• Food Science and Preservation
• /
• v.10 no.2
• /
• pp.246-251
• /
• 2003

Pretense produced by Bacillus subtilis PANH765 was purified from culture supernatant by using ammonium sulfate fractionation DEAE-cellulose ion exchange chromatography, and gel filtration with Sephacryl S 200 HR and Sepharose CL-6B. DEAE-cellulose ion exchange column chromatography, separated the pretense into one fraction. This fraction was further purified using Sephacryl S 200 HR and Sepharose CL-6B gel titration. The molecular mass of pretense was estimated to be 35.0 kDa by the SDS-PAGE and gel filtration using Sepharose CL-6B. The results indicated that the purified pretense are monomeric proteins. Specific activity and purification folds of pretense were 657 U/mg and 4.35, respectively. The optimum temperature, optimum pit stable at a temperature range and pH ranges for the purified protease were 65$^{\circ}C$, 7.05, 50 ∼ 75$^{\circ}C$ and 6.0 ∼ 7.5, respectively. The pretense activity was decreased by the presence of PMSF and DFP, which the protease activity was increased by the presence of Na$\^$+/, K$\^$+/, Mg$\^$2＋/ and NH$_4$$\^$+/ ions.

• Proceedings of the Materials Research Society of Korea Conference
• /
• 2005.05a
• /
• pp.262-262
• /
• 2005

• Journal of the Korean Ceramic Society
• /
• v.22 no.1
• /
• pp.35-39
• /
• 1985

Synthetic mica $NaMg_{2.5}(Si_4O_{10})F_2 (Na-TSM)$ was treated with HCl solution and H-type exchange resin to investigate the chemical stability and the ion exchange by measuring the dissolution of chemical components and the exchanged $H^+$ ion. The replacement of $Na^+$ ion occurred in contact with HCl solution and H-type ion exchange resin at the surface of Na-TSM particles reached $Na^+$ ions at maximum value of 70~80%. $Mg^{2+}$ ion of octahedral layer became to dissolve from the pH2 solution and th amount of it dissolved in-creased almost proportional to $H^+$ ion concentration from around 0.02N $H^+$ ion equilibrium concentration. The crystalline structure of Na-TSM was destructed by dissolution of Mg2+ ion in cncentrated hydrochloric acid solution and resulted silica gel precipitation.

• Journal of Life Science
• /
• v.9 no.1
• /
• pp.45-49
• /
• 1999

Seaweed alginate was acetylated by activated carbon immobilized Pseudomonas syringae in a fluidized bed, up-flow reactor. The acetylation degree of seaweed alginate was about 30%. Calcium-acetylated seaweed alginate gel bead was made and compared to calcium-seaweed alginate gel bead by the scanning electron microscopy (SEM). Structural difference of two gel beads may results from increased viscosity and decreased affinity of acetylated seaweed alginate for calcium ion. On the basis of interior and exterior structure of calcium-acetylated seaweed alginate gels and property of acetylated seaweed alginate, it seems that acetylated seaweed alginate is used for the supporter for electrophoresis and packing materials for liquid chromatography and gel filtration.

• Journal of the Korean Institute of Electrical and Electronic Material Engineers
• /
• v.17 no.6
• /
• pp.608-614
• /
• 2004

The gel polymer electrolyte was prepared by radical polymerization using tetra(ethylene glycol) diacrylate and tri(ethylene glycol) dimethacrylate to investigate affect of the number of ethylene oxide. The gel polymer electrolyte showed good electrochemical stability up to 4.5 V vs. Li/Li and high ionic conductivity at various temperatures. The lithium-ion polymer batteries with the gel polymer electrolyte, tetra(ethylene glycol) diacrylate- and tri(ethylene glycol) dimethacrylate-based, also represented good electrochemical performances such as rate capability, low-temperature performances and cycleability. However, the cell with tri(ethylene glycol) dimethacrylate, which has three ethylene oxide, showed better electrochemical performance.

• Proceedings of the Korean Vacuum Society Conference
• /
• 1997.02a
• /
• pp.118-119
• /
• 1997

• 한국전기화학회:학술대회논문집
• /
• 2003.04a
• /
• pp.21-21
• /
• 2003

• BMB Reports
• /
• v.32 no.3
• /
• pp.239-246
• /
• 1999

A tripeptidase (PepT) was purified to homogeneity from Bacillus subtilis through four sequential chromatographies including DEAE-Sepharose ion exchange, hydroxylapatite, mono-Q FPLC ion exchange, and Superose-12 FPLC gel filtration. The apparent molecular mass of the enzyme was 49,200 Da and 51,400 Da as determined by sodium dodecylsulfatepolyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration chromatography, respectively, and the enzyme exists in a monomeric form. The physicochemical properties of the enzyme were as follows: optimum pH at 7.5, optimum temperature at $60^{\circ}C$, and pI at 4.9. The $K_m$ and $V_{max}$ values of the enzyme were 4.3 mM and 2.5 mmol/min/mg, respectively, with MetAla-Ser as substrate. The B. subtilis PepT requires $Co^{2+}$ ion(s) for activation, while it is inactivated by EOTA and 1,10-phenanthroline, suggesting that it is a metalloprotein. The enzyme was not inhibited by any of serine protease, aspartic protease, or leucine aminopeptidase inhibitors. The enzyme showed comparable activities towards four different substrates including Met-Ala-Ser, Leu-Gly-Gly, Leu-Ser-Phe, and Leu-Leu-Tyr. The amino terminal sequence of PepT determined by Edman degradation was found to be MKEEIIERFTTYVXV and turned out to be identical to that of PepT deduced from a cloned B. subtilis pepT.

• Journal of the Korean Applied Science and Technology
• /
• v.29 no.2
• /
• pp.278-285
• /
• 2012

Effects of ion species on the expansion behavior of Poly(styrene sufonic acid)(PSSA) hydrogel were investigated in aqueous solution of selected anions, cations and hydrophobic ions. The deexpansion extent of Poly(stylene sulfonic acid) gel follow the sequence $SCN^-$<$Br^-$<$Cl^-$<$F^-$ in low concentration solutions due to the destabilization of anions to hydrogen bond between ${SO_3}^-$ and water. The deexpansion in cations followed the sequence of counterion interactions between ${SO_3}^-$ and cations. It was discussed the effects of ions on the hydrogen bonding through ${SO_3}^-$ and phenyl ring in salt solutions. Other interactions, such as the cation-${\pi}$ interaction, hydrophobic interaction, and dispersion force, contributed to the ion specific swelling of PSSA hydrogel.

• The Korean Journal of Food And Nutrition
• /
• v.7 no.1
• /
• pp.23-28
• /
• 1994

Soybean $\beta$-amylase was purified by DEAE-cellulose ion exchange chromatography, Sephadex G-100 gel chromatography, CM Sephadex C-50 ion exchange chromatography and CM Sephadex C-50 ion exchange rechromatography The purified enzyme showed 1, 020 unit/mg of specific activity. The purified enzyme was identified as homogenious by disc PAGE and analysis of reaction product.