• Journal of Life Science
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• v.7 no.3
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• pp.228-233
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• 1997

A thiol protease has been isolated and partially purified from encysted brine shrimp Artemia franciscana using a four-step procedure(filtration, salting out, gel filtration and ion exchange chromatography). The optimum pH of the enzyme for caseinolytic activity was appeared to be 3.0, and the enzymematic activity was stable up to pH 6.0 but lost completely at the pH higher than 8.0. The optimal temperature of the enzyme was appeared to be 35$^{\circ}$C, and ninety percent of the enzyme activity was lost at 45$^{\circ}$C. Various metal ions, e.g., zinc, copper, iron, inhibited the enzyme activity; however, heavy metal chelator, e.g., EDTA, stimulated the enzyme activity. The protease was concluded to be a member of the thiol group protease, since it was inhibited by thiol protease inhibitors and iodoacetate. The protease was also concluded to be a acid protease based on optimum pH.

• Membrane Journal
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• v.29 no.2
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• pp.96-104
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• 2019

The purpose of this paper is whether or not the in-situ restoration of the reverse osmosis (RO) membranes which its membrane function is lost is possible. The damaged RO membranes are double coated through the salting-out method by the poly(styrene sulfonic acid) sodium salt as the cationic exchange polymer and the polyethyleneimine as the anionic exchange polymer and also conducted the opposite order of the coating materials. And according to the concentration, time and ionic strength, the flux and rejection are measured for the coated membranes. Then the best coating condition is to apply for the RO membrane module of the household water purifier to know the possibility of the in-situ restoration for the commercial module. When the condition of the PEI 30,000 ppm (IS = 0.1)/PSSA 20,000 ppm (IS = 0.7) is applied, the rejection was enhance from 69% for the damaged module to 86% (90% for the pristine module).

• Journal of Environmental Science International
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• v.27 no.11
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• pp.1095-1104
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• 2018

The adsorption characteristics of bisphenol A (BPA) were investigated using activated carbon based on waste citrus peel (which is abandoned in large quantities in Jeju Island), denoted as WCP-AC, and surface-modified with various $P_2O_5$ concentrations (WCP-SM-AC). Moreover, coconut-based activated carbon (which is marketed in large amounts) was surface-modified in an identical manner for comparison. The adsorption equilibrium of BPA using the activated carbons before and after surface modification was obtained at nearly 48 h. The adsorption process of BPA by activated carbons and surface-modified activated carbons was well-described by the pseudo second-order kinetic model. The experimental data in the adsorption isotherm followed the Langmuir isotherm model. With increasing $P_2O_5$ concentration (250-2,000 mg/L), the amounts of BPA adsorbed by WCP-SM-AC increased till 1,000 mg/L of $P_2O_5$; however, above 1,000 mg/L of $P_2O_5$, the same amounts adsorbed at 1,000 mg/L of $P_2O_5$ were obtained. With increasing reaction temperature, the reaction rate increased, but the adsorbed amounts decreased, especially for the activated carbon before surface modification. The amounts of BPA adsorbed by WCP-AC and WCP-SM-AC were similar in the pH range of 5-9, but significantly decreased at pH 11, and increased with increasing ionic strength due to screening and salting-out effects.

• Journal of the Korean Society of Food Culture
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• v.25 no.1
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• pp.61-69
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• 2010

This study was carried out to investigate the effects of various kinds of commercial salts, including sun-dried (Korea), purified, and traditional salts on the chemical and sensory properties and growth of microorganisms involved in kimchi fermentation. Kimchi was prepared by salting in 10% NaCl solution for 2 hours followed by addition of other spices and fermentation at $20^{\circ}C$. The decreases in pH suggested that kimchi fermentation can be classified into 3 steps: initial, intermediate, and final stages. In texture analysis, the hardness and fracturability of traditional salt kimchi were higher than those of regular kimchi. From the sensory evaluation test for kimchi, sensory scores were high for traditional salt addition, especially taste, overall preference and texture. Among various microorganisms related to kimchi fermentation, the growth of Leuconostoc mesenteroides, Lactobacillus plantarum, Pichia membranaefaciens and Escherichia coli were examined. Based on the conditions of kimchi fermentation, a 2% and 5% concentration of each salt were studied. Also, the conditions of the cultures at $37^{\circ}C$ were examined. There was no considerable difference in the growth of Leuconostoc mesenteroides, Lactobacillus plantarum, Escherichia coli in the different kinds of salts. However, the growth of Pichia membranaefaciens was strongly inhibited by a 5% concentration of traditional salt during incubation at $37^{\circ}C$.

• The Korean Journal of Pesticide Science
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• v.18 no.4
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• pp.296-313
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• 2014

A QuEChERS (Quick, Easy, Cheap, Effective, Rugged and Safe) multiresidue method was developed for the simultaneous analysis of 124 pesticides in soil by LC-MS. The procedure involved liquid extraction of soil immersed with 0.2N $NH_4Cl$ by acetonitrile with 1% acetic acid, followed by anhydrous $MgSO_4$ and sodium acetate, and dispersive SPE cleanup with $MgSO_4$, primary secondary amine (PSA) and $C_{18}$. The extracts were analyzed with LC-MS/MS in ESI positive mode. Standard calibration curves were made by matrix matched standards and their correlation coefficients were higher than 0.99. Recovery studies for the validation were carried out using two type soils, loam and sandy loam, at four concentration levels (0.005, 0.01, 0.02, and 0.1 mg/kg). The recoveries of pesticides were in the range of 70-120% with < 20% RSD except 4 pesticides, Benfuracarb, Ethiofencarb, Pymetrozine, and Pyrethrin. This result indicated that the method using QuEChERS and LC-MS/MS could be applied for the simultaneous determination of pesticide residues in soils.

• Journal of the Korean Society of Food Science and Nutrition
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• v.2 no.1
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• pp.1-21
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• 1973

The muscle of abalone, Notohaliotis discus (REEVE), and top-shell, Turbo cornutus Solander, were examined for protein composition. Then paramyosins which are known as one of the important structural protein of the muscle fibrils were isolated from the both muscle and their physico-chemical properties such as solubility, salting-out behaviour, intrinsic viscosity, ATPase activity, etc. involving amino acid composition and N-terminal amino acid residues were investigated to elucidate phylogenie characteristics more intensively from the viewpoint of comparative biochemistry. The analysis of protein composition resulted in the following estimations: abalone muscle; water-soluble protein of 22 %, salt-soluble protein, 34%, alkali-soluble protein, 20%, and stroma protein, 24%, and top-shell muscle; water-soluble protein of 16%, salt-soluble protein, 30%, alkali-soluble protein, 29%, and stroma protein, 25%, respectively. It is demonstrated in sedimentation analysis that paramyosin and myosin-actomyosin account for approximately 65% and 35% of the salt-soluble protein of abalone, and that the composition of both sediments in top-shell was approximately 70% and 30%, respectively. The ultracentrifugally homogenous paramyosins isolated essentially according to Bailey's ethanol-dried method from both of the muscle showed a $S^{\circ}_{20,w}$ of 3. 14s for abalone and a $S^{\circ}_{20,w}$ of 3.50s for top-shell. The both paramyosins were commonly rich in arginine, aspartic acid, and glutamic acid, while scarcely contained proline and tryptophan, in rough accord with the other paramyosins thus far reported. It is clear that these gastropod paramyosins showed of having the characteristic N-terminal amino acid residues such as N-aspartic acid, N-valine, N-serine, and N-threonine in common. The abalone paramyosin completely salted in with KCl beyond $0.35{\mu}$ and the top-shell paramyosin beyond $0.30{\mu}$. The abalone paramyosin was salted-out between 18% and 30% saturation of ammonium sulphate and the top-shell paramyosin between 22% and 29% saturation. The intrinsic viscosities at abalone and top-shell paramyosins at $25^{\circ}C$ were estimated respectively to be 3.1 dl/g and 2.6 dl/g showing somewhat higher than the values for some other paramyosins from lamellibranchs. In regard with the ATPase activity, the para myosin specimens did not exhibit any significant activity over through the pH conditions of 5 to 9.5. irrespective of the presence of $Ca^{++}$ or $Mg^{++}$. So was the case with the abalone paramyosin prepared by a slightly modified Bailey's wet-extraction method.

• Journal of the Korean Chemical Society
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• v.47 no.4
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• pp.363-369
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• 2003

Selenized yeast (Se yeast) containing $0.1{\%}$(w/w) of selenium was obtained when the yeast was incubated at a selenium concentration of 1$1.14{\times}10_-3 M$ in rich medium. After washing several times, the inorganic selenium on the cell wall was confirmed with MBRT. There was no indication of inorganic selenium on the cell wall when the blue color in MBRT was stayed for 15 minutes. The selenized yeast was sonicated, then the selenium contained protein was obtained after salting out by ammonium sulfate at the concentration $80{\%}$ saturation. The seven protein bands were seperated by SDS-PAGE and the selenium concentration in protein was measured by ICP-AES. Analytical data showed that the large expressed protein band contained a relatively large amount of selenium. The proteins of the 47kDa was contained the concentrations of 69.5 ${\mu}$ Se/g of most many content. The protein (47 kDa) was seperated from PVDF membrane by tank-electroblotting. The isolated protein was hydrolyzed under acid condition and reacted with PITC. The derivatives of amino acids were analyzed by HPLC and compared with the data obtained from regular yeast. The resulting selenium-yeast was analyzed with the selenomethionine concentration of $2{\%}$ comparaed with general amino acids. The goal of this study is to analyze the selenium concentration in protein bands and measure the degree of biotransformation of selenomethionine in a specific protein.

• Journal of the Korean Society of Food Science and Nutrition
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• v.25 no.2
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• pp.240-248
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• 1996

To clarify the potentiality of sea cucumbers as dietary food, the effects of those glycoprotein on dietary proteins and physicochemical properties of those proteins were studied. Crude glycoprotein was efficiently extracted using 20mM sodium phosphate beffer(pH 7.0) and by salting out with 80% ammoniym sulfate saturation. The fractions obtained through the DEAE-cellulose ion exchange chromatography was identified as glycoprotein by Schiff's reagent and SDS polyacrylanide gel electro-phoresis. The yields of each glycoprotein from the three kinds of sea cucumbers were 0.814(red), 0.184(blue) and 0.232(black) and the molecular weights of the glycoproteins subunits were ranged from 20,000 dalton(blue and black) to 29,000 dalton(red), respectively. The electrophoretic patterns of the glycoprotein isolates were similar to each other and any significant difference in amino acid pattern was observed. Predominant arnino scids were Asx(aspartic acid and asparagine) and Glx(glutamic acid and glutamine) ; in contrast, histidine and methionine were below 2% as compared to total amino acids. water holding capacities of the glycoprotein isolates from red, blue and black cucumbers were equally 100% and emulsion activities ranged from 53% to 64%. In addition the emulsion stabilities were 7.04, 1.37 and 2.44, respectively. In vitro digestibility of some proteins(casein, SPI and squid) was decreased as increasing the level of the freeze dried sea cucumber powder and glycoprotein isolates. But squid protein was not affected.

• Korean Journal of Environmental Agriculture
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• v.20 no.4
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• pp.244-251
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• 2001

This study was performed to investigate the recovery efficacy of 2-methylisobomeol (2-MIB) and Geosmin, odor contaminants produced by algae, by pretreatment techniques, and also to investigate both adsorption characteristics and removal efficiency to get some information for the effective removal of 2-MIB and Geosmin by batch experiments. In pretreatment experiments, the best recovery efficiency of both odorants at 0.2 and $2\;{\mu}g/L$ in raw water was 30 mL of sampling size, 9 g NaCl for salting out headspace of sampling phase and 40 minutes of adsorption. At the best condition, the recovery efficiency of 2-MIB was 85% at $0.2\;{\mu}g/L$ and 95% at $2\;{\mu}g/L$, whereas the efficiency of Geosmin was lower than that of 2-MIB : 61% at $0.2\;{\mu}g/L$ and 81% at $2\;{\mu}g/L$. In batch experiments, the removal efficiency of the Geosmin and 2-MIB by adsorbents using distilled water were increased in comparison with raw water, the efficiency in raw water was little different by their concentrations. When these results were applied to the Freundrich adsorption isotherm, the K value of 2-MIB for zeolite, coal activated carbon, and coconut activated carbon was 0.671, 1.811, and 1.340, respectively, and the value of Geosmin was 0.6125, 1.771, and 1.5191, respectively. Thus the adsorption efficiency of 2-MIB and Geosmin was in the order of zeolite, coconut activated carbon, coal activated carbon.

• Korean Journal of Food Science and Technology
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• v.26 no.1
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• pp.81-87
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• 1994

Two different trypsin inhibitors, TRTI-1 and TRTI-2, were purified to near homogenity from Trichosanthes kirilowii root, by $0{\sim}90%$ saturated ammonium sulfate salting out, DEAE-Sephacel ion exchange chromatography, Sephadex G-50 gel filtration chromatography and trypsin-affinity chromatography. The molecular weight of TRTI-1 and TRTI-2 were estimated to be about 5,000 Da and 24,000 Da, respectively, by gel filtration and must be monomer and homodimer since they contain 4,000 Da and 10,000 Da each on SDS-polyacrylamide gel electrophoresis. TRTI-1 was stable after heating for at least 2 hr at $100^{\circ}C$ but TRTI-2 was completely inactivated after heating for 10 min at $90^{\circ}C$. When Bz-dl-Arg-pNA was used as a substrate of TPCK-treated trypsin, half-maximal inhibitions of TRTI-1 and TRTI-2 were observed at $0.8\;{\mu}M$ and 6\;${\mu}M$, repectively. Both TRTI-1 and TRTI-2 inhibited the hydrolysis of trypsin competitively and Km values were $0.97\;{\mu}M$ and $0.63\;{\mu}M$, respectively. Both TRTI-1 and TRTI-2 specifically inhibited trypsin but they did not inhibit other proteases tested, chymotrypsin, papain, elastase, collagenase, thermolysin, Nagarase, pepsin, and thrombin.