• Journal of the Korean Society of Safety
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• v.30 no.4
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• pp.79-85
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• 2015

Onboard fire extinguishing system is important to protect cargo and human lives and every oil tanker has foam type fire extinguishing system. Because of environmental problem, agent which contains materials such as Perfluorinated compounds are regulated and the development of the environmental friendly agent is required. The protein foam has less environmental pollution problem and has an excellent fire extinguish performance to oil fire. In the research, bivalency metal salts were added as stabilizer to increase fire resistance and stability of the foam. Ferrous sulfate, Iron chloride and Nickel chloride were used and to adjust to vessel, sea water was applied. As a stabilizer increased, the expansion ratio was raised. However 25% drainage time was decreased over 2.0 wt.% which is knowable that the foam brokes easily. The amount of generated foam was measured to check fluidity of foam and it appeared that when $FeSO_4$ 1.2 wt.% was added, the amount of generated foam reached large and also the 25% drainage time was high. To evaluate the fire extinguishing performance for oil fire, the small scale oil fire test was executed. When $FeSO_4$ 1.2 wt.% was added, fire extinguishing time was in its shortest which informs fluidity of foam and stability are important factors on fire extinguishing efficiency.

• Journal of Microbiology and Biotechnology
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• v.13 no.5
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• pp.738-744
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• 2003

The gene ADH encoding NAD-dependent alcohol dehydrogenase from Bacillus stearothennophilus was cloned and overexpressed as a GST fusion protein at a high level in Escherichia coli. The expressed fusion protein was purified simply by glutathione affinity chromatography. GST fusion protein was then cleaved by thrombin, while soluble enzyme was further purified by glutathione affinity chromatography. The recombinant enzyme had the same elctrophoretic mobility as the native enzyme from Bacillus stearothennophilus. The recombinant enzyme catalyzed the oxidation of a number of alcohols and exhibited high activities towards secondary alcohols. The $K_m\;and\;V_{max}$ values of the recombinant enzyme for ethanol were 5.11 mM and 61.35 U/mg, respectively. Pyridine and imidazole notably inhibited the enzymatic activity. The activity of the recombinant enzyme optimally proceeded at pH 9.0 and $70^{\circ}C$. The midpoint of the temperature-stability curve for the recombinant enzyme was approximately $68^{\circ}C$, and the enzyme was not completely inactivated even at $85^{\circ}C$. The recombinant enzyme showed a high resistance towards denaturing agents (0.05% SDS, 0.1 M urea). Therefore, due to its stability and relatively broad substrate specificity, the recombinant enzyme could be utilized in bio-industrial processes and biosensors.

• Animal cells and systems
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• v.11 no.2
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• pp.205-213
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• 2007

Nek6 belongs to NIMA1 (never in mitosis, gene A) related kinase, which was originally identified in Aspergillus nidulans as a serine/threonine kinase critical for cell cycle progression. We noticed that the putative SUMOylation site is localized on the $K^{252}$ residue in $^{251}FKsD^{254}$ of Nek6, based on the consensus sequence ${\Phi}KxE$; where ${\Phi}$ represents L, I, V or F and x is any amino acid. We observed that the Nek6 SUMO mutant (K252R) has decreased protein kinase activity, nuclear speckle localization and protein stability, compared with that of the Nek6 wild type. However, the Nek6 SUMO mutant increased the cell survival rate of COS-1 cells as determined by FACS analysis. Therefore, our data suggest that SUMOylation on the $K^{252}$ residue of Nek6 is required for its normal functions, such as proper nuclear localization, kinase activity and protein stability, to control cell cycle.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.45 no.3
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• pp.201-206
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• 2012

Supercritical carbon dioxide ($SCO_2$) extraction was used to recover concentrated proteins and to remove lipids and odor causing compounds from anchovy. Engraulis japonicus $SCO_2$ was used as the solvent for extraction, which was performed in a semi-batch flow reactor. The experimental conditions used were pressure, 15-25 MPa; temperature, $40-60^{\circ}C$ and sample size, 500 ${\mu}m$. The proteins obtained under these conditions performed well in a sensory evaluation; moreover, effective lipids and odor removal was achieved. The stability and characteristics of the proteins recovered with different solvents were also evaluated. The samples were sterilized by processing with $SCO_2$. Escherichia coli was not detected after storage for several days. The sensory characteristics were found to be superior to those of a sample produced by hexane extraction. Thus, the protein concentrate was obtained at $60^{\circ}C$ and 25 MPa was deemed valuable as a foodstuff.

• Food Science and Biotechnology
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• v.16 no.4
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• pp.572-575
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• 2007

The angiontensin converting enzyme (ACE) inhibitory peptides were separated from beef sarcoplasmic protein extract and their amino acid sequences were identified as GFHI, DFHINQ, FHG, and GLSDGEWQ. The 4 peptides were synthesized in a laboratory and the ACE inhibitory activities of pep tides was measured after 2 months of storage at $4^{\circ}C$ under different pH conditions (6.0, 6.5, 7.0, 7.5, and 8.0) and the exposure of different temperatures (70, 80, 90, and $100^{\circ}C$) for 20 min to evaluate industrial use. No significant difference was detected by pH and temperature abuse for 20 min during storage. When the synthetic peptides were digested by pepsin, trypsin, and chymotrypsin, the ACE inhibitory activity was not changed. These results indicated that the 4 synthetic peptides with ACE inhibitory activity were pH-stable, heat-stable, and resistant to proteinases in gastro-intestinal tracts. Therefore, those 4 peptides can be used as a source for functional food product with various applications.

• Journal of the Korean Home Economics Association
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• v.28 no.4
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• pp.41-50
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• 1990

Soy protein was isolated from Korean soy bean 'Chang ryub' and chemically modified with succinic anhydride. Functionality of the soy protein isolate(SPI), succinylated SPI(SPPI), and PP590(commercial) at various pH were investigated. The mechanical and sensory properties of soy bean curds made from several mixing ratio of succinylated soy bean milk were observed. The solubility of SPI significantly increased with succinylation. The solubility of PP590 was lower than that of SSPI. The solubility of SPPI increased significantly in 0.03M CaCl2 solution. The emulsifying activity of SSPI increased. On the range of pH above pI the emulsifying activity of PP590 was higher than that of SPI. There was no difference in emulsion stability among the groups. The foam expansion capacity of SPPI increased at higher pH than pI but the foam stability decreased significantly above pH 9. Mechanical texture profile analysis revealed the modified soy bean curds had the lower hardniss, chewiness and cohesiveness with increased modification. The mechanical characteristics of modified soy bean curds revealed generalized Maxwell Model of 7-elements or 5-elements. In sensory evaluation, the hardness, the springiness and acceptability of modified soy bean curds were lower significantly than those of control soy bean curd.

• Food Science of Animal Resources
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• v.34 no.6
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• pp.808-814
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• 2014

This study investigated the effect of gum arabic (GA) combined with microbial transglutaminase (TG) on the functional properties of porcine myofibrillar protein (MP). As an indicator of functional property, heat-set gel and emulsion characteristics of MP treated with GA and/or TG were explored under varying NaCl concentrations (0.1-0.6 M). The GA improved thermal gelling ability of MP during thermal processing and after cooling, and concomitantly added TG assisted the formation of viscoelastic MP gel formation. Meanwhile, the addition of GA decreased cooking yield of MP gel at 0.6 M NaCl concentration, and the yield was further decreased by TG addition, mainly attributed by enhancement of protein-protein interactions. Emulsion characteristics indicated that GA had emulsifying ability and the addition of GA increased the emulsification activity index (EAI) of MP-stabilized emulsion. However, GA showed a negative effect on emulsion stability, particularly great drop in the emulsion stability index (ESI) was found in GA treatment at 0.6 M NaCl. Consequently, the results indicated that GA had a potential advantage to form a viscoelastic MP gel. For the practical aspect, the application of GA in meat processing had to be limited to the purposes of texture enhancer such as restructured products, but not low-salt products and emulsion-type meat products.

• Molecules and Cells
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• v.38 no.9
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• pp.814-820
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• 2015

PinX1, a nucleolar protein of 328 amino acids, inhibits telomerase activity, which leads to the shortening of telomeres. The C-terminal region of PinX1 is responsible for its nucleolar localization and binding with TERT, a catalytic component of telomerase. A fraction of TERT localizes to the nucleolus, but the role of TERT in the nucleolus is largely unknown. Here, we report a functional connection between PinX1 and TERT regarding PinX1 stability. The C-terminal of $PinX1^{205-328}$, a nucleolar fragment, was much more stable than the N-terminal of $PinX1^{1-204}$, a nuclear fragment. Interestingly, PinX1 was less stable in TERT-depleted cells and more stable in TERT-myc expressing cells. Stability assays for PinX1 truncation forms showed that both $PinX1^{1-328}$ and $PinX1^{205-328}$, nucleolar forms, were more rapidly degraded in TERT-depleted cells, while they were more stably maintained in TERT-overexpressing cells, compared to each of the controls. However, $PinX1^{1-204}$ was degraded regardless of the TERT status. These results reveal that the stability of PinX1 is maintained in nucleolus in the presence of TERT and suggest a role of TERT in the regulation of PinX1 steady-state levels.

• Korean Journal of Food Science and Technology
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• v.25 no.3
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• pp.295-298
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• 1993

This study was carried out to investigate the effects of heating temperature, heating time and protein concentration on the gel properties and heat stability of a mixed system of pork plasma and myofibrillar to increase the utility of porcine blood as protein resources of the food industry, especially meat processing industry. The solubility of plasma protein and mixture (plasma + myofibrillar protein) decreased significantly at $70^{\circ}C\;to\;90^{\circ}C$ when heating temperature rised, whereas myofibrillar protein decreased slightly at $40^{\circ}C\;to\;60^{\circ}C$, and the gel strength and the turbidity of those increased significantly at these heating temperatures. The solubility of plasma protein and mixture decreased when the heating time increased at $75^{\circ}C$, whereas the gel strength and turbidity increased, and the solubility, the gel strength and the turbidity of myofibrillar protein showed no changes.

• Journal of Life Science
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• v.19 no.4
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• pp.436-441
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• 2009

B23/nucleophosmin, a nucleolar protein, translocates into the nucleus from the nucleolus when cells are damaged by extracellular stresses. Recently, it was shown that such translocation of B23/nucleophosmin in normal fibroblasts under stress conditions increases both the stability and activation of the p53 protein by disrupting its interaction with MDM2. Senescent cells have a single large nucleolus and a diminished capacity to induce p53 stability upon exposure to various DNA damaging agents. To investigate the role of B23/nucleophosmin in p53 stability in senescent cells, we established a senescence model system by expressing the ras oncogene in IMR90 cells. The stability of p53 was reduced in these cells in response to nucleolar stress, although the level of B23/nucleophosmin protein was not changed. In addition, p53 did not accumulate in the nucleus and B23/nucleophosmin did not translocate into the nucleoplasm. The binding affinity of B23/nucleophosmin with p53 was reduced in senescent cells, whereas the interaction between MDM2 and p53 was stable. Taken together, the stability of p53 in ras-induced senescent cells may be influenced by the ability of B23/nucleophosmin to interact with p53 in response to nucleolar stress.