• Journal of Applied Biological Chemistry
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• v.59 no.4
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• pp.285-288
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• 2016

Proteolytic enzymes perform hydrolysis of the peptide bonds in the protein and most commonly use in the industry. Pseudoxanthomonas sp. WD12 and WD32 were previously isolated as protease producers from a rotten wood sample. Here, we report the secreted proteolytic enzymes. The optimum enzyme reaction temperature for the secreted crude enzyme from the strain WD12 and WD32 were $50^{\circ}C$ at pH 9.0 and $45^{\circ}C$ at pH 8.0, respectively. The enzyme activities of both strains were increased by addition of KCl, NaCl, $CaCl_2$ or $MnSO_4$, and decreased by addition of $AgNO_3$, $CuSO_4$, $FeCl_3$ or $AlCl_3$. Secreted enzymes of both strains were most strongly inhibited by addition of $FeCl_3$ or $CuSO_4$. Taken together these results, WD12 could be a candidate strain of industrial alkaline protease production.

• Journal of Animal Science and Technology
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• v.46 no.4
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• pp.625-634
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• 2004

The objective of this experiment is to study the possibility of lactate dehydrogenase(LDH) enzyme to prevent lactate accumulation in the rumen, For understanding capacity of bacterial LDH in rumen environments, this study was conducted to explore the effects of temperature, pH, VFAs and metal ions on Lactobacillus sp. FFy111-1's LDH activity, and the LDH activation in rumen fluid accumulated lactate. The optimum pH and temperature of LDH were pH 7.5 and 40$^{\circ}C$, respectively. The LDH activity had a good thennostability at range from 30 to 50$^{\circ}C$. The highest pH stability of the enzyme was at ranges from pH 7.0 to 8.0 and the enzyme activities showed above 64% level of non-treated one at pH 6.0 and 6.5. The LDH was inactivated by VFAs treatments but was enhanced by metal ion treatments without NaCl and $CuSO_4$ Especially, the LDH activity was increased to 127% and 124% of its original activity by 2 mM of $BaCl_2$ and $MnSO_4$, addition, respectively. When the acidic rumen fluid was treated by LDH enzyme of Lactobacillus sp. FFy111-1, the lactate concentration in the rumen fluid was lower compared with non-treated rumen fluid(P<0.05). This lactate reduction was resulted from an action of LDH. It was proved by result of purified D,L-LDH addition that showed the lowest lactate concentration among the treatments(P<0.05). Although further investigation of microbial LDH and ruminal lactate is needed, these findings suggest that the bacterial LDH has the potential capability to decrease the lactate accumulated in an acidic rumen fluid. Also, screening of super LDH producing bacteria and technical development for improving enzyme activity in rumen environment are essential keys for practical application.

• Clean Technology
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• v.18 no.3
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• pp.272-279
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• 2012

In this study, an environmental-friendly cleaning agent utilizing organic acids and various additives has been developed and applied to the field for removal of scale deposited on the cleaning beds or distribution reservoirs of the waterworks. As an analytical result of scale on the cleaning beds, we found that it consists of mainly metallic oxides such as $SiO_2$, $Al_2O_3$, $Fe_2O_3$, and MnO. Malic acid, malonic acid, and citric acid showed relatively better solvency on $Al_2O_3$, $Fe_2O_3$, and MnO except $SiO_2$ among various organic acids. Mixed organic acid solutions of malic acid, malonic acid, and citric acid were prepared with certain weight ratios and their solvencies on mixed metal oxides of $Al_2O_3$, $Fe_2O_3$, and MnO were investigated. The experimental results showed that an 10% mixed organic acid solution prepared with weight ratio of malic acid : malonic acid : citric acid = 6 : 2 : 2 were found to have best scale solvency power of about 29%. The formulated cleaning agents with a small amount of nonionic surfactant showed much better solvency on mixed oxides than mixed organic solution alone. Especially, the formulated cleaning agent with 0.2 wt% LA-7 surfactant appeared to have best scale removal efficiency of about 35%. However, the formulated cleaning agent with disinfectants such as NaClO, $H_2O_2$ and $Ca(ClO)_2$ showed poor solvency on mixed oxides. It is inferred that surfactants are able to improve scale removal efficiency due to their capability of emulsification, and disinfectants cause to degrade scale solvency in water because of their oxidation. Based on these basic experimental results, formulated cleaning agents have been prepared with mixed organic acid solution, nonionic surfactants, and disinfectants and successfully applied to removal of scales on the cleaning beds and distribution reservoir at city D waterworks.

• The Journal of the Korea Contents Association
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• v.16 no.5
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• pp.660-667
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• 2016

Conventional decontamination methods utilize water-based systems, which generate high amounts of secondary wastes. Herein, we describe an environmentally benign decontamination method using liquid and supercritical $CO_2$. The use of $CO_2$ as a solvent affords effective waste reduction by its ability to be recycled, thereby leaving be hind only the contaminants upon its evaporation. In this study, a $CO_2$ solution process was assessed using t-salen(t-butylsalen), DC18C6 (dicyclohexano-18Crown6), 8-HQN(8-hydroxyquinoline), NEt4PFOSA(perfluoro-1-octanesulfonic acid tetra-ethyl ammonium salt), and NEt4PFOA(pentadecafluorooctanoic acid ammonium salt) to extract spiked radioactive contaminants(Nb,Zr,Co,Sr) from an inert sample matrix, namely filter paper. With the static extraction method, Sr was extracted with a maximum extraction rate of 97%, and Nb was extracted with a maximum extraction rate of 75%. Additionally, we were also able to extract Co and Zr with maximum extract ion ratesof 73% and 64%, respectively.

• Proceedings of the Korean Vacuum Society Conference
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• 1999.07a
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• pp.154-154
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• 1999

금속산화막은 전자부품 및 광학적 응용에 널리 사용되고 있다. 특히 알루미늄의 산화막은 유전체의 재료로 커패시터에 많이 사용되고 있다. 이러한 알루미늄 산화막을 plasma를 이용한 ion plating에 의해 형성하였다.Activated Reactive Evaporation은 화합물의 증착율을 높이는데 좋은 증착법이다. 이러한 증착법에는 reactive ion plating와 ion-assisted deposition 그리고 ion beam sputtering 등이 있다. 본 연구에서는 알루미늄 산화막을 증착시키기 위해 plasma를 이용한 electron-beam법을 사용하였다. Turbo molecular pump로 챔버 내의 진공을 약 10-7torr까지 낸린 후 5$\times$10-5torr까지 O2와 Ar을 주입시켰다. 각 기체의 분압은 RGA(residual gas analyzer)로 조사하여 일정하게 유지시켰다. plasma를 발생시키기 위해 filament에서 열전자를 방출시키고 1kV 정도의 electrode에 의해 가속시켜 이들 기체들과 반응시켜 plasma를 발생시켰다. 금속 알루미늄을 5kV정도의 고전압과 90mA의 전류로 electron beam에 의해 증발시켰다. 기판의 흡착율을 높ㅇ기 위해 기판에 500V로 bias 전압을 걸어 주었다. 증발된 금속 알루미늄 증기들이 plasmaso의 산소 이온들과 활성 반응을 이루어 알루미늄 기판 위에 Al2O3막을 형성하였다. 알루미늄 산화막을 분석하기 위해 XPS(X-ray Photoelectron Spectroscopy)로 화학적 조성을 조사하였는데, 알루미늄의 2p전자의 binding energy가 76.5eV로 측정되었다. 이는 대부분 증착된 알루미늄이 산소 이온과 반응하여 Al2O3로 형성된 것이다. SEM(Scanning electron Microscopy)과 AFM(Atomim Force microscopy)으로 증착박 표면의 topology와 roughness를 관찰하였다. grain의 크기는 10nm에서 150nm이었고 증착막의 roughness는 4.2nm이었다. 그리고 이 산화막에 전극을 형성하여 유전 상수와 손실률 등을 측정하였다. 이와 같이 plasma를 이용한 3-beam에 의한 증착은 금속의 산화막을 얻는데 유용한 기술로 광학 재료 및 유전 재료의 개발 및 연구에 많이 사용될 것으로 기대된다.

• The Korean Journal of Mycology
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• v.33 no.2
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• pp.69-74
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• 2005

Fibrinolytic enzyme has been isolated and purified from the edible mushroom, Lepista nuda. The apparent molecular mass of purified enzyme was estimated to be 34 KDa by SDS-polyacrylamide gel electrophoresis. The N-terminal amino acid sequence of the enzyme was Tyr-Pro-Ser-Pro-Ser-His-Gln-Thr-Ala-Val-Asn-Ala-Ile-Ile-X. It has a pH optimum at $7.0.{\sim}9.5$, suggesting that the purified enzyme is an alkaline protease. It shows the maximum fibrinolytic activity at $55^{\circ}C$. The fibrinolytic activity was inhibited by phenylmethylsulfonyl fluoride, indicating that the purified enzyme is a serine protease. The activity of the purified enzyme was totally inhibited by $Hg^{2+}$.

• Microbiology and Biotechnology Letters
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• v.30 no.4
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• pp.352-358
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• 2002

An amylase that hydrolyzes starch into maltopentaose as a main product was found in the culture supernatant of a strain of Bacillus megaterium KSM B-404 isolated from local soil. The enzyme was purified 129-fold by ammonium sulfate precipitation, DEAE-Toyopearl and Superdex 75 HR 10/30 column using a FPLC system. The molecular weight of the amylase was determined as about 68 kDa by using SDS-PAGE. Optimum pH and temperature of amylase were found to be $50^{\circ}C$ and pH 6.0~7.0, respectively. The enzyme was stable up to $60^{\circ}C$ by addition of $Ca^{2+}$ and its pH stability was in the range of 6.0~10.0. The activity of enzyme was inhibited by $Cu^{2+}$ $Hg^{2+}$ , and $Fe^{3+}$ and maintained by $Ca^{2+}$ and $Mg^{2+}$ . EDTA and pCMB also showed inhibitory effect to the enzyme. TLC and HPLC analysis of the products of the enzyme reaction showed the presence of maltopentaose(52%), maltotriose (25%), maltose (11%), glucose, and maltotetraose in the starch hydrolysates.

• The Korean Journal of Mycology
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• v.15 no.4
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• pp.224-230
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• 1987

Effects Of organic compound, photosensitizer and $K^+$ ion influx. On the light-induced ATPase of mitochondria in L. edodes purified by linear sucrose density gradient centrifugation were studied. The mitochondrial ATPase activity was investigated by various wavelength illumination at dark state. The mitochondrial ATPase was activated 139% and 128% by 10m mol dithiothreitol and 0.1m mol quinacrine, respectively. This enzyme also was activated 36% by 0.1m mol phenazine methosulfate as photosensitizer. But, 100 mg oligomycin and 1m mol phlorizin inhibited activity of enzyme to 48% and 45%, respectively. Its optimum wavelength was 690 nm on the effect of $K^+$ ion influx, its optimum pH and temperature were found to be 7.2 and $55^{\circ}C$.

• KSBB Journal
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• v.19 no.2
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• pp.159-163
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• 2004

The X-ray structure of the cydodextrin-glucanotransferase of Bacillus macerans was solved by molecular replacement at 2.0 ${\AA}$ resolution. The refined structure has a crystallographic R-factor of 16.6%, (R$\sub$free/ = 20.5%). A new metal binding site occupied by two Ca$\^$2+/-ions was found at an accession channel of the active site. There is a large accumulation of negative charges that bind these Ca$\^$2+/-ions, thereby connecting segment ${\beta}$13-${\alpha}$G (residue 254-276) to the main body of domain A (at ${\alpha}$H, residue 283-297). The segment 313-${\alpha}$G contains the catalytic residue Glu258 between subsite 1 and -1 and Tyr260 (subsite 2) which is located at the entrance of the active site. The Ca$\^$2＋/-site 3a,b may have a major role for the activity and specificity of this CGTase, although it is not even conserved for the a-subclass of CGTases.

• Journal of the Korean Electrochemical Society
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• v.3 no.2
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• pp.69-71
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• 2000

Redox-active calix[4]arenes with carboxylic acid and disulfide groups were prepared and spontaneous deposition on silver and gold surfaces was observed. Owing to their unusual structure, the calix[4]arenes exhibit selective affinity fur alkaline earth metal ions in aqueous media. When annular ionophores are immobilized on the surface, voltammetric and spectroscopic studies show the entrapment of metal ions. Furthermore, it was possible to reversibly capture and remove the ions using strong chelating agents such as ethylenediaminetetraacetic acid (EDTA).