• 한국식품과학회지
• /
• 제28권3호
• /
• pp.421-427
• /
• 1996

한국의 발초식품 중 가장 많이 섭취하고 있는 김치 중에서 배추김치를 각 지방에서 15개, 시중에서 판매 되고 있는 5개를 수집하여 김치의 특성을 고려하여 ethyl carbamate의 부분 정제를 시도하였다. 단계별 효율을 검색하면서 에틸아세테이트로 추출하여 불용성 고분자 물질과 수용성 물질을 제거하고, $C_{18}$ 수지로 소수성 색소를 제거한 후 알루미나, Florisil을 순차적으로 통과시켜서 수분과 비극성 물질을 제거하는 부분 정제법을 정립하였다. 가스 크로마토그래프 상에 분리된 표준 ethyl carbamate 피크와 같은 시간에 검출된 김치 추출액의 피크의 질량 분석 스펙트럼을 비교한 결과, 분자 이온 m/z 89와 m/z 74.62 토막 이온이 공통적으로 나타났다. 선택 이온 모드로 감도와 선택성이 가장 좋은 Mxlafferty 토막 이온 m/z 62에서 정량한 결과 ethyl carbamate의 범위는 검출 한계 농도 이하부터 4.6 ppb까지 분포하였으며, 김치의 숙성이 진행될수록 ethyl carbamate 농도는 증가하는 경향을 보였다. 이 양은 다른 식이는 고려하지 dskg고 김치에서만 하루에 섭취하는 ethyl carbamate 양으로 추정하였을 때, 사람에게 실질적으로 안전하다고 보고된 양 정도의 수준에 미치는 것으로 나타났다.

• 한국환경과학회지
• /
• 제13권12호
• /
• pp.1067-1078
• /
• 2004

Atmospheric particulate matters were collected by 8-stage non viable cascade impactor from October 2002 to August at Jeju City. Eight water-soluble ionic components $(Na^+,\;NH_{4}_{+},\;K^+,\;Ca{2+},\;Mg^{2+},\;CI^-,\;NO_{3}^-\;and\;SO_{4}^{2-})$ were analyzed by Ion Chromatography. The concentration of particulate matters and eight water-soluble ionic components were determined to investigate their size distributions. Particulate matters exhibited a tri-modal distribution with peak value around $0.9,\;4.0{\mu}m\;and\;9.5{\mu}m.$ In summer, the last peak value was lower than other season values likely due to particulate matter scavenged by rain water. Four ionic components $(Na^+,\;Ca^{2+},\;Mg^{2+}\;and\;CI^-)$ exhibited a bi-modal distribution in the coarse mode whereas three ionic components $(NH_{4}^+,\;K^+\;and\;SO_{4}^{2-})$ in the fine mode, with maximum peak value around $0.9{\mu}m.\;NO_{3}^-$ was found in both the coarse and the fine mode. The enrichment factor (E.F.) of each ionic components was calculated. Based upon E.F., it is considered that $Na^+,\;CI^-,\;and\;K^+$ in coarse paricle mode were delivered form oceanic source, but other components might have other source origins.

• 대한한의학방제학회지
• /
• 제22권2호
• /
• pp.15-24
• /
• 2014

Objectives : Gwakhyangjeonggi-san (GJS) which consists of 13 herbal medicines has been used to treat gastrointestinal disorders caused by common cold. This study was performed to compare GJS decoctions produced using different pressure levels for various extraction times. Methods : Decoctions were prepared by the pressure levels of $0kgf/cm^2$ (non-pressurized) or $1kgf/cm^2$ (pressurized) for 30-180 min. The extraction yield, total soluble solid content (TSSC), and hydrogen ion concentration (pH) were measured, and the contents of the nine marker compounds were determined using high performance liquid chromatography. Results : The higher pressure and longer extraction time significantly increased TSSC value, while decreased the pH value. However, only extraction time affected the extraction yield of pressurized decoction. Variation of the amounts of chemical compounds was shown in pressurized and non-pressurized decoctions during extraction time. The result of regression analysis showed that pressure and extraction time can influence to extraction yield, TSSC, pH, and the content of chemical compounds. Conclusions : This study suggests that the pressure and extraction time can significantly affect the extraction efficiency of components from GJS decoctions.

• Asian Journal of Atmospheric Environment
• /
• 제7권1호
• /
• pp.1-7
• /
• 2013

To establish the method for investigating the behavior of aerosol particles deposited on the leaf surface against fog water under natural conditions, scanning electron microscopy with energy-dispersive X-ray (SEM-EDX) analysis and wash water analysis by ion chromatography after the washing treatment were performed using leaves of white birch collected from low part of the tree crown and the top of the tree in Sapporo City, Hokkaido, northern Japan. Each of collected leaves was divided into two parts according to the treatment performed: leaf surface (adaxial side) was 1) untreated, and 2) washed with deionized water with a pipette. In untreated samples, many particles of various shapes, including soil particles and organic debris, were deposited on the surface. Particles containing S were found on the surface of samples collected from only low part of the tree crown. After the washing treatment, SEM-EDX analysis revealed that soil particles and particles containing S had been washed off with water, although some particles such as soil particles and organic debris still remained on the leaf surface. The major anion such as $SO{_4}^{2-}$ was detected in wash water of all samples, although the peak of S in X-ray spectra was not detected from samples collected at top of the tree. The combination of SEM-EDX analysis with wash water analysis indicated that $SO{_4}^{2-}$ was deposited on the leaf surface in dissolved state and/or in state of submicron particles. These results suggested that fog water could remove soil particles and particles containing S and $SO{_4}^{2-}$ from the leaf surfaces, but not all particles. There was no difference in sampling position in the tree crown. Our study suggested that combination with SEM-EDX analysis and wash water analysis would be effective for investigation of the behavior of particles on the leaf surface against fog water.

• Journal of Microbiology and Biotechnology
• /
• 제6권1호
• /
• pp.1-6
• /
• 1996

A bacterial strain NS70 producing an alkaline protease was isolated from soil samples taken near a hot spring and identified as Bacillus licheniformis by its morphological and physiological properties and cellular fatty acid analysis. The isolated alkaline protease was purified by ammonium sulfate fractionation, DEAE-, CM-, and Phenyl-Sepharose column chromatography. The molecular weight of the purified enzyme was estimated to be 32, 000 Da by sodium dodecylsulfate polyacrylamide gel electrophoresis. Its optimal pH and temperature for proteolytic activity against Hammarsten casein were 12 and $65^{\circ}C$, respectively. The enzyme was stable at alkaline pH range from 6.0 to 12.0, and fairly stable up to $65^{\circ}C$. The enzyme was inhibited by phenylmethylsulfonyl fluoride but not by EDTA and N-ethylmaleimide indicating that the enzyme is serine protease. Enzyme activity was markedly inhibited by $Hg^{2+}$ and $Cu^{2+}$. Autolytic phenomena were observed on purified protease NS70 but autolysis was reduced by the addtion of $Ca^{2+}$ ion or bovine serum albumin.

• Journal of Microbiology and Biotechnology
• /
• 제21권3호
• /
• pp.256-262
• /
• 2011

A 20.9-kDa metalloprotease was isolated from dried fruiting bodies of the wild basidiomycete mushroom Lepista nuda. The N-terminal amino acid sequence of the protease was seen to be ATFVLTAATNTLFTA, thus displaying no similarity with the sequences of previously reported metalloproteases. The protease was purified using a procedure that entailed ion-exchange chromatography on CM-Cellulose, Q-Sepharose, and Mono S, and FPLC-gel filtration on Superdex 75. The protease functioned at an optimum pH of 7.0 and an optimum temperature of $50^{\circ}C$. It was also noted that the protease demonstrated a proteolytic activity of 1,756 U/mg toward casein. The $K_m$ of the purified protease toward casein was 6.36 mg/ml at a pH of 7.0 and with a temperature of $37^{\circ}C$, whereas the $V_{max}$ was 9.11 ${\mu}g\;ml^{-1}\;min^{-1}$. The activity of the protease was adversely affected by EDTA-2Na, suggesting that it is a metalloprotease. PMSF, EGTA, aprotinin, and leupeptin exerted no striking inhibitory effect. The activity of the protease was enhanced by $Fe^{2+}$, but was curtailed by $Cd^{2+}$, $Cu^{2+}$, $Hg^{2+}$, $Pb^{2+}$, $Zn^{2+}$, and $Fe^{2+}$ ions. The protease also exhibited inhibitory activity against HIV-1 reverse transcriptase with an $IC_{50}$ value of 4.00 ${\mu}M$. The $IC_{50}$ values toward hepatoma Hep G2 and leukemia L1210 cells in vitro were 4.99 ${\mu}M$ and 3.67 ${\mu}M$, respectively.

• Journal of Microbiology and Biotechnology
• /
• 제24권7호
• /
• pp.925-935
• /
• 2014

A cold-adapted carbohydrate esterase, CEST, belonging to the carbohydrate esterase family 6, was cloned from Microbulbifer thermotolerans DAU221. CEST was composed of 307 amino acids with the first 22 serving as a secretion signal peptide. The calculated molecular mass and isoelectric point of the mature enzyme were 31,244 Da and pH 5.89, respectively. The catalytic triad consisted of residues Ser37, Glu192, and His281 in the conserved regions: GQSNMXG, QGEX(D/N), and DXXH. The three-dimensional structure of CEST revealed that CEST belongs to the ${\alpha}/{\beta}$-class of protein consisted of a central six-stranded ${\beta}$-sheet flanked by eight ${\alpha}$-helices. The recombinant CEST was purified by His-tag affinity chromatography and the characterization showed its optimal temperature and pH were $15^{\circ}C$ and 8.0, respectively. Specifically, CEST maintained up to 70% of its enzyme activity when preincubated at $50^{\circ}C$ or $60^{\circ}C$ for 6 h, and 89% of its enzyme activity when preincubated at $70^{\circ}C$ for 1 h. The results suggest CEST belongs to group 3 of the cold-adapted enzymes. The enzyme activity was increased by $Na^+$ and $Mg^{2+}$ ions but was strongly inhibited by $Cu^+$ and $Hg^{2+}$ ions, at all ion concentrations. Using p-nitrophenyl acetate as a substrate, the enzyme had a $K_m$ of 0.278 mM and a $k_{cat}$ of $1.9s^{-1}$. Site-directed mutagenesis indicated that the catalytic triad (Ser37, Glu192, and His281) and Asp278 were essential for the enzyme activity.

• 한국식품과학회지
• /
• 제22권1호
• /
• pp.7-12
• /
• 1990

산화촉진제 존재하에서의 트리글리세리드 분자종의 산화특성을 밝히기 위하여, 규산 컬럼으로 분획한 대두유 트리글리세리드에 $Fe^{2+}$와 heme 화합물인 myoglobin을 첨가하여 이들 산화촉진제가 트리글리세리드 각 분자종의 신화안정성에 미치는 영향을 조사하였다. 대두유 트리글리세리드에 대한 산화촉진효과는 본 실험의 조건에서는 myoglobin이 $Fe^{2+}$보다 켰으나, 트리글리세리드 분자종의 산화안정성에 있어서는 첨가한 산화촉진제의 종류에는 큰 영향을 받지 않았다. 또 산화촉진제의 효과는 분자종의 구성지방산의 불포화도가 낮은 경우는 뚜렷하였으나 불포화도가 높은 경우는 뚜렷하지 않았다. 그리고 산화촉진제를 첨가하였을 때 트리글리세리트 분자종의 산화안정성은 분자종의 이중결합수가 같은 경우는 구성지방산의 불포화도가 낮을수록 높았으나, 구성지방산의 불포화도가 같은 경우 공존하는 포화지방산 acyl기의 사슬길이에는 영향을 받지 않았다.

• 대한화학회지
• /
• 제29권6호
• /
• pp.615-622
• /
• 1985

옥살산과 아세트산 용액의 농도변화에 따른 우라늄과 바나듐의 음이온교환수지로부터의 용리거동 및, UV및 스펙트럼 변화로부터 이들 이온의 화학종과 평형관계를 연구하였다. 0.005~0.5M 옥산살산 용액속에서 우라늄과 바나듐은 각각 $UO_2(C_2O_4)_2^{2-}$, $UO_2(C_2O-4)_3^{4-}$ 및 $VO_2(C_2O_4)_2^{3-}$의 화학종으로 존재하고, 0.01~0.1M의 아세트산 용액에서 우라늄은 $VO_2(Ac)_2^0$, $UO_2(Ac)_3^{1-}$의 화학종으로 존재하며, 바나듐은 $VO_2^++2Ac^-=VO_2(Ac)_2^-$의 평형이 이루어짐을 확인하였다.

• 미생물학회지
• /
• 제30권2호
• /
• pp.71-77
• /
• 1992

Serratia marcescens ATCC 21074 의 세포배양액으로 부터 순수분리한 metalloprotease 의 자가분해성 및 안정성과 관련된 몇가지 효소적 특성을 조사하였다. 최적 반응온도와 pH 는 각각 37.deg.C, pH 8.0 였으며 안정성은 pH 5.0-11.0 범위에서, 온도의 경우 10-37.deg.C 에서 비교적 안정한 것으로 나타냈다. Differential scanning calorimeter 로 이효소의 열적 성질을 분석한 결과 변셩 시작 온도는 37.6 .deg.C, endothermic peak 온도는 43.2 .deg.C, enthaply 변화량은 -8.4 mJ/mg 이었다. 이 효소는 30.deg.C 에서 24 시간 동안 거의 자가분해가 일어나지 않았으나 변성된 단백질의 셩우 쉽게 자가분해되는 것으로 나타났다. 또한 이효소는 trypsin, .alpha.-chymotrypsin, elastase 에 의해서 분해되지 않았으나 분해되지 않았으나 thermolysin 에 의해서는 쉽게 분해되었다.