• Title/Summary/Keyword: 정제 부분

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석유산업 대외개방 영향과 대응방안 (상)

  • Korea Petroleum Association
    • Korea Petroleum Association Journal
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    • no.9 s.208
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    • pp.42-52
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    • 1998
  • 이 자료는 산업자원부와 정유5사 및 에너지경제연구원등이 석유산업 대외개방에 대비하여 공동으로 마련한 연구자료 중 「정제업 및 주유소업 대외개방의 영향 및 대응방안」 부분을 발췌한 것이다. <편집자 주>

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석유산업 대외개방 영향과 대응방안(하)

  • Korea Petroleum Association
    • Korea Petroleum Association Journal
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    • no.11 s.209
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    • pp.85-96
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    • 1998
  • 이 자료는 산업자원부와 정유 5사 및 에너지경제연구원등이 석유산업 대외개방에 대비하여 공동으로 마련한 연구자료 중 「정제업 및 주유소업 대외개방의 영향 및 대응방안」부분을 발췌한 것이다. <편집자 주>

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Development of Efficient Address Cleaning System for CRM (CRM 위한 효율적인 주소 정제 시스템 개발)

  • Park, Gyu-Jin;Song, Won-Mun;Kim, Eun-Ju;Kim, Myeong-Won;Han, Young-Jin;Rim, Young-Gun
    • Proceedings of the Korean Information Science Society Conference
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    • 2007.06c
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    • pp.313-318
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    • 2007
  • 최근 기업들은 인터넷, 이벤트 등의 다양한 매체를 통해 방대한 양의 고객 주소 데이터를 수집하고 있다. 이렇게 수집된 고객 주소 데이터는 DM발송 등을 통한 마케팅 및 캠페인에 활용함으로써 서비스의 질을 향상시키고, 고객의 충성도를 높인다. 그러나 사용자가 입력한 주소의 일부는 띄어쓰기가 정확하지 않은 주소, 정보가 누락된 주소, 오타가 있는 주소, 구주소 등의 입력으로 주소의 표준 형태를 갖지 않거나 일관성이 없다. 또한 2007년 4월부터 부분시행예정인 신주소 체계를 위해 기존의 주소를 적절히 변환해야만 한다. 본 논문에서는 부정확하거나 불완전한 주소를 표준 형태의 정확한 주소로 변경하는 효율적인 주소 정제 시스템을 제안하고 개발한다. 본 시스템은 먼저 입력 주소의 유니코드 분석을 통한 한글 입력 오류 교정과 해쉬테이블을 이용한 건물명의 표준 형태 변환을 수행한다. 이 과정이 완료된 주소들은 주소 트리 모델 구축을 통해 띄어쓰기가 부정확한 주소의 처리, 역주소테이블(inverted address table)을 이용한 누락 주소의 처리(enrichment), 구주소에 대한 트리 모델을 생성한 신주소 변환 처리 등의 프로세스를 통해 정제하게 된다. 실험을 위해 오타와 띄어쓰기, 누락된 정보가 있는 주소를 생성하여 타 정제 시스템과 성능을 비교하였다. 생성된 데이터를 비교한 결과 기존 주소 정제 시스템의 오류율 7.5% 보다 제안된 방법으로 개발된 본 시스템의 오류율이 0.45%로 낮음을 확인하였다.

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Partial Purification and Properties of Non-specific $\beta$ -fructofuranosidase Produced by Bacillus subtilis (Bacillus subtilis가 생산하는 비특이적 $\beta$-fructofuransoidase의 부분정제 및 특성)

  • 송근섭;엄태붕
    • Microbiology and Biotechnology Letters
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    • v.18 no.5
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    • pp.484-489
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    • 1990
  • An intracellular inulase ( fJ-fructofuranoside fructohydrolase, EC 3.2.1.26) from Bacillus subtilis has been partially purified and its mode of action and general properties were studied. The enzyme had an apparent molecular weight of 49,000 as estimated by gel filtration and its pI point was 5.2. Substrate concentration studies showed an apparent Km of 10 mM for sucrose and of 18 mM for raffinose. The enzyme was an acid-labile protein with a pH optimum of 6.6. The optimum temperature was 50$^{\circ}$C. The enzyme acts on straight chain oligo- and poly-fructosides of the inulin series via a exo-wise cleavage mechanism, as well as on sucrose.

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Isolation and Partial Characterization of Cysteine Proteinase from Sparganum (스파르가눔 총체에서 분리한 cysteine proteinase의 정제 및 부분 특성)

  • 송철용;최동호
    • Parasites, Hosts and Diseases
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    • v.30 no.3
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    • pp.191-200
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    • 1992
  • A proteolytic enzyme was purified from the tissue extract of spargana (plerocercoids of Spirometra erinacei) by DEAE-Trisacryl M ion exchange chromatography and thiopropyl-sepharose affinity chromatography resulted in a 21-fold purification. The proteinase activity was assayed with a synthetic fluorescent substrate, carbobensoxy-phenylalanyl-7-amiso-4-trifluoromethyl-coumarin. SDS-polyacplamide gel electrophoresis of the purified materials revealed a single 28,000 dalton band. Inhibitor profiles of the band indicated that it belonged to cysteine endopeptidases. It exhibited identical pH curves with optimum at pH 5,5, and 50% activity from pH 4.7 to 8. It could completely degrade collagen chains to three identical products. It also showed some activity on hemoglobin. Furthermore, the band on immunoblots was reactive to the sera of sparganosis patients. These results suggest that the proteolytic enzyme belongs to cysteine proteinase which plays a role in the tissue penetration. Also it may be used as the antigen for diagnosis of active sparganosis.

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Bacillus stearothermophilus 에서 부분 정제한 Cytosine Deaminase 의 특성

  • 장영채;이경형;김성영;조윤래;김종규
    • Korean Journal of Microbiology
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    • v.30 no.4
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    • pp.305-309
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    • 1992
  • Cytosine deaminase (EC 3.5.4.1) from BaciNus stc~urorhermophilus was partially purified 7.2-fold with an overall yield of 52.7%. The partially purified enzyme deiiminated cytosine only.but not 5-methylcytosine and 5-fluorocytosine. The apparent Michaclis constant. Km valuefor cytosine was 5.9 mM. The enzyme was relatively stable in the range of pH 4.0 to 7.0.furthermore extremely thermo-stable : more than 75'X) of the activity was remained afterheating at 80$^{\circ}$C for I0 min at pH 6.5. The enzyme had a pH optimum at around pH7.0 to 7.5. and temperature optimum at 35 to 31$^{\circ}$C. And the activation energ (En value)determined from an Arrhenius plot was 26 Kcal/mol. The enzyme activity was stronglyinhibited by heavy metal ions such as Cd", Hg". Cut' at 1 mM, anJ by o-phenanthroline,and p-chloromcrcuribcnzoate at I mM. But the enrymc activity was activatetl increased byGMP, and CMP at 1 mM.ased by GMP, and CMP at 1 mM.

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Partial Purification and Characterization of Enzymes Involved in the Processing of Pre-M1 RNA at the 3' End in Escherichia coli (대장균에서 선구-M1 RNA의 3'-말단 가공에 관여하는 효소들의 부분 정제와 그 특성 조사)

  • Kim, Ha Dong;Ko, Jae Hyeong;Cho, Bong Rae;Lee, Young Hoon;Park, In Won
    • Journal of the Korean Chemical Society
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    • v.43 no.3
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    • pp.307-314
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    • 1999
  • Ml RNA, the RNA component of RNase P from Escherichia coli, is produced by 3' processing of pre-Ml RNA, a major primary transcript of the rnpB gene. The enzyme fraction containing the processing activity was partially purified and characterized. Since exposure of the active fraction to the high salt condition results in the inactivation of the processing activity, the processing enzyme seems to be an enzyme complex composed of multiple enzymes. The enzyme fraction loses the processing activity when treated with the chemical nuclease lead(II) ion, but regains its activity by the addition of RNA isolated from the enzyme fraction itself, suggesting that an RNA molecule(s) may be essential for the processing activity. Analysis of cleavage sites produced by the partially purified enzyme fraction also implies that the 3' processing occurs by multiple enzymes and at least in two distinct pathways.

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Antibacterial Activity of actobacillus sp. KJ-5 Isolated from Pig Feces (돼지분변에서 분리한 Lactobacillus sp. KJ-5의 항균특성)

  • 박경준;유연우
    • KSBB Journal
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    • v.10 no.5
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    • pp.553-560
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    • 1995
  • A lactic aci bacteria producing antibacterial substance was isolated from pig feces. This strain was identified as a genus Lactobacillus, through its morphological, cultural and physiological characteristics. Lactobacillus sp. KJ-5 isolated showed the strong inhibitory effect on the growth of Salmonella paratyphi. The production of antibacterial substance was growth associated form during the batch culture of Lactobacillus sp. KJ-5 and the maximum production was obtained at the culture temperature of $37^{\circ}C$ as well as optimum temperature of cell growth. The antibacterial activity of the filtrate of culture broth was decreased by adjusting the pH 6.2 and was not affected by catalase treatment. The antibacterial substance was partially purified by methanol and acetone extraction, whtch exhibited three spots in the thin-layer chromatography and one of them showed an antibacterial activity, This substance also showed the maximum absorption of UV at 270nm and an antibacterial activity was completely inactivated by the treatment of proteolytic enzymes.

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Characterization of the Bacteriocin from Enterococcus faecium CJNU 2008 (Enterococcus faecium CJNU 2008 균주 생산 박테리오신의 특성 규명)

  • Seo, Souk-Jin;Yang, Jung-Mo;Moon, Gi-Seong
    • Journal of Food Hygiene and Safety
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    • v.33 no.6
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    • pp.516-520
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    • 2018
  • Bacteriocin is a proteinaceous compound produced by microorganisms showing antimicrobial activities. In this study, the physicochemical properties of the bacteriocin produced by Enterococcus faecium CJNU 2008 strain were characterized. Partially purified bacteriocin showed stabilities against heat treatments at $100^{\circ}C$ for 30 min and $121^{\circ}C$ for 15 min and against solvents treatments such as methanol, ethanol, acetone, acetonitrile and chloroform. The bacteriocin also exhibited stabilities against lipase and ${\alpha}-amylase$ treatments but the stability was abolished at protease treatment, indicating that the antimicrobial agent from E. faecium CJNU 2008 was a proteinaceous bacteriocin. The bacteriocin also showed bactericidal mode of action against Listeria monocytogenes. The molecular mass of the bacteriocin was estimated to be under 6.5 kDa by a tricine-SDS-PAGE analysis. The bacteriocin was purified by HPLC. Further studies toward biochemical analysis of the bacteriocin are needed in near future.

Chemical Properties of Fucoidans from Hizikia fusiformis and Sargassum fulvellum (톳과 모자반 fucoidan의 화학적 특성)

  • KOO Jae-Geun;JO Kil_Suk;DO Jeong-Ryong;PARK Jin-Hee;YANG Cha-Bum
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.28 no.5
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    • pp.659-666
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    • 1995
  • Fucoidans were isolated from Hizikia fusiformis and Sargassum fulvellum and characterized on their chemical properties. Crude fucoidans were extracted at $65^{\circ}C$ for 1hr with acid solution of pH 2.0, and cetylpyridinum chloride was used for partial purification. The yields of partially purified fucoidans were $2.51\%$ for H. fusiformis, and $65\%$ for S. fulvellum, respectively. The partially purified fucoidans were separated into 3 fractions by DEAE-Sephadex A-25 ion exchange column chromatography and the major fractions were refractionated with fractional preripitation with ethanol. $60-70\%$ ethanol precipitated fraction(P-70) of H. fusiformis and $60-65\%$ ethanol precipitated fraction(P-65) of S. fulvellum turned out to be homogeneous by cellulose acetate electrophoresis and gel filtration chromatography. The molar ratios of fucose, galactose, and sulfate In the purified fucoidans were 1 : 0.66 2.74 for H. fusiformis and 1 : 0.24. 1.46 for 5. fulvellum. The averaged molecular weights of the purified fucoidans from H. fusiformis and S. fulvellum were 26,000 and 105,000, respectively.

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