• Molecules and Cells
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• v.23 no.3
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• pp.370-378
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• 2007

A superoxide dismutase was purified 62-fold in seven steps to homogeneity from Methylobacillus sp. strain SK1, an obligate methanol-oxidizing bacterium, with a yield of 9.6%. The final specific activity was 4,831 units per milligram protein as determined by an assay based on a 50% decrease in the rate of cytochrome c reduction. The molecular weight of the native enzyme was estimated to be 44,000. Sodium dodecyl sulfate gel electrophoresis revealed two identical subunits of molecular weight 23,100. The isoelectric point of the purified enzyme was found to be 4.4. Maximum activity of the enzyme was measured at pH 8. The enzyme was stable at pH range from 6 to 8 and at high temperature. The enzyme showed an absorption peak at 280 nm with a shoulder at 292 nm. Hydrogen peroxide and sodium azide, but not sodium cyanide, was found to inhibit the purified enzyme. The enzyme activity in cell-free extracts prepared from cells grown in manganese-rich medium, however, was not inhibited by hydrogen peroxide but inhibited by sodium azide. The activity in cell extracts from cells grown in iron-rich medium was found to be highly sensitive to hydrogen peroxide and sodium azide. One mol of native enzyme was found to contain 1.1 g-atom of iron and 0.7 g-atom of manganese. The N-terminal amino acid sequence of the purified enzyme was Ala-Tyr-Thr-Leu-Pro-Pro-Leu-Asn-Tyr-Ala-Tyr. The superoxide dismutase of Methylobacillus sp. strain SK1 was found to have antigenic sites identical to those of Methylobacillus glycogenes enzyme. The enzyme, however, shared no antigenic sites with Mycobacterium sp. strain JC1, Methylovorus sp. strain SS1, Methylobacterium sp. strain SY1, and Methylosinus trichosproium enzymes.

• Journal of the Korean Applied Science and Technology
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• v.31 no.1
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• pp.1-6
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• 2014

Gemini type of cationic surfactant, namely ${\alpha},{\omega}$-alkane-bis(N-lauroyloxyethyl-N,N-dimethyl)-diammonium bromide was synthesized and confirmed by FT-IR and $^1H$-NMR spectroscopy. Their inhibition effect on corrosion of mild steel in 1 M HCl solution was tested by weight loss method. Surface tensions were measured by surface tensiometer Sigma 70. Their c.m.c. values evaluated by surface tension method was $4.01{\times}10^{-5}{\sim}4.99{\times}10^{-5}mol/L$. The Krafft point of the these surfactants were < $0^{\circ}C$. The emulsifying properties of synthesized cationic gemini surfactants and sodium dodecyl sulfate (SDS), tetradecyl trimethyl ammonium bromide (TTAB) was investigated. Of these, ${\alpha},{\omega}$-alkane-bis(N-lauroyloxyethyl-N,N-dimethyl)-diammonium bromide has been confirmed as a good emulsifier. The inhibition efficiency increases by increasing cationic gemini surfactant concentration. As a result, these surfactants are expected to be applied as corrosion inhibitors.

• Biotechnology and Bioprocess Engineering:BBE
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• v.7 no.4
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• pp.216-220
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• 2002

1,4-Benzoquinone reductase was purified to electrophoretic homogeneity from bovine liver, and the purified enzyme found to have a molecular mass of 29 kDa, as determined by sodium dodecyl sulfate- polyacrylamide gel electrophoresis The enzyme exhibited pH optimum between 8.0 and 8.5. The apparent fm for 1,4-benzoqulnone was 1.643 mM, and the apparent Km for NADH was 1.837 mM. Various divalent cations, such as Hg$\^$2+/, Cu$\^$2+/, and Zn$\^$2+/, exhibited strong inhibitory effects. The enzyme activity was also strongly inhibited by quercetin, dicumarol, and benzoic acid. Incubation of the enzyme with N-bromosuccinimide and pyridoxal 5’-phosphate led to inhibitions of 100% and 99%, respectively. Accordingly, these results suggest that trypto-phan and Iysine residues are Involved at or near the active sites of the enzyme.

• Journal of Microbiology and Biotechnology
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• v.11 no.2
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• pp.275-280
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• 2001

Bacteriocin J105 is a proteinaceous inhibitory substance produced by Latococcus latis subsp. lactis j105 isolated from Kimchi. Bacteriocin J105 was purified to homogeneity by the pH-dependent adsorption-desorption method and reverse-phase HPLC from the culture broth of Lactococcus lactis subsp. lactis J105. Purification of bacteriocin J105 resulted in a 1.47-fold increase in the specific activity and the recovery was 1.5%. Its molecular mass measured by the electrophoretic pattern in the sodium, dodecyl sulfate polyacrylamide gel was about 3.4 kDa. It was stable at $121^{\circ}C$ for 15 min at pH between 2 and 4. However, at pH above 5, bacteriocin was rapidly inactivated. Twenty-one residues from the N-terminal portion of bacteriocin J105 were sequenced using sequence analysis of lantibiotics. Bacteriocin J105 showed significant homology with known nisin A from lactic acid bacteria.

• Bulletin of the Korean Chemical Society
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• v.23 no.4
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• pp.545-549
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• 2002

A simple and rapid technique for the separation and preconcentration of lead in water and biological samples has been devised. Preconcentrationis based on the depositionof analyte onto a column packed with dithizone immobilized on sodium dodecyl sulfate coated alumina at pH $\geq$ 3. The trapped lead is eluted with 5 mL of 4 M nitric acid and determined by flame atomic absorption spectroscopy. A sample of 1 L, results in a preconcentration factor of 200 and the precision at 20${\mu}g$ $L^{-1}$ is 1.3%(n=8). The procedure is applied to tap water, well water, river water, vegetable extract and milk samples, and accuracy is assessed through recovery experiments and by independent analysis by furnace atomic absorption.

• Bulletin of the Korean Chemical Society
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• v.23 no.12
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• pp.1719-1723
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• 2002

1,5-diphenylcarbazone was immobilized on sodium dodecyl sulfate coated alumina. The alumina particle was effectively used for collection of mercury(II) and methylmercury cations at sub-ppb level. The adsorbed mercury was eluted with l mol $L^{-1}$ of hydrobromic acid solution. The mercury(II) was then directly measured by cold vapor atomic absorption spectrometry utilizing tin (II) chloride where as the total mercury was determined after the oxidation of methylmercury into the inorganic mercury. The methylmercury concentration was calculated by the difference between the value of total mercury and mercury (II). Mercury (II) and methylmercury cations were completely recovered from water with a preconcentration factor of 100 (for 1 L solution.) Relative standard deviation at Hg L ${\mu}gL^{-1}$ level 1.7%(n=8) and the limit of detection was 0.11 ${\mu}gL^{-1}$. The procedure was applied to spring water, well water and seawater and accuracy was assessed through recovery experiments.

• Archives of Pharmacal Research
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• v.19 no.6
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• pp.502-506
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• 1996

Protein X is one of the subunits of pyruvate dehydrogenase complex. The biological role of this protein has not been fully elucidated, mainly because of the difficulty in its dissociation from the tightly bound dihydrolipoamide acetyltransferase-protein X subcomplex. We have found that the detachment of protein X from acetyltransferase subunit can be easily accomplished by the cycles of freezing and thawing proces. Several lines of evidence including sodium dodecyl sulfate-polyacrylamide gel electrophoresis, N-terminal amino acid sequence analysis and acetylation with $[2^{14}C]$ pyruvate confirmed that the purified protein is protein X. The purified intact form of protein X was acetylated by $[2^{14}C]$ pyruvate in the presence of py-ruvate dehydrogenase subunit.The acetylation efficiency of this protein was lower than that of acetyltransferase and was not affected by the presence of acetyltransferase.

• Journal of Microbiology and Biotechnology
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• v.7 no.6
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• pp.386-390
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• 1997

A xylanase from the Bacillus sp. strain DSNC 101, isolated from soil, was purified to homogeneity by anion-exchange and hydrophobic interaction chromatography followed by gel filtration chromatography. The enzyme cleaved xylan, but not carboxymethyl cellulose, Avicel, soluble starch, and pNPX. The main product of oat spelts xylan hydrolysates was xylobiose. The xylanase had a molecular weight of 25 kDa determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Optimum temperature and pH for the xylanase activity were $50^{\circ}C$ and 6.0, respectively. $K_{m}\;and\;V_{max}$ of the enzyme for oat spelts xylan were 12.5 mg of xylan/ml and 869.5 unit/mg of protein, respectively. Xylanase was completely inhibited by Hg, Cu, and N-bromosuccinimide, but was stimulated by Ca, Co, and Mg.

• Journal of the Korean Applied Science and Technology
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• v.28 no.2
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• pp.140-145
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• 2011

Cationic gemini-surfactant, namely 1,4-butane-bis(N-alkanoyloxyethyl-N,Ndimethyl)-diammonium bromide was synthesized and their inhibition effect on corrosion of mild steel in 1 M HCl solution was tested by weight loss method. The synthesized product was confirmed by FT-IR and $^1H-NMR$ spectroscopy. Surface tensions were measured by surface tensiometer Sigma 70. Their c.m.c. values evaluated by surface tension method was $4.1{\times}10^{-5}{\sim}5.4{\times}10^{-5}$ mol/L. The Krafft point of the these surfactants were <0~$10.7^{\circ}C$. The emulsifying properties of synthesized cationic gemini surfactants and sodium dodecyl sulfate (SDS), tetradecyl trimethyl ammonium bromide (TTAB) was investigated. Of these, 1,4-butane-bis(N-lauroyloxyethyl-N,N-dimethyl)- diammonium bromide, CGL 14-4-14 has been confirmed as a good emulsifier. The inhibition efficiency increases by increasing cationic gemini surfactant concentration. As a result, these surfactants are expected to be applied as corrosion inhibitors.

• Membrane Journal
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• v.18 no.1
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• pp.7-25
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• 2008

Sodium dodecyl sulfate, which was anionic surfactant, at a concentration higher than its critical micellar concentration was added to calcium solution for forming micelles. Then aggregates were formed by adsorption or binding of calcium ions on the surface of micelles, and gathering between them, and then rejected by two kinds of ceramic membranes to remove calcium ions. As result, rejection rates of calcium were higher than 99.98%. And in our experimental range the higher TMP trended to increase the resistance of membrane fouling ($R_f$), total permeate volume ($V_T$), dimensionless permeate flux ($J/J_o$) and permeate flux (J) because TMP was driving force. And we investigated effects of $N_2$-back-flushing time and filtration time, that was back-flushing period, during periodic $N_2$-back-flushing on ceramic membranes. As result, optimal BTs for NCMT-623l ($0.07{\mu}m$ pore size) and NCMT-7231 membrane ($0.10{\mu}m$) were 10 sec and 15 sec, respectively. Also, optimal FT was 5 min for both membranes, and the frequent $N_2$-back-flushing could decrease membrane fouling effectively. Then, the optimal conditions resulting from our experiments for synthetic calcium solution were applied to groundwater using as washing process of soymilk package. As result, rejection rates of calcium were higher than 99.98%.