• Journal of the Korean Society of Food Science and Nutrition
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• v.25 no.6
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• pp.915-921
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• 1996

An alkaline pretense Producing microorganism was isolated from Korean traditional soy sauce and identified as Bacillus subtilis CCKS-111. The optimum culture condition of Bacillus subtilis CCKS-111 for the production of alkaline pretense was as follow: 2% soluble starch, 0.2% peptone, 0.1% (NB$_4$)$_2$S$_2$O$_{8}$ , 0.2% MgSO$_4$, pH 7.0, 35$^{\circ}C$ and 24hrs. The optimum pH and temperature for the enzyme activity of alkaline pretense producing Bacillus subtilis CCKS-111 were pH 9.0 and 5$0^{\circ}C$, respectively. The enzyme was relatively stable at pH 6.0~11.0 and at temperature below 4$0^{\circ}C$. The activity of the enzyme was inhibited by $K^{+}$ and Hg$^{2+}$, whereas Cu$^{2+}$ exhibited rather activating effects on the enzyme activity. Ethylenediaminetetraacetic acid and phenylmethanesulfonyl fluoride inhibited the enzyme activity. This indicates that this is serine pretense which requires metal ion group for the enzyme activity. Km value was 2.313$\times$10$^{-4}$ M/L, V$_{max}$ value was 39.216$\mu\textrm{g}$/min. This enzyme hydrolyzed casein more rapidly than the hemoglobin.lobin.

• Journal of Life Science
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• v.8 no.5
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• pp.614-621
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• 1998

An extracellular inulinase from Penicillium sp. which isolated from soil sample was purified to a single protein th-rough ammonium sulfate fractionation, DEAE-Sephacel ion exchange chromatography and Toyopearl HW 65 F gel filtration. The temperature and pH for the enzyme reaction were around 6$0^{\circ}C$ and 4.0, respectively. The enzyme was stable at 3$0^{\circ}C$-5$0^{\circ}C$ and in the pH range of 4 to 5. $CuCl_2$, $HgCl_2$ and EDTA inhibited the enzyme activity strongly. By contrast, $MnCl_2$ and $CaCl_2$ activated the enzyme activity. The molecular weight of the purified enzyme was esti-mated to be 77,000 dalton by SDS-polyacrylamide gel electrophoresis. The Km values of the enzyme for inulin were calculated to be $2.2\times10^{-3}$M. TLC analysis suggested that purified enzyme is exo-type inulinase. The NH2-terminal amino acid sequences of the purified enzyme was determined to be $NH_2$-X-Glu-Ser-Tyr-Thr-Glu-Lys/Leu-Tyr-Arg-Pro.

• Applied Biological Chemistry
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• v.47 no.1
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• pp.41-48
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• 2004

Cyclodextrin glucanotransferase (CGTase) of Bacillus sp. isolated from soil was purified and its enzymological characteristics were investigated. It was found that the production of CGTase reached to the maximum when the strain was cultured in the broth containing 0.1 % albumin, 2% $NH_4Cl$, 2% soluble starch and 0.2% $NH_2PO_4$ for 72 hrs at $37^{\circ}C$. The purity of CGTase was increased by 9.7 folds through purification procedures by the following column chromatography DEAE-cellulose ion exchange chromatography and Sephadex G-100, G-150 gel filtration and its specific activity was 528.0 unit/mg. The optimum pH and temperature for the CGTase activity were 8.0 and $80^{\circ}C$, respectively. The enzyme was stable in pH $8.0{\sim}11.0$ at $60{\sim}80^{\circ}C$. The activity of purified enzyme was inhibited by $Pb^{2+},\;Hg^{2+}$ and $Zn^{2+}$. When CGTase was treated with each 20.5 unit, 41 unit, 205 unit and 410 unit to investigate the transglucosylation to stevioside by purified cyclodextrin glucanotransferase, transglucosylation rate to stevioside was 74.9%, 75.7%, 68.7% and 57.9%. Brown effect was observed above the concentration amounting to 205 unit of our CGTase.

• The Korean Journal of Mycology
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• v.25 no.4 s.83
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• pp.297-304
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• 1997

Effects of cultural conditions on the production of xylanase by Tremella fuciformis, symbiotic fungi and mixed fungi were investigated. The optimum carbon source for high production of xylanase by T. fuciformis, symbiotic fungi and mixed fungi was xylose. The optimum nitrogen source for both T. fuciformis and symbiotic fungi was $KNO_3$, whereas mixed fungi was $(NH_4)_2SO_4$. The optimum culture period for high production of xylanase was 5 days for both T. fuciformis and mixed fungi, and 6 days for symbiotic fungi, respectively. The optimum temperature for T. fuciformis and symbiotic fungi was $40^{\circ}C$, and the corresponding value for mixed fungi was $45^{\circ}C$. Xylanase activity was high at pH 6 for T. fuciformis and symbiotic fungi, and pH 7 for mixed fungi. Except $Hg^{2+}$ and $Pb^{2+}$, metal ions in T. fuciformis inhibited the activity of xylanase, and, thermal stability of xylanase in T. fuciformis, symbiotic fungi and mixed fungi maintained 80% of activity until $50^{\circ}C$. The Michaelis constant (Km) of xylan was $6.25{\times}10^{-5}\;M$ in T. fuciformis, $5.6{\times}10^{-2}\;M$ in symbiotic fungi, $5.2{\times}10^{-2}\;M$ in mixed fungi.

• Applied Biological Chemistry
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• v.39 no.6
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• pp.460-465
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• 1996

The production of bacterial protease and its characteristics were investigated with Bacillus subtilis globigii CCKS-118 which was isolated from Korean traditional soy sauce. The optimum culture condition of the strain for the production of alkaline protease was as follow : 2% soluble starch, 0.2% yeast extract, 0.1% $(NH_4)_2SO_4$, 0.2% $MgSO_4$, pH 7.5, $35^{\circ}C$ and 20h rs. The optimum pH and temperature for the enzyme action of alkaline protease producing Bacillus subtilis globigii CCKS-118 were pH 9.0 and $50^{\circ}C$, respectively. The enzyme was relatively stable at $pH\;6.0{\sim}9.0$ and at temperature below $40^{\circ}C$. The activity of the enzyme was inhibited by $Hg^{2+}$ whereas $Cu^{2+}$ gave rather activating effects on the enzyme activity. The enzyme was inhibited by phenylmethane-sulfonyl fluoride indicating serine pretense metal ion group are required for the enzyme activity. Km value was $1.242{\times}10^{-4}M$, $V_{max}$ value was $25.99\;{\mu}g/min$. This enzyme hydrolyzed casein more rapidly than the hemoglobin.

• KSCE Journal of Civil and Environmental Engineering Research
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• v.35 no.4
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• pp.791-799
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• 2015

This study focuses on the algae growth restraining. Many researches on a critical damage from algae growth are published, but it is hard to find how th restrain. Abnormal algae increasing is a problem, because it makes red tides, biodeterioration, etc. Therefore this study aims to decrease the damage from algae growth. Some metal ions have been used microorganism killing materials from old times. Especially, Cu ions are highly effective. Based on these uses of the metal ions, a functional mortar which restrains algae growth is developed. The mortar contains soluble glass which dissolve in water. The soluble glass was made of Cu ions and phosphates. When the soluble glass is dissolved, Cu ions are soaked out stably from the soluble glass. Culture mediums which incubate algae were made to evaluate the developed mortar specimens. Culture mediums were filled with fresh water and sea water. Algae were incubated for fourteen days in culture mediums. The evaluating methods are measuring volume of the dissolved organic carbon and the chlorophyll. Using these two measurements, the mortar specimens are judged that can restrain algae or not. According to the result, the functional mortars of culture medium filled with fresh and sea water shows similar trend. The functional mortar for restraining algae growth performs that's role well.

• Korean Journal of Soil Science and Fertilizer
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• v.21 no.2
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• pp.129-134
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• 1988

Enzymatical properties of Streptomyces sp. S-45 producing chitinase and ${\beta}$-1.3-glucanase isolated from soil were investigated. Chitinase activity was 3.01(U/ml) and ${\beta}$-1.3-glucanase activity was 2.49(U/ml). The optimum medium for mycolytic enzyme production of strain was composed of 0.7% colloidal chitin, 0.3% glucose, 0.5% asparagine, 0.2% peptone, 0.01% NaCl, 0.01% $K_2HPO_4$ and 0.01% $MgSO_4{\cdot}7H_2O$ in intial pH 7.0. The optimal condition for mycolytic enzyme activities were: pH 6.5-7.0, $45-50^{\circ}C$. Enzyme activities were activated by metal ion as $10^{-2}M\;Co^{{+}{+}}$, $Cu^{{+}{+}}$, $Mn^{{+}{+}}$, $Al^{{+}{+}{+}}$ and $10^{-3}M\;Sn^{{+}{+}}$ but $Ag^{{+}{+}}$, $Hg^{{+}{+}}$ inhibited.

• Journal of Life Science
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• v.25 no.3
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• pp.345-348
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• 2015

An organic solvent stable lipase from solvent-tolerant Pseudomonas sp. BCNU 171 had an optimal pH of 8 and an optimal temperature of 37℃. This crude extracellular lipase from BCNU 171 exhibited increased stability in the presence of various types of solvents at high concentrations (25%, v/v). The lipase stability was found to be highest in the presence of xylene (137%), followed by toluene (131%), octane (130%), and butanol (104%). Overall, BCNU 171 lipase tended to be more stable than immobilized commercial lipase (Novozyme435) in the presence of organic solvents. Furthermore, BCNU 171 lipase maintained about 90% of its enzyme original activity in the presence of NH₄⁺, Na⁺, Ba²⁺, Hg²⁺, Ni²⁺, Cu²⁺, and Ca²⁺ion and significantly increased its enzyme activity in the presence of various emulsifying agents. Thus, the organic solvent stable lipase from Pseudomonas sp. BCNU 171 could be usable as a potential whole cell biocatalyst and for synthetic applications of enzymes for industrial chemical processes in organic solvents without using immobilization.

• Journal of the Korean Society of Food Science and Nutrition
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• v.40 no.9
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• pp.1321-1327
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• 2011

The microorganism producing an invertase (E.C. 3.2.1.26) was isolated from wine and tentatively identified as Saccharomyces cerevisiae by cellular fatty acid analysis. The invertase was purified to homogeneity by ammonium sulfate precipitant, dialysis, ion-exchange chromatography on DEAE-Sephadex A-50, and gel chromatography on Sephadex G-200 from the culture supernatant of Saccharomyces cerevisiae JS59. The specific activity and the purification fold of the purified invertase were 7620.9 unit/mg protein and 13.9, respectively. The molecular weight of the purified invertase was estimated to be 38.5 kDa by SDS-PAGE. The optimum pH and temperature for the invertase activity were pH 5 and $55^{\circ}C$, respectively. The invertase activity was relatively stable at pH 4~6 and temperature $55^{\circ}C$. The activity of invertase was inhibited by $Ag^{2+}$ and $Hg^{2+}$, but on the contrary, activated by $Co^{2+}$ and $Mn^{2+}$. Michaelis constant ($K_m$) for invertase reaction in sucrose solution was 11.5 mM. TLC analysis of the products produced in sucrose solution during invertase reaction showed the progressive presence of glucose and fructose in accordance with sucrose hydrolysis.

• Clean Technology
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• v.28 no.4
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• pp.323-330
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• 2022

Microfluidic paper-based analytical devices (μPADs) have recently been in the spotlight for their applicability in point-of-care diagnostics and environmental material detection. This study presents a double-sided printing method for fabricating 3D-μPADs, providing simple and cost effective metal ion detection. The design of the 3D-μPAD was made into an acryl stamp by laser cutting and then coating it with a thin layer of PDMS using the spin-coating method. This fabricated stamp was used to form the 3D structure of the hydrophobic barrier through a double-sided contact printing method. The fabrication of the 3D hydrophobic barrier within a single sheet was optimized by controlling the spin-coating rate, reagent ratio and contacting time. The optimal conditions were found by analyzing the area change of the PDMS hydrophobic barrier and hydrophilic channel using ink with chromatography paper. Using the fabricated 3D-μPAD under optimized conditions, Ni²⁺, Cu²⁺, Hg²⁺, and pH were detected at different concentrations and displayed with color intensity in grayscale for quantitative analysis using ImageJ. This study demonstrated that a 3D-μPAD biosensor can be applied to detect metal ions without special analysis equipment. This 3D-μPAD provides a highly portable and rapid on-site monitoring platform for detecting multiple heavy metal ions with extremely high repeatability, which is useful for resource-limited areas and developing countries.