• Proceedings of the Korean Society of Soil and Groundwater Environment Conference
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• 2003.04a
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• pp.438-441
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• 2003

남해 동부 연안 지역 지하수의 해수 침투 영향을 광역적으로 파악하기 위하여, 202개소의 지하수 시료를 채취하고 수리지구화학적 연구를 수행하였다. 전체 시료 중 14.4%가 500 $\mu\textrm{m}$/cm을 초과하는 높은 EC값을 나타내어 해수 영향을 시사해 주었다. 해수 영향 판단의 또 다른 파라메터로 사용되는 CI/HCO$_3$ 몰비는 전체 시료의 23.3%가 1.3 이상의 값을 나타내었다. 한편, 대표적으로 해수침투 영향 및 인위적 오염의 영향을 각각 반영하는 것으로 알려진 Cl과 NO$_3$의 농도에 관한 누적도수분포도를 작성하여 배경수질군과 오염영향군을 구분짓는 배경치(background concentration)를 구한 결과, 각각 Cl = 22.3 mg/1 및 NO$_3$= 23.1 mg/l로 나타났다. 이 두 파라메터의 농도 분포를 기준으로 하여 채취된 지하수 시료를 크게 4개의 그룹으로 나눌 수 있었다. 그 결과, 자연적 또는 인위적 기원의 오염이 배제된 그룹 1은 전체 시료의 31%, 자연적 오염(해수 영향)을 반영하는 그룹 2는 전체의 24%, 인위적 오염의 영향을 반영하는 그룹 3은 전체의 9%, 해수 영향 및 인위적 오염을 동시에 반영하는 그룹4는 전체의 36%로 나타났다. 또한 그룹2와 그룹4는 대부분 Na-Cl유형으로 진화하는 Ca-Cl유형을 나타내었다. 따라서, 여러 지구화학 방법에 의한 해수 영향 판단 결과는 서로 잘 일치하고 있음을 알 수 있다. 결국, 지구화학적 파라메터를 종합적으로 활용함으로써, 연안 지역 해수침투의 효과적인 파악은 물론 예측 및 방지, 복구에 효과적으로 사용될 수 있을 것으로 판단된다.으로 토양에서 유동 가능성이 있는 중금속만을 추출하였다. 분석실험은 토양의 Cd2+ 와 Pb2+를 대상으로 행하여졌으며, 여러 토양에서 추출 분석한 결과를 EDTA분석결과와 비교하였다. 실험결과, 중금속은 매우 신속하게 고분자 자성체와 결합하였고, 그 후 자성체를 외부 자장으로 모은 후 산으로 용해시키고, 결합된 중금속은 Graphite furnace AAS로 분석함으로써 빠르고 효율적으로 분석실험을 수행할 수 있음을 알 수 있었다. 한편, 실험에서 나타난 수치들을 비교 검토한 결과 토양 분석시 sandy soil에서는 자성체를 이용한 분석이 EDTA에 의한 방법보다 더 높은 추출도를 보인 반면, silt 함량이 많은 토양의 경우에서 EDTA분석에서 더 높은 중금속 추출도를 보였다.s 중에서 490nm와 555nm의 복합밴드를 포함하는 OC2 알고리즘(ocean color chlorophyll 2 algorithm)을 사용하는 것이 OC2 series 및 OC4 알고리즘보다 좋은 추정 값을 도출할 수 있을 것으로 기대된다.환경에서는 5일에서 7월에 주로 이 충체의 유충이 발육되고 전파되는 것으로 추측되었다.러 가지 방법들을 적극 적용하여 금후 검토해볼 필요가 있을 것이다.잡은 전혀 삭과가 형성되지 않았다. 이 결과는 종간 교잡종을 자방친으로 하고 그 자방친의 화분친을 사용할 때만 교잡이 이루어지고 있음을 나타내고 있다. 따라서 여교잡을 통한 종간잡종 품종육성 활용방안을 금후 적극 확대 검토해야 할 것이다하였다.함을 보이고 있다.X> , ZnCl$_{3}$$^{-}$같은 이온과 MgCl$^{+}$, MgCl$_{2}$같은 이온종을 형성하기 때문인것 같다. 한편 어

• Journal of Applied Biological Chemistry
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• v.60 no.3
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• pp.257-263
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• 2017

A cellulolytic strain Y2 was isolated from soil obtained in the Canadian Alpine region. The isolate was identified as Paenibacillus sp. Y2 by 16S rRNA sequencing. When grown in LB medium supplemented with carboxymethyl-cellulose (CMC), CMCase production increased to 122.0% of that observed in LB without CMC. Culture supernatant was concentrated by ultrafiltration and 80% ammonium sulfate precipitates were separated by Hi-Trap Q and CHT-II chromatography. The purified enzyme (EG-PY2) showed a homogeneous single band and the molecular mass was estimated to be 38 kDa by SDS-PAGE. Optimum pH and temperature of the enzyme were 4.5 and $30^{\circ}C$, respectively. The half-life of enzyme activity at 50 was 140.7 min, but the enzyme was drastically inactivated within 5 min at $55^{\circ}C$. The enzyme was highly activated to 135.7 and 126.7% by 5.0 mM of $Cu^{2+}$ or $Mg^{2+}$ ions, respectively, and moderately activated by $Ba^{2+}$ and $Ca^{2+}$ ions, whereas it was inhibited to 76.8% by $Fe^{2+}$, and to ${\leq}50%$ by $Mn^{2+}$, $Co^{2+}$, $Zn^{2+}$, and EDTA. The enzyme was activated to 211.5% in the presence of 0.5 M of NaCl and greatly tolerant to 3.15M of NaCl. The enzyme showed 2.98 times higher ${\beta}$-glucanase activity than CMCase activity. Based on these results, it can be concluded that EG-PY2 is an acidophilic, cold-active, and halotolerant endoglucanase. The authors suggest it is considered to be useful for various industrial applications, such as, fruit juice clarification, acidic deinking processes, high-salt food processing, textile and pulp industries, and for biofuel production from seaweeds.

• YAKHAK HOEJI
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• v.37 no.2
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• pp.129-135
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• 1993

Serratia sp. Y-4 was isolated from soil. Many characteristics of the strain and optimum cultivation condition for protease production were investigated.,The protease from Serratia sp. Y-4 was purified and studied for the properties of the enzyme. The isolated strain was identified to the genus Serratia. The strain was cultivated in 1%-casein, 0.5%-Na$_{3}$PO$_{4}$.7H$_{2}$O, 0.1%-NaCl, 0.05%-KCI, 0.02%-MgSO$_{4}$.7H$_{2}$O, 0.02%-CaCl$_{2}$.2H$_{2}$O, 0.02%-ZnSO$_{4}$.7H$_{2}$O, 0.02%-MnCl$_{2}$.4H$_{2}$O and 0.5%-soy bean oil at pH 7.0 for 35 hrs. The enzyme was purified about 5.89 fold from the culture broth with 31.1% recovery and 19,613 u/mg through ultrafiltration, ammonium sulfate, DEAE-sephacel and Superose-12 chromatography. The purified enzyme was identified as one band by isoelectric focusing, SDS- and native-PAGE. It has maxium activity at $37^{\circ}C$ and pH 9.0. Molecular weight of it is approx. 50 kD and pl is about 6.70. Its Km value for casein was 20 mg/ml. 5 mM-EDTA, 5mM-SDS, Ag$^{+1}$, Cu$^{+2}$, Hg$^{+2}$ and Pb$^{+2}$ inhibited the enzyme.

• Microbiology and Biotechnology Letters
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• v.17 no.4
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• pp.358-364
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• 1989

A crystalline alkaline pretense- producing Streptomyce sp. YSA-130 was isolated from soil in alkaline medium(pH 10.5). The optimum culture condition of Streptomyce sp. YSA-130 for the production of alkaline protease was as follows; 2.0% soluble starch, 1.0% soytone, 0.3% $K_2$HPO$_4$, 0.02% MgSO$_4$.7$H_2O$, 0.8% Na$_2$CO$_3$, pH 10.5, 3$0^{\circ}C$, and 12 hr. The alkaline pretense from the culture broth of Streptomyce sp. YSA-130 was purified about 24 folds by ammonium sulfate precipitation , dialysis, DEAE-cellulose ion exchange chromatography, gel filtration on Sephadex G-15 and crystallization. Optimum temperature and pH of purified enzyme were 6$0^{\circ}C$, and 11.5. Temperature and pH stability of purified enzyme were 5$0^{\circ}C$, and 5.5-12.0. Calcium ion was effective to stabilize the enzyme at higher temperature. The molecular weight of the purified enzyme was approximately 30,000. The purified enzyme was inactivated by diisopropyl flurophosphate(DFP) but not affected by metal ion, EDTA, sulfhydryl reagent and stable detergent.

• Microbiology and Biotechnology Letters
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• v.32 no.3
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• pp.230-237
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• 2004

In this study nitroreductase from Pseudomonas sp. HK-6 capable of degrading 2,4,6-trinitrotoluene (TNT) was characterized. Through a series of purification process including ammonium sulfate precipitation, DEAE-sepharose, and Q-sepharose, three different fractions I, II, and III having the enzyme activity of NTRs whose molecular weights were approximately 27 kDa were detected in fractions from HK-6 cells. Specific activity of the three fractions were approximately 4.85 unit/mg, 5.47 unit/mg, and 5.01 unit/mg, and concentrated to 9.0-, 10.1-, and 9.3-fold compared to crude extract, respectively. The optimal pH and temperature for the three NTR fractions were approximately 7.5 and $30^{\circ}C$, respectively. Metal ions, $Ag^{＋}$ , $Cu^{ 2+}$, $Hg^{2＋}$ inhibited approximately 70% of enzymes activities of all NTR, while $Fe^{2＋}$ did not stimulate or inhibit the activities. Monitoring the effect of chemicals on the enzyme activity revealed that those NTR fractions lost enzyme activity in presence of $\beta$-mercaptoethanol, but were a little influenced by dithiothreitol, EDTA and NaCl. The three NTR fractions demonstrated enzyme activities for nitrobenzene and RDX as well as TNT.

• Proceedings of the Korean Society of Postharvest Science and Technology of Agricultural Products Conference
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• 2003.04a
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• pp.119.1-119
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• 2003

단체 급식의 증가와 더불어 편의식품을 선호하는 소비 경향에 맞추어 최소가공한 과일의 갈변저해를 위한 저해제를 탐색하였다. 실험에 사용한 과일은 배와 감으로 각각 박피하여 속심을 제거한 후 배는 8조각으로 절단하고 감은 1~2cm 두께로 slice 하였다. 저해제는 1% ascorbic acid, citric acid, NaCl, MgCl$_2$, CaCl$_2$, oxalic acid, EDTA, raffinose, salicylic acit, sporix를 사용하였다. 또한 열수 추출한 오약, 계피, 황기, 당기, 건칡, 진피, 천궁, 감초 등도 저해제로 사용하였다. 최소가공한 과일은 저해제에 3분간 침지한 후 물기를 제거하고 tray에 포장하여 실온에서 저장하면서 colorimeter를 이용하여 갈변도의 변화를 측정하였다. 갈변 정도를 나타내는 $\Delta$E 는 시간의 경과에 따라 점차 감소하는 경향을 보였으나 배의 경우 변화 정도가 크지 않았다. NaCl, MgCl$_2$, CaCl$_2$를 처리한 배의 갈변 정도가 가장 적었다. cysteine을 처리한 구에서는 황화합물 냄새가 났다. 또한 oxalic acid를 처리한 구에서는 연화가 빠르게 일어났으며 저장 시간이 경과함에 따라 수분이 용출되었다. 한약재는 자체 색으로 인해 배의 색변화를 증가시켰으며 이취가 발생했다. 또한 저장 시간이 경과함에 따라 건조가 빠르게 일어나 관능적으로도 좋지 않은 결과를 나타냈다. 감에서는 CaCl$_2$, MgCl$_2$를 처리한 구에서 색의 변화가 가장 적었으며 cysteine은 색변화는 적었으나 배의 경우과 같이 이취가 발생하였다. 한약제는 계피와 진피를 처리한 감에서 색의 변화를 저해하는 효과를 보였다.를 처리하였을 경우 당귀, 천문동을 처리한 구에서 효과를 보였다. oxalic acid는 갈변저해에는 효과적이었으나 시간이 경과함에 따라 수분의 용출이 증가하였으며 물성의 변화도 컸다. 또한 ZnCl$_2$를 처리한 구에서는 이취 발생과 수분 용출이 컸으며 색의 변화도 컸다.내었다. 고온 단시간 처리구의 경우 저온 장시간 처리구와는 달리 저장 1일 후부터 그 농도가 다소 상승되었다가 다시 감소는 경향을 보였다. 한편 열처리하여 냉각시킨 직후 및 저장1주 후 사과의 pH, 산도, 당도, 경도, 과육의 갈변도 등을 조사하였던 바 대조구 및 처리구간에 일부 항목에 있어서는 약간의 차이를 나타내었다. 대치할 수 있을 것이라고 사료된다. 수분함량은 기계적 검사보다 관능검사와 더욱 높은 상관관계를 나타냈다.내었다. 항균활성이 우수한 생약재를 농도별로 활성을 조사한 결과, 물 추출물과 10% Ethanol 추출물 모두 낮은 농도에서도 우수한 항균활성을 나타내었다.취와 함께 점질성 갈변물질이 생성되었다. 이와 같은 결과로 볼 때, BAAG의 처리는 BAAC의 경우보다 가격은 저렴하면서도 항균력은 우수한 천연 항균복합제재로써 농산물 식품원료에 적용하여 선도유지 기간을 연장할 수 있는 효과를 기대할 수 있었다. 과일 등의 포장제로서 이용할 가능성을 확인하였다.로 [-wh] 겹의문사는 복수 의미를 지닐 수 없 다. 그러면 단수 의미는 어떻게 생성되는가\ulcorner 본 논문에서는 표면적 형태에도 불구하고 [-wh]의미의 겹의문사는 병렬적 관계의 합성어가 아니라 내부구조를 지니지 않은 단순한 단어(minimal $X^{0}$ elements)로 가정한다. 즉, [+wh] 의미의 겹의문사는 동일한 구성요 소를 지닌 병렬적 합성어([$[W1]_{XO-}$ $[W1]_{XO}$ ]

• Journal of environmental and Sanitary engineering
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• v.23 no.1
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• pp.25-31
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• 2008

A bacterial strain, Bacillus megaterium L-49 has been isolated and identified that produces alkaline ${\alpha}$-amylase. The cell is ellipsoidal, about $1.0-1.2{\times}3.0-3.6{\mu}m$ in diameter, Gram-positive, motile, and central partial central. Growth occurs in media containing 7% of NaCl. This strain could utilize D-glucose, lactose, xylose, sucrose, mannose, and maltose, and but it does not utilize D-fructose, and glycogen. Among the various concentrations of saturated ammonium sulfate, the retractation ratio in range of 70 to 100% was about 93%. However, in the case of acetone, it was about 98.7%. EDTA has activating effect and Ca2+ has no effect on alkaline ${\alpha}$-amylase activity. The alkaline ${\alpha}$-amylase has low thermal stability. The optimal temperature for reaction is $50^{\circ}C$. The alkaline ${\alpha}$-amylase activity maintained stabilizing at pH 6-11 and the optimal pH for reaction was 9-10.

• Journal of Microbiology and Biotechnology
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• v.8 no.6
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• pp.639-644
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• 1998

Extracellular serine proteases were isolated from a soil bacterium, alkalophilic coryneform bacterium TU-19, which have been grown in a liquid medium optimized at 3$0^{\circ}C$ and pH 10.0. Three different sizes, 120 kDa (protease I), 80 kDa (protease II), and 45 kDa (protease III), of serine pro teases were purified using Sephadex G-150 and QAE-Sephadex chromatography (Kang et al. 1995. Agric. Chem Biotech. 38: 534-540). SDS-PAGE showed that the 120 kDa protease was degraded into the 80 kDa protease in 20 mM Tris-HCI (pH 8.0) buffer solution. This degradation was enhanced in the presence of 0.5 M NaCl and 5 mM EDTA, but was inhibited in the presence of 5 mM $CaCl_2$. These results indicated that the $Ca^{2＋}$ ion seems to stabilize the 120 kDa protease like other proteases derived from Bacillus species. The $NH_2$-terminal amino acid sequences of the 10 residues of both proteases were completely identical: Met-Asn-Thr-Gln-Asn-Ser-Phe-Leu-Ile-Lys. In contrast to this, the 80 kDa protease has 1.5 times higher specific activity than the 120 kDa protease does (Kang et al. 1995. Agric. Chern. Biotech. 38: 534-540). Therefore the C-terminal of the 120 kDa protease seems to be autolyzed to the 80 kDa protease but this autolysis did not decrease the protease activity. Optimum pH and temperature of both 80 kDa and 120 kDa proteases were pH 10.5 and $45^{\circ}C$, respectively, and pH and thermal stability were almost identical. Several divalent ions except the $Fe^{2＋}$ ion showed similar effects on activities of both proteases, which are similarly resistant to three different detergents.

• Journal of Microbiology and Biotechnology
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• v.17 no.4
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• pp.624-631
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• 2007

Thermostable protease is very effective to improve the industrial processes in many fields. Two thermostable extracellular proteases from the culture supernatant of the thermophilic fungus Chaetomium thermophilum were purified to homogeneity by tractional ammonium sulfate precipitation, ion-exchange chromatography on DEAE-Sepharose, and Phenyl-Sepharose hydrophobic interaction chromatography. By SDS-PAGE, the molecular mass of the two purified enzymes was estimated to be 33 kDa and 63 kDa, respectively. The two proteases were found to be inhibited by PMSF, but not by iodoacetamide and EDTA. The 33 kDa protease (PRO33) exhibited maximal activity at pH 10.0 and the 63kDa protease (PRO63) at pH5.0. The optimum temperature for the two proteases was $65^{\circ}C$. The PRO33 had a $K_m$ value of 6.6mM and a $V_{max}$ value of $10.31{\mu}mol/l/min$, and PRO63 l7.6mM and $9.08{\mu}mol/l/min$, with casein as substrate. They were thermostable at $60^{\circ}C$. The protease activity of PRO33 and PRO63 remained at 67.2% and 17.31%, respectively, after incubation at $70^{\circ}C$ for 1h. The thermal stability of the two enzymes was significantly enhanced by $Ca^{2+}$. The residual activity of PRO33 and PRO63 at $70^{\circ}C$ after 60min was approximately 88.59% and 39.2%, respectively, when kept in the buffer containing $Ca^{2+}$. These properties make them applicable for many biotechnological purposes.

• Resources Recycling
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• v.31 no.2
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• pp.20-32
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• 2022

This study implemented a chelating agent (Ethylenediaminetetraacetic acid, EDTA) in purification to obtain high-purity vanadium pentoxide (V₂O₅) for use in VRFB (Vanadium Redox Flow Battery). V₂O₅ (powder) was produced through the precipitation recovery of ammonium metavanadate (NH₄VO₃) from a vanadium solution, which was prepared using a low-purity vanadium raw material. The initial purity of the powder was estimated to be 99.7%. However, the use of a chelating agent improved its purity up to 99.9% or higher. It was conjectured that the added chelating agent reacted with the impurity ions to form a complex, stabilizing them. This improved the selectivity for vanadium in the recovery process. However, the prepared V₂O₅ powder exhibited higher contents of K, Mn, Fe, Na, and Al than those in the standard counterparts, thus necessitating additional research on its impurity separation. Furthermore, the vanadium electrolyte was prepared using the high-purity V₂O₅ powder in a newly developed direct electrolytic process. Its analytical properties were compared with those of commercial electrolytes. Owing to the high concentration of the K, Ca, Na, Al, Mg, and Si impurities in the produced vanadium electrolyte, the purity was analyzed to be 99.97%, lower than those (99.98%) of its commercial counterparts. Thus, further research on optimizing the high-purity V₂O₅ powder and electrolyte manufacturing processes may yield a process capable of commercialization.