• Bulletin of the Korean Chemical Society
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• v.31 no.4
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• pp.905-909
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• 2010

Magnetic beads (Dynabeads$^{(R)}$) embedded in ~1 micron size polystyrene beads bearing surface carboxylic acid groups were modified with aminobenzyl ethylenediaminetetraacetic acid (ABEDTA) to concentrate or separate metal ions using pH gradients on micro and nano scales. The immobilization of ABEDTA was achieved by amide formation. The presence of the metal chelating functional group in the fully deprotonated form was confirmed by FT-IR. The chelation efficiency of beads was tested by determining metal ions in supernatant using GFAAS when pH gradients from 3 to 7. Mixtures of Cu and Mg and of Cd and Mn (at 10 ng/mL of metal) were separated as the difference in formation constant with the functional group of ABEDTA. The separation was repeated twice with relative standard deviation of <18%. A polydimethylsiloxane (PDMS) microchip column packed with EDTA-coated magnetic beads was optimized to concentrate metal ion for practical applications by eluting a Cu solution of micro scale at pH 3.

• Microbiology and Biotechnology Letters
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• v.18 no.1
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• pp.56-60
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• 1990

A bacterial strain of Brevibacterium sp. CHI was isolated from soil and used to produce an enzyme (nitrile hydratase) necessary for carrying out the bioconversion of acrylonitrile to acrylamide. Various immobilization methods and enzyme stability were investigated. The nitrile hydratase showed the maximum stability at pH 7 for the free cells. EDTA and phenyl methyl sulfonyl fluoride were selected as the protease inhibitor and the enzyme stability was evaluated by changing inhibitor concentration. Acrylamide beads were the best carriers among four carriers we tested in terms of stability and physicoehemical strength. The storage stability of the immobilized cells decreased with increasing acrylamide concentration of the gel phase at 4$^{\circ}C$, and was very low at acrylarnide concentration above 25%.

• Journal of Korean Society of Environmental Engineers
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• v.31 no.8
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• pp.663-672
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• 2009

In this studies, the adsorption test using Chlorella pyrenoidosa was conducted to examine the effect of Pb adsorption according to various immobilized methods such as Ca-alginate, K-carrageenan, and Polyacrylamide. From the results, the duration to need to reach adsorption equilibrium was delayed according to the immobilization. And, the higher adsorption capacity of immobilized Chlorella pyrenoidosa was represented in the higher concentration of Pb, the smaller amount of immobilizing agent, and the higher pH of solution. The maximum adsorption capacity of Pb was shown in the adsorption test using Chlorella pyrenoidosa immobilized with Ca-alginate even though it was sensitive pH. The adsorption results properly represented with Freundlich isotherm equations. And, pseudo second-order chemisorption kinetic rate equation was applicable to all the biosorption data over the entire time range. The FT-IR analysis showed that the mechanism involved in biosorption of Pb by Chlorella pyrenoidosa was mainly attributed to Pb binding of carbo-acid and amide group. Adsorbed Pb on immobilized Chlorella prenoidosa was easily desorbed in the higher concentration of desorbents(NTA, HCl, EDTA, $H_2SO_4,\;Na_2CO_3$). Among the several desorbents, NTA showed the maximum desoption capacities of Pb from Chlorella pyrenoidosa immobilized with Ca-alginate and K-carrageenan and EDTA was the most effective in Chlorella pyrenoidosa immobilized with polyacrylamide. The desoprtion efficiency in the optimum condition was 90.0, 83.0, and 80.0%, respectively.

• The Korean Journal of Food And Nutrition
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• v.14 no.3
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• pp.193-198
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• 2001

고정화 inulinase를 이용하여 inulin으로부터 fruc-tose 시럽을 연속적으로 생산하기 위하여 Bacillus sphaericus 188-1이 생성하는 inulinase를 부분 정제한후 5시간 NaIO$_4$로 산화시킨 cellulose에 고정화시킨 다음 이들의 성질을 조사하였다. 산화 cellulose에 고정화시킨 inulinase의 활성은 g당 47 Unit 이었고 고정화수율과 활성수율은 각각 41%와 39%이었다. 고정화시킨 inulinase의 작용 최적온도와 pH는 각각 5$0^{\circ}C$, pH 9.0이었고 5$0^{\circ}C$, pH 8.0~10.0에서 비교적 안정 하였다 고정화시킨 inulinas의 활성은 K+, Ca2+, Mn2+과 Hg2+에 의하여 활성화 되었으며 EDTA(10mM)에 의하여 심하게 저해되었다.

• Korean Journal of Food Science and Technology
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• v.22 no.4
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• pp.426-433
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• 1990

The conditions for immobilization of the partially purified ${\beta}-galactosidase$ form Bacillus subtilis HP4 and the properties of the immobilized enzyme have been investigated. The crude enzyme precipitated with cold acetone was purified about 68-fold through DEAE-cellulose and sephadex G-100 chromatography and its recovery was 19.9% The optimal conditions for Immobilization of enzyme were obtained in 2%(w/v) sodium alginate, 15%(v/v) enzyme solution and 2%(w/v) calcium chloride, and also the optimal stirring thme was 2 hours on the above conditions. The optimum temperature and pH values for immobilized enzyme were $55^{\circ}C$ and 6.5, respectively. Its residual activity was show 25% after heat treatment for an hour at $65^{\circ}C$, and found its high stability in pH 6.0 to 8.0. The enzyme activity was not affected b)· EDTA, 2-mercaptoethanol, KCN, protective agents, and other methal ions except Hg ion and Cu ion. The $K_m\;and\;V_{max}$ values of the immobilized enzyme on ONPG were $1.82{\times}10^{-2}M\;and\;3.57{\times}10^{-8}mole/min$, whereas those on lactose were $2.94{\times}10^{-2}M\;and\;1.68{\times}10^{-7} mole/min$, respectively. The remained enzyme activity for the immobilized enzyme was 95%t of original activity after storage of 40 days at $4^{\circ}C$, and when reused for 5 times was 81%. When skim milk(4.8% lactose) and 5% lactose solution were reacted with the immobilized enzyme(250 units/g) of lactose were 51% and 43%, respectively.

• Journal of the Korean Chemical Society
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• v.53 no.2
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• pp.144-151
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• 2009

An optode for cadmium ion determination has been designed by immobilization of dithizone on triacetylcellose membrane. When the optode membrane is introduced into a real samples containing cadmium, there is a color change from green to red, making it possible to use the change in absorbance at 611 nm as the analytical signal. The sensor could be used in the range of 0.3-3 ${\mu}g\;ml^{-1}$ (2.67-26.67 ${\mu}M$) of $Cd^{2+}$ ions with a limit of detection of 0.025 ${\mu}g\;ml^{-1}$ (25 ng $ml^{-1}$). The response time of optode is within 15 min depending on the concentration of $Cd^{2+}$ ions. It can be easily and completely regenerated by dilute EDTA solution. The effect of different possible interfering species has been examined and was shown the optode has a good selectivity. The results obtained for the determination of cadmium ion in polluted soil and water samples using the proposed optode was found to be comparable with the well-established atomic absorption method.

• Journal of fish pathology
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• v.12 no.1
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• pp.24-31
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• 1999

Optimization and standardization of solid phase enzyme immunoassay were done for the diagnosis of edwardsiellosis in fish. The analyzed degree of immobilized antibody on surface of solid phase with peroxidase saturation method showed the optimized result by using partially purified $50{\mu}g/ml$ of rabbit anti-E. tarda Edk-2 antibody in sodium bicarbonate buffer for overnight incubation to cover the surface of polystyrene beads. Optimized immunoreaction was observed in the treatment of $50{\mu}g/ml$ of biotin conjugated antibody followed extravidin-peroxidase diluted 1 : 2,000 in PBS. The detectable concentrations of the this method were $1{\times}10^5$ cells/ml and $1{\times}10^5$ cells/ml expressed as the source of antigen amount for EDTA extraction and heat extraction, respectively. High cross-reaction of solid phase ELISA with the prepared rabbit and-E. tarda Edk-2 was observed against E. tarda strains isolated from flounder suffering from edwardsiellosis in aquatic farms of Korea. It suggested that the potential of this solid phase of ELISA technique is very powerful for the application to different strains of E. tarda isolated in farms of many different areas.