• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.4
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• pp.619-624
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• 1995

Sesame protein concentrate(SPC) was prepared from defatted sesame flour(DSF) at several different pH(2.0, 7.0, 9.0, 11.0) for protein extraction. Some of their functional properties were determined in order to compare the effects of pH during preparation of concentrates. Compared with DSF, nitrogen solubility was markedly improved in all SPC, and SPC extracted at pH 11.0 showed the highest solubility at all pH leaves examined. Fatabsorption was increased in all SPC prepared, but water absorption was decreased as the extraction pH of protein increased. The emulsifying properteis and foaming properties of SPC were remarkably higher than DSF. As the extraction pH of protein was increased, the emulsion activity was also increased, but emulsion stability was decreased. SPC extracted at pH 7.0 showed the highest foaming capacity on the other hand, the highest foaming stability was shown in SPC extracted at pH 2.0. As the protein extraction pH increased, the viscosity of the protein solution was increased. SPC extracted at pH 11.0 showed highest viscosity at all protein concentrations tested.

• Proceeding of EDISON Challenge
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• 2016.03a
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• pp.90-95
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• 2016

Heat Shock 70kDa Protein 1-Like(HSPA1L)는 Heat-shock protein70(HSP70) family에 속하는 chaperone protein으로 polypeptide folding, assembly, protein degradation 등 다양한 biological processes에 관여하고 있다. HSPA1L은 human methyltransferase-like protein 21A(METTL21A)에 의해 lysine residue에 methylation이 일어나게 되는데, 암세포에서 일반적인 HSPA1L은 주로 세포질에서 발견되는 반면 methylated HSPA1L의 경우 주로 핵에서 발견이 됨으로써 HSPA1L methylation이 암 세포 성장에 중요할 역할을 할 것이라 추측되며 anti-cancer drug target으로 주목 받고 있다. 하지만 현재 HSPA1L의 구조가 부분적으로만 밝혀져 있어 HSPA1L와 METTL21A가 어떤 residue들이 interaction 하여 binding을 하는지에 대해서 아직 밝혀 지지 않았다. 이로 인해 anti-cancer drug target으로서의 연구에 제한이 있다. 이번 연구에서는 homology modeling(Galaxy-TBM, Galaxy-refine)을 통해 HSPA1L 전체 구조를 밝혀 낸 후, HSPA1L 와 METTL21A를 protein-protein docking을 통해 binding pose 예측을 하였다. 이러한 binding pose를 protein interaction analysis하여 HSPA1L과 METTL21A binding에 관여하는 중요 residue들을 밝혀 냈다. 이러한 structural information은 methylated HSPA1L와 암 세포 성장간의 연관성, 더 나아가 anti-cancer drug 개발로 까지도 이어 질 수 있을 것이라 생각한다.

• Journal of the Korean Magnetic Resonance Society
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• v.23 no.4
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• pp.104-107
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• 2019

Many proteins are expressed as an insoluble form during the production using Escherichia coli (E. coli) system. Although various methods are applied to increase their amounts of soluble expression, refolding is the only feasible way to obtain a target protein in some cases. Moreover, protein NMR experiments require ¹³C/¹⁵N-labeled proteins that can only be obtained from E. coli systems in terms of cost and technical difficulty. The finding of appropriate refolding conditions for a target protein is a time-consuming process. In particular, it is very difficult to determine whether the refolded protein has a native structure, when a target protein has no enzymatic activity and its refolding yield is very low. Here, we showed that 1-dimensional ¹H-¹⁵N heteronuclear single quantum correlation (1D ¹H-¹⁵N HSQC) experiment can be efficiently used to screen an optimal condition for the refolding of a target protein by monitoring both the structure and concentration of the refolded protein.

• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.1
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• pp.41-47
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• 1995

This experiments was designed to evaluated the chemical components and nutrition of Aspergillus fumigatus cells. This dried fungal mycellia was consist of crude protein 48.5%, crude lipid 2.9%, carbohydrate 44.7% and total ash 3.4%, respectively. The major fatty acid of total lipid were 27.9% of linoleic acid, 24.6% of oleic acid, 15.4% of palmitic acid and 10.6% of linolenic aicd. Amino acid analysis indicated that the protein was rich in aspartic acid, glutamic acid, leucine, lysine but poor in cystein, methionine, histidine. The fungal cake of Aspergillus fumigatus, when dried and specially processed, has been found to serve as a source of protein in place of soybean meal in the diet of experimental mice. Animal were fed a control diet first, and an incease in weight proved the formulation to be satisfactory. At the end of a 30-day period, the experimental mice showed increases in weight comparable to those of the control animals. The net protein efficiency ratio for the control diet was 3.42$\pm$0.15 and the fungal protein and succinylated fungal protein with DL-methionine they were 3.12$\pm$0.39 and 2.98$\pm$0.06 respectively. This supports the view that dried and succinylated fungal protein can be substituted as a protein source.

• Animal cells and systems
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• v.7 no.1
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• pp.81-87
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• 2003

While screening proteins that interact with DnaA protein, the initiator protein for Escherichia coil chromosomal DNA replication, we found a 52-kD sized protein which bound to DnaA protein in a salt-dependent manner. This protein was identified as trigger factor, a ribosome-associated peptidyl-prolyl- cisltrans isomerase with chaperone activity. Trigger factor was overproduced and purified to near homogeneity, and its effect on the function of DnaA protein was examined, Enhanced binding of DnaA protein to DnaA box with no apparent supershift in the gel-shift experiments suggested that trigger factor, by virtue of its chaperone activity, exerts a change on DnaA protein thus increasing its binding affinity for DnaA box.

• Journal of Korean Ophthalmic Optics Society
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• v.19 no.1
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• pp.51-57
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• 2014

Purpose: The present study was conducted to establish the experimental condition for the proper evaluation of protein removal efficacy when developing protein removal agents. Its protein removal efficacy was further analyzed and compared with the result from protein removal efficacy against protein deposition on contact lens to suggest the evaluation method for efficacy of protein removal agents. Methods: Protein digestibility assay presented in the Korean pharmacopoeia was selected to establish the evaluation method for efficacy of papain, pancreatin, subtilisin A and protease itself as a ingredient and protein removal tablets or solution containing those enzymes and find a suitable test conditions. Furthermore, the cleaning efficacy of commercially available protein removal tablets and solution on balafilcon A lens deposited with protein artificially was measured and the correlation between two evaluation methods was further analyzed. Results: When pancreatin itself and the product containing pancreatin was evaluated by protein digestibility assay, both reached 28 IU/mg, the standard value of protein digestibility suggested by the Korean pharmacopoeia. In case of protease and subtilisin A tested with trichloroacetic acid B solution, both of them met the enzyme activity level proposed by the manufacturers when they were evaluated by protein digestibility assay however, papain and subtilisin A tested with trichloroacetic acid A solution were not reached the enzyme activity level. Among protein removal agents, three products except a product containing pancreatin did not meet the enzyme activity value specified by the manufacturer when they were evaluated by protein digestibility assay. However, actual protein removal efficacy of three products except a papain-containing product on the lens was greater than 90% protein removal. In the case of papain-containing protein removal product, its effect was not measured by protein digestibility assay however, its actual protein removal efficacy on the lens reached 73.72%. Conclusions: From the results, it was confirmed that the efficacy of protein removal agents for contact lens should be evaluated by different method according to the type of proteolytic enzyme contained. That is, the protein removal agents containing pancreatin, protease and subtilisin A can be evaluated by protein digestibility assay and protein removal efficiency evaluation and the products containing papain can be effectively evaluated by only the evaluation method for protein removal efficiency employing the lens.

• Preventive Nutrition and Food Science
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• v.7 no.3
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• pp.278-281
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• 2002

The objective of the current study was to determine the influences of dietary proteins and methionine on plasma lipid concentrations. Thirty growing male Sprague-Dawley rats were fed diets similar in all respects except that dietary protein was from either casein, soy protein isolate, or soy protein isolate supplemented with L-methionine (0.24 %). The animals were fed experimental diets ad libitum for nine weeks. Plasma total-cholesterol concentrations were unaffected by the protein source or methionine supplementation. Plasma triglyceride concentrations were lower in rats of methionine supplemented soy protein diets (76 mg/dL) than in the rats fed casein or soy diet (120 mg/dL, 109 mg/dL, respectively). These results indicate that soy protein reduces plasma triglycerides relative to casein in rats fed cholesterol free diets, and that methionine-supplemented soy diets decrease plasma triglyceride concentrations more than soy protein alone.

• Asian-Australasian Journal of Animal Sciences
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• v.9 no.3
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• pp.261-266
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• 1996

Carcass analysis of most economical parts of broilers were studied after they were fed with different protein levels of 16, 18, 20 and 23% for the starter period and 16, 18 and 20% for the grower period. The energy value of the feed was constant at 3,200 kcal ME/kg. The results for the starter and grower broilers showed similar pattern of responses. There were significant increased in weight gain, feed intake, protein intake, while there were significant decrease in the feed conversion ratio (FCR), abdominal fat and carcass fat when dietary protein increased. For the economical parts of the carcass, most of the fats were found in the thigh meat, while the lowest was found in the breast meat. The protein levels did not influence the meat production of the breast, drumstick and thigh portion. Increasing the protein intake, increased the broiler performance in relation to increased protein content of the breast, drumstick and thigh meat. The different fat contents of the meat might be due to differences in the rate of lipogenesis and fat deposition of the meat.

• Bulletin of the Korean Chemical Society
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• v.28 no.10
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• pp.1756-1762
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• 2007

Envelope proteins of virus contain a segment of hydrophobic amino acids, called as fusion peptide, which triggers membrane fusion by insertion into membrane and perturbation of lipid bilayer structure. Potential fusion peptide sequences have been identified in the middle of L or M proteins or at the N-terminus of S protein in the envelope of human hepatitis B virus (HBV). Two 16-mer peptides representing the N-terminal fusion peptide of the S protein and the internal fusion peptide in L protein were synthesized, and their membrane disrupting activities were characterized. The internal fusion peptide in L protein showed higher activity of liposome leakage and hemolysis of human red blood cells than the N-terminal fusion peptide of S protein. Also, the membrane disrupting activity of the extracellular domain of L protein significantly increased when the internal fusion peptide region was exposed to N-terminus by the treatment of V8 protease. These results indicate that the internal fusion peptide region of L protein could activate membrane fusion when it is exposed by proteolysis.

• The Korean Journal of Food And Nutrition
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• v.14 no.6
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• pp.562-567
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• 2001

In order to utilize okara protein as a food auditive, nutritional composition of soymilk okara was investigated. Protein in okara Is highly insoluble due to excessive heat treatment during soymilk processing. Protein content of okara was 37.3% as compared to 42.5 % for soybean. Carbohydrate and lipid contents of okara were 40.6% and 17.9%, respectively. Okara lipid extracted with chloroform-methanol consisted of neutral lipid, glycolipid and phospholipid, with neutral lipid making up 98.6% . Linoleic acid, ileic acid, and palmitic acids accounted for about 80% of the total fatty acids with linoleic acid sharing 50.3% of the total. Amino acid composition of okara protein was dissimilar to that of soy Protein : Cysteine was totally absent in okara while lysine, which is the limiting amino acid of soy protein, was present in higher amount in okara on dry weight basis. Both aqueous extract of okara protein and soy Protein were found to have ACE inhibitory activity.