• Journal of Life Science
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• v.28 no.9
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• pp.1062-1067
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• 2018

Reliable labeling of fish products can reassure consumers regarding the identity and quality of seafoods. Therefore, techniques that can identify adulteration or mislabeling are valuable. To rapidly identify two Trachurus species, Trachurus japonicus and Trachurus novaezelandiae, a highly efficient, rapid, duplex polymerase chain reaction (PCR) having two species-specific primers simultaneously was identified. This species-specific primer focused on a single nucleotide mismatch in the 3'-terminal base of a primer designed in the mitochondrial cytochrome c oxidase (COI) subunit I DNA. To optimize the duplex PCR condition, gradient PCR reactions were conducted to determine the primer annealing temperature and the primer concentration. The PCR's product was observed on the gel, suggesting that DNA molecules may be useful in differentiating the two species. The length of the amplification fragments were 103 bp for Trachurus japonicus and 214 bp for Trachurus novaezelandiae, which, along with the species-specific primer visualized by agarose gel electrophoresis, enabled accurate distinction of the species of the Trachurus genus. These results indicate that the duplex PCR, which has a species-specific primer based on single nucleotide polymorphism (SNP), can be useful for rapidly differentiating the two species of Trachurus. This duplex PCR analysis is simple, rapid, and reliable, and could be beneficial to protecting consumers' rights.

• Microbiology and Biotechnology Letters
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• v.36 no.3
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• pp.195-200
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• 2008

Saxifraga stolonifera (Saxifragaceae) is a perennial herbaceous plant growing in Korea, China, Japan and Russia. The aerial part has been used as herbal medicine for treatment of pneumonia, frostbite, inflammation and microbial infection. In this study, fresh juice and methanol extract were prepared from the aerial part of S. stolonifera, and their antimicrobial, antithrombin, and antioxidant activity were evaluated, respectively. The fresh juice showed weak antimicrobial activity against Proteus vulgaris, Escherichia coli O157:H7 and Candida albicans with ignorable DPPH scavenging activity. But, the methanol extract showed strong antioxidant activity ($IC_{50}$ of $37.5{\mu}g/mL$) with minor, broad-range antimicrobial activity. Antithrombin activities were not observed in fresh juice and extract, up to 1.5 mg/mL. Sequential organic solvent fractionation of methanol extract showed that $IC_{50}s$ of ethylacetate and the butanol fraction were 6.9 and $7.8{\mu}g/mL$, respectively, that is comparable with vitamin C or butylated hydroxytoluene. Analysis of component in extract and fractionates suggested that the antioxidants in fractions are diverse and the active substances have glycosylated phenolic structure. Our results suggest that the aerial part of S. stolonifera could be used as the natural source of potential antioxidant.

• Journal of Sericultural and Entomological Science
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• v.33 no.1
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• pp.13-20
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• 1991

The flacheric virus(FV) was isolated from the diseased larvae with flaccidity symptoms of the silkworm, Bombyx mori, which were collected in Hyangnam, Kyunggi Province and in Youcheon, Kyungpook Province. The properties of the virus were investigated and compared with the Japanese FV in morphology, size, nucleic acid and structural proteins. The Hyangnam isolate had a diameter of 27$\pm$1, 7nm with speherical shape and contained RNA of which the electrophoretic pattern was same as that of the Japanese FV. The virus had four sturctural proteins and their molecular weight were estimated as 35, 000, 33, 000, 31, 000, and 11, 400 daltons, respectively. The Youcheon isolate had two different sizeds in diameter of 27$\pm$1.7nm and 21$\pm$0.8nm. The antigenicity of the Hyangnam isolate was proved to be identical to that of Japanese FV, whereas the antisera against the Youcheon isolate (mixed with two different sizes) reacted with Japanese FV and densonucleosis virus type 1, respectively. From these characteristic of the isolated viruses, it was concluded that the Hyangnam isolate was identical to the Japanese FV and the Youncheon isolate contained the same viruses as the Japanese FV and DNVI.

• The Korean Journal of Zoology
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• v.33 no.4
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• pp.461-467
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• 1990

To investigate the neurological effect of acrylamide, whole brain of Intoxicated mouse induced early hindlimbs ataxia was examined by using the methods of SDS-PAGE and two-dimensional electrophoresis. In the gel patterns by SDS-PAGE, when the patterns of each group were compared relatively, there were no remakable changes but in the patterns of 2D-PAGE, some protein alterations were observed. Especially, the spots containing 20 (14,500, 5.64) and 21 (19,900, 6.78) were disappeared, and the spots 9 (31,300, 5.82), 11 (31,300, 5.36) and 19 (16,400, 5.42) showed marked decrease relatively in the case of treatment group. Among these changed spots, the spot 20 (14,500, 5.64) showed higher quantity than that of control group but several spots containing the spots 11 (31,300, 5.36), and 19(16.400, 5.42) were identical or equal to those of control In quantity in the case of recovery group. It seems that acrylamide might already inhibit the brain protein synthesis mechanism at the time of onset of distal neuropathy by participation in the protein metabolism so as to impair the brain regulation ability followed by a malfunction of mouse central nervous system (CNS) and recovery is gradually progressed with the dose and duration dependence after the cessation of acrylamide administration.

• Applied Biological Chemistry
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• v.36 no.2
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• pp.105-110
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• 1993

Inulin fructotransferase from Enterobacter sp. S45 was purified with DEAE-cellulose column chromatography and fast protein liquid chromatography. The purified enzyme gave a single band on polyacrylamide gel electrophoresis. The molecular weight was estimated to be 42,800 by SDS-polyacrylamide gel electrophoresis. The optimal pH and temperature for the enzyme reaction were pH 5.5 and $55^{\circ}C$, respectively. $Mg^{2+}$ activated the enzyme activity, but $Fe^{3+}$, $Cu^{2+}$, $Hg^{2+}$ significantly inhibited. After exhaustive digestion of inulin by the enzyme, DFA III, sucrose, 1-kestose and nystose were produced. Sucrose, 1-kestose, raffinose and melezitose can't be used as substrates by the enzyme, but nystose and 1-F-fructofuranosyl nystose were hydrolysed. The Km and Vmax for inulin of the enzyme were 1.4 mM and $0.196\;{\mu}mole/min$, respectively.

• Journal of the Korean Institute of Traditional Landscape Architecture
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• v.32 no.4
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• pp.120-131
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• 2014

Sajikdan(a sort of national shrine in Korea) built at the time of foundation of Joseon was entrenched into Sajik Park going through Japanese colonial era and recently the efforts to restore it is in progress. The details of change in Sajikdan in terms of diachronic analysis are as follows: Firstly, the first period refers to one prior to Japanese colonial era from the first king (also named as "Taejo" in Korean) of the Joseon Dynasty, during which it secured and strengthened the presence as a place for performing important national rites in a nation. It was built on the foot of Inwangsan Mt. at the time of the first king in Joseon Dynasty at first, was destroyed fully by fire during a Japanese Invasion period to Korea(1592-98) and afterward its ancestral ritual facilities were completed under the regime of Youngjo. However, as Japanese intervention coming to the fore, its place was destroyed and then ancestral rites were also abolished in 1908. Secondly, next period falls on 1910 to 1944 when it was transformed and entrenched into a park by the Japanese Empire. While facilities related to a park and an heterogeneous building around the part of boundary were set up, the area of altar, a ritual house and d door of Sajikdan were also designated as historical remains and treasures. Thirdly, this period refers to one from Korea's liberation year from Japanese colony(1945) to the year of 1984 when it had a mixed placeness with the statues, monuments and buildings with heterogeneous nature built. Furthermore, a door of Sajikdan was removed and reconstructed over twice due to opening of Sajik Tunnel. Fourthly, a final period falls on 1985 to the present when efforts are in progress to restore the historicity and symbolism of Sajikdan. A plan for restoration is promoted but now is a difficult time suffering from troubles caused by residents' resistance. Scrutinized historical researches through excavation investigation and residents' understanding are required altogether for restoration of Sajikdan.

• Microbiology and Biotechnology Letters
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• v.20 no.5
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• pp.551-558
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• 1992

The extracellular endoinulase from Streptomyces sp. 556 was purified and characterized, The culture broth was fractionated by ammonium sulfate saturation followed by DEAE-cellulose column chromatography and 5ephadex G-200 gel filtration, The ultimately purified fraction revealed a single band in 7.5% polyacrylamide gel electropherogram. The purified enzyme showed the maximal activity at pH 5.5-6.0 and $50^{\circ}C$, but lost 93% of inulase activity after 30 min incubation at $55^{\circ}C$ . The essen.tial amino acid residue for catalytic activity appeared to be tryptophan. This endo inulase was activated by $Mn^{2+}$, whereas inactivated by $Ag^{+}$, $Hg^{+}$, $Cu^{2+}$, $Zn^{2+}$, $Fe^{3+}$ and $Mo^{6+}$ EDTA and 8-hydroxyquinoline inhibited the enzyme so that the enzyme was considered to be a metalloenzyme. The Km value for inulin was 0.287 mM, and no invertase or $\alpha$-glucosidase activity was found in the enzyme.

• Korean Journal of Food Science and Technology
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• v.30 no.1
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• pp.82-89
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• 1998

This study was performed to elucidate the purification and characterization of pretease from saewoo-jeot, a Korean traditional salt-fermented shrimp product. The protease in saewoo-jeot (Acetes japonicus) were extracted, desalted through electrodialysis and purified by ammonium sulfate fractionation, Sephadex G-100 gel filtration and DEAE-cellulose column chromatography. Purified enzyme had specific activity of 8.4 unit/mg, yield of 14% and purification fold of 9.8. Purified enzyme was confirmed as single band protein by polyacrylamide gel electrophresis and the molecular weight was estimated to be about 24 kDa. The optimal pH and temperature for the enzyme activity were 8.0 and $40^{\circ}C$, respectively. The range of its stability to the pH and temperature were 7.0 to 10.0 and $30^{\circ}C\;to\;60^{\circ}C$, respectively. The activity of enzyme to synthetic substrate showed BAPNA and TAME. The enzyme was activated significantly by manganese ions, while inhibited by STI, TLCK. metals $(K^+,\;Li^+,\;Na^+,\;Ca^{++},\;Co^{++},\;Cu^{++},\;Mg^{++},\;Ba^{++},\;Hg^{++},\;Zn^{++},\;Fe^{+++})$. The Km value of the enzyme was $5.1{\times}10^{-7}\;M$ to hammersten casein. It's suggested that purified protease from saewoo-jeot seemed to be trypsin-like enzyme.

• Applied Biological Chemistry
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• v.26 no.1
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• pp.65-72
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• 1983

The composition of four rice protein groups is greatly affected by the extraction conditions. The extraction amounts of albumins and glubulines primarily depended on the temperature rather than the method of extraction. The total amount of glutelins, the major components of rice storage proteins, could be extracted by a successive extraction processes, extraction with 0.5% SDS-0.1M borate buffer(pH 8.3) followed by extraction with 0.5% SDS-0.6% ${\beta}-mercaptoethanol-0.1M$ borate buffer(pH 8.3). The extracted amounts of glutelin with these solvents were 54.1 and 45% respectively. The further purification of SDS soluble glutelins was achieved by Sephadex G-150 gel column chromatography. The molecular weight of the components in four protein groups has been estimated by SDS-polyacrylamide gel electrophoresis with or without ${\beta}-mercaptoethanol.$ The comparison of albumins and globulins by starch gel electrophoresis at pH 3.1 permitted us to identify seven rice varieties. However, at pH 8.95, the specific bands for Japonica type rice varieties were observed.

• Journal of the Korean Society of Food Science and Nutrition
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• v.32 no.8
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• pp.1292-1296
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• 2003

The purpose of this study is to investigate the changes of physico-chemical properties of chilled plaice muscle, stored at 4$^{\circ}C$ for 0 ∼ 21 days, with different packaging methods (vacuum packaged with PVDC and aerobic packaged with HDPE). pH value in aerobic packaged plaice muscle (APPM) decreased from 6.3 to 6.09 at first 2 day storage, and then increased gradually during storage time. Although pH pattern of vacuum packaged plaice muscle (VPPM) was similar to that of APPM, change of pH value during storage time was slower and lower than APPM. VBN value in aerobic packaged one increased during storage time. Especially it increased significantly after 7 days of storage. While VBN value in VPPM increased only a little to 14 days. TBA value showed significant difference between APPM and VPPM. WHC of APPM was higher than that of VPPM after 7 days of storage. In electrophoretic pattern of myofibril of APPM stored for 14 days hydrolysis of heavy chain and tropomyosin was observed. However, in VPPM, some hydrolysis occurred only in heavy chain. SDS-PAGE analysis showed that hydrolysis of VPPM occurs later than that of APPM.