WY-60 균주의 단백질생산 최적조건은 fructose 4.0%, polypeptone 1.0%, $NH_4NO_3$ 0.1%, $K_2HPO_4$ 0.1%, $MgSO_4{\cdot}7H_2O$ 0.005%, $CaCO_3$ 1.0%, pH 8.0 및 온도 $30^{\circ}C$이였다. WY-60 균주는 penicillin G와 lincomycin을 첨가시에 단백질 생산을 촉진하였고 그 외의 항생물질의 첨가시는 단백질 생산을 증가하는 효과가 없었다. 배양시간에 따른 단백질 생산은 배양 5일째에 0.214 mg/ml로 최대가 되었다.

• Fisheries and Aquatic Sciences
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• 제17권3호
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• pp.319-324
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• 2014

An 8 weeks feeding trial was carried out to evaluate the effects of dietary microbial phytase (P) supplementation on nutrient digestibility, and body composition in juvenile olive flounder Paralichthys olivaceus fed soybean meal-based diets. Seven experimental diets were formulated to be isonitrogenous and isocaloric to contain 50.0% crude protein (CP) and 16.7 kJ of available energy/g with or without dietary phytase supplementation. White fish meal (FM) provided 92.4% of the total protein in the basal diet ($S_0$), in the other 6 diets, 30% or 40% FM protein was replaced by soybean meal: 70% FM + 30% soybean meal ($S_{30}$); 70% FM + 30% SM + 1000 U phytase/kg diet ($S_{30}P_{1000}$); 70% FM + 30% SM + 2000 U phytase/kg diet ($S_{30}P_{2000}$); 60% FM + 40% SM ($S_{40}$); 60% FM + 40% SM + 1000 U phytase/kg diet ($S_{40}P_{1000}$); and 60% FM + 40% SM + 2000 U phytase/kg diet ($S_{40}P_{2000}$). After two weeks of the conditioning period, triplicate groups of 25 fish initially averaging $6.15{\pm}0.04g$ ($mean{\pm}S.D.$) were randomly distributed into the aquarium and were fed one of the experimental diets for 8 weeks. After feeding trial, supplementation of phytase significantly improved the apparent digestibility coefficients of phosphorus in flounder diets (P<0.05) containing 30% and 40% soybean meal regardless the levels. However, phytase had no significant influence on growth performance and whole body composition of fish. Based on the experimental results, we conclude that dietary supplementation of phytase could improve the apparent digestibility coefficient of phosphorus in olive flounder.

• Bulletin of the Korean Chemical Society
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• 제30권3호
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• pp.577-581
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• 2009

Interactions between the surface and capsid proteins of the hepatitis B virus (HBV) are critical for the assembly of virus particles. In this study, we developed a cell-based method to visualize the interactions between the capsid and surface proteins of HBV. Capsid-GFP, a capsid protein fused to a green fluorescence protein (GFP), forms nucleocapsid-like structures in the cytoplasm of mammalian cells. It relocates to the plasma membranes in cells expressing PH-PreS, a fusion protein consisting of the PreS region of the HBV surface protein and the PH domain of PLC-$\gamma$. Membrane localization of the capsid-GFP in these cells is prevented by an inhibitory peptide that blocks the interaction between the capsid and surface proteins. This dynamic localization of capsid-GFP is applicable for screening compounds that may potentially inhibit or prevent the assembly process of HBV particles.