• Economic and Environmental Geology
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• v.50 no.5
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• pp.341-352
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• 2017

Along with Cs-137 (half-life: 30.17 years), Sr-90 (half-life: 28.8 years) is one of the most important environmental monitoring radioactive elements. Rapid and easy monitoring method for Sr-90 using Laser-Induced Breakdown Spectroscopy (LIBS) has been studied. Strontium belongs to a bivalent alkaline earth metal such as calcium and has similar electron arrangement and size. Due to these similar chemical properties, it can easily enter into the human body through the food chain via water, soil, and crops when leaked into the environment. In addition, it is immersed into the bone at the case of human influx and causes the toxicity for a long time (biological half-life: about 50 years). It is a very reductive and related with the specific reaction that makes wet analysis difficult. In particular, radioactive strontium should be monitored by nuclear power plants but it is very difficult to be analysed from high-cost problems as well as low accuracy of analysis due to complicated analysis procedures, expensive analysis equipment, and a pretreatment process of using massive chemicals. Therefore, we introduce the Laser-Induced Breakdown Spectroscopy (LIBS) analysis method that analyzes the elements in the sample using the inherent spectrum by generating plasma on the sample using pulse energy, and it can be analyzed in a few seconds without preprocessing. A variety of analytical plates for samples were developed to improve the analytical sensitivity by optimizing the laser, wavelength, and time resolution. This can be effectively applied to real-time monitoring of radioactive wastewater discharged from a nuclear power plant, and furthermore, it can be applied as an emergency monitoring means such as possible future accidents at a nuclear power plants.

• Analytical Science and Technology
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• v.6 no.1
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• pp.29-37
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• 1993

Some new podands containing phenyl(B), benzyl(Bz), pyridine(Py), quinoline(Q) and naphthalene(Np) as end-groups, and oxygen(O) and sulfur(S) in ether chains as donor atoms have been synthesized. The univalent cation binding characteristics of these podands have been studied by NMR titration and solvent extraction. By NMR titration we have found that the most of podands form 1:1 complexes with $Ag^+$ ion. Especially, the substituted sulfur atoms in ether chains show the effects to enhance the stabilities. We also carried out the extractions of univalent cation picrates including alkaline metal, $Ag^+$, $Tl^+$ and $NH_4{^-}$ ions from aqueous to chloroform layer by using these podands. We found that the extractabilities of $Ag^+$ ion with the quinoline-containing podands such as, $Q_2O_4$, $Q_2O_5$ and $BQO_5$ were 86.8, 86.6 and 48.0% respectively, but the naphthalene-containing podands such as, $Np_2O_4$ and $Np_2O_5$ extracted quite small amount. Otherwise, in cases of $Bz_2O_3S_2$(89.4%), $B_2O_2S_2$(96.8%), $B_2O_3S_2$(58.9%), $Py_2O_2S_2$(58.8%), $Py_2O_3S_2$(42.1%), and $B_2O_4S$(15.0%), interestingly, $Bz_2O_3S_2$ which have sulfur atoms and benzyl groups showed the highest extraction selectivity for $Ag^+$ ion. This result seems due to not only the strong interaction of $Ag^+$ ion with sulfur donors according to the HSAB theory, but also the effective ${\pi}-{\pi}$ stacking interaction between two aromatic end-groups which is enhanced by the flexible methylene spacing group in benzyl groups instead of phenyl groups. The extraction coefficients gave the similar tendency as the extractabilities and the stabilities. From these results, it could be concluded that the predominant factor affected to extraction coefficients is the stabilities, which are strongly influenced by the structures of podands.

• Korean Journal of Food Science and Technology
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• v.7 no.4
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• pp.229-237
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• 1975

An attempt was made to utilize the enzyme produced by Asp. oryzae as meat tenderizer. The production, purification, and various properties of proteinase produced by Asp. oryzae were investigated. Results obtained are as follow; 1. A strain which had the highest proteolytic activity was selected among 9 Aspergillus species. 2. Culture medium consisted of wheat bran 10g, 2% glucose, 0.03% urea and 0.1% $MgSO_4$ (pH 6.5). Mold was incubated at $30^{\circ}C$ for 3 days. 3. Enzyme extract from culture medium were fractionated with ammonium sulfate and purified by Sephadex G-75 column chromatography. 4. When pH of reaction mixture was controlled, maximal activity of proteinase by Asp. oryzae was obtained at pH 3, pH 6.6, $8.4{\sim}8.5$ and pH 10.0 to 10.5. Those results were interpreted to show that enzyme consists of acid proteinase, neutral proteinase and alkaline proteinase. Enzyme was stable at pH 6 to 10. 5. Opt. temperature for proteinase activity was $50^{\circ}C$, but enzyme was stable up to $40^{\circ}C$. 6. The proteinase was inhibited by $Ag^+$. It was also inhibited by EDTA. 7. When myofibrillar proteins were treated by proteinase from Asp. oryzae, ATPase activities of myofibrillar proteins changed remarkably. Accordingly, it was concluded that proteinase produced by Asp. oryzae were able to be used as meat tenderizer.