• 제목/요약/키워드: Natural purification

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Purification and Some Properties of an Extracellular Pectinase from Bacillus sp. BS-214

  • Jeon, Beong-Sam;Song, Jae-Young;Lee, Gang-Deog;Kim, Beom-Kyu;Cha, Jae-Young;Lee, Young-Choon
    • Journal of Life Science
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    • 제10권1호
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    • pp.1-5
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    • 2000
  • Pectinase was isolated from culture medium of Bacillus sp. BS-214 and purified 105-fold with 3.4% yield by ammonium sulfate precipitation, gel filteration using Sephadex G-75 and DEAE-cellulose followed by gel filteration through Sephadex G-100. The molecular weight of the purified enzyme was estimated to be about 43 kDa on SDS-PAGE and by gel filtration, indicating that the enzyme is a monomer. the optium pH and temperature of the enzyme were 9.0 and 55$^{\circ}C$, respectively. the enzyme was stable at 60$^{\circ}C$ for 30min and in a pH range from 7.5 to 10.5 for 12 h ant 4$^{\circ}C$. The enzyme activity was highly enhanced by Ca2+, and also K+, Li+ and Na+showed a positive effect, while stongly inhibited by Zn2+ and Hg2+.

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파지 K11 라이자소임의 amidase 활성도 (Amidase activity of phage K11 lysozyme)

  • 이상수
    • 자연과학논문집
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    • 제17권1호
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    • pp.55-64
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    • 2006
  • 이 연구에서는 6개의 히스티딘이 첨부된 파지 K11 라이소자임의 제조 분리 및 특성을 알아보고자 하였다. 첨부된 히스티딘에 의한 이 효소의 활성도의 변화는 없었으며, 효소 활성의 최적 pH는 7.2-7.4 이었다. 여러 다른 종류의 양이온 존재하의 활성도를 측정한 결과 칼슘과 마그네슘 이온에 의해 효소 활성이 완전히 억제되었으나, 아연이나 나트륨 이온은 효소의 활성도를 이 이온들이 없을 때와 같은 정도로 유지하였다. 단지 100 mM 이상의 아연 이온 농도에서 K11 라이소자임 효소 활성도를 완전히 억제하였다.

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수변구역 산림에 의한 수질정화기능 증진에 관한 고찰 (Investigation on the Enhancement of Water Purification Functions in Forest Watershed)

  • 박재현
    • 한국환경복원기술학회지
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    • 제4권4호
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    • pp.72-81
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    • 2001
  • This study is aimed to review the previous research accomplishments with analysis of problems and to suggest the counter plan for the watershed management and the ongoing research strategy. Phytoremediation provides a cost-effective techniques having a merit of low investment and maintenance cost. It could be one of the best techniques, which is an alternative plan to overcome economical situation and lack of experts in our country. In forest watershed affected by waste water and heavy metal pollutants should be controlled by vegetative remediation system, but the disposal techniques of harvested plant materials should be developed. Also, high degree areas of natural vegetation as a key model to recover the vegetation should be well conserved. It is important to restore forest continuity between upper stream and lower stream basin with the restoration of damaged in forest watershed. It is established to integrated protection system for land use and management plan and to natural environment evaluation methods affected by projects such as erosion control and developments in stream and forest. In addition, I suggest the continuous environmental monitoring system to treat the pollutions concerned.

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Streptomyces fradiae에서 분리된 Aspartate Aminotransferase의 특성 (Characterization of Aspartate Aminotransferase Purified from Streptomyces fradiae)

  • Lee, Sang-Hee;Lee, Kye-Joon
    • 미생물학회지
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    • 제31권3호
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    • pp.237-244
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    • 1993
  • Aspartate aminotransferase (ASAT) (L-aspartate : 2-oxyoglutarate, EC 2.6. 1. 1.) from Streptomyces fradiae NRRL 2702 has been purified by acetone precipitation, DEAE-cellulose, hydroxyapatite, and preparative electrophoresis (Prep cell), of which the last was the most effective step in the purification of ASAT. The molecular mass was estimated to be 54,000 dalton by SDS-PAGE and 120,000 dalton by gel filtration chromatography. Preparative isoelectric focusing of purified ASAT resulted in one polypeptide band with a pI of 4.2, showing homogeneity and indicating that the enzyme is composed of two identical subunits. The enzyme was specific for L-aspartate as an amino donor ; the $K_{m}$ values were determined to be 2.7 mM for L-aspartate, 0.7 mM for 2-oxoglutarate, 12.8 mM for L-glutamate, and 0.15 mM for oxaloacetate. The enzyme was relatively heat-stable, having maximum activity at 55.deg.C, and it had a broad pH optimum ranging from 5.5 to 8.0. The activity of the purified enzyme was not inhibited by ammonium ions. This paper reports the first purification and characterization of the aspartate aminotransferase from a species of Streptomyces.s.

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Purification and Characterization of Catalase-2 from Deinococcus radiophilus

  • Oh, Kyung-A;Lee, Young-Nam
    • BMB Reports
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    • 제31권2호
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    • pp.144-148
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    • 1998
  • A bifunctional catalase-peroxidase, designated catalase-2, of a UV resistant Deinococcus radiophilus was purified to electrophoretic homogeneity by both chromatographic and electrophoretic methods. Its molecular weight was 310 kDa and composed of a tetramer of 80 kDa subunits. The catalase-2 exerted its optimal activity at $30^{\circ}C$ and around pH 9. Its $K_m$ value for $H_{2}0_{2} $ was about 10 mM. It showed the typical ferric heme spectrum with maximum absorption at 403 nm which shifted to 419 nm in the presence of cyanide. The ratio of A40i' A2S0 was 0.48. Fifty percent inhibition of the enzyme activity was observed at $4.6{\times}10^{-6}$, $7.7{\times}10^{-6}$, and $3.0{\times}10^{-6}$ M of NaCN, $NaN_3$, and $NH_{2}OH$, respectively. The enzyme was thermostable and not sensitive to 3-amino-1,2,4-triazole. Treatment of the enzyme with ethanol-chloroform caused a partial loss (30%) of its activity. The catalase-2 was distinct from the Deinococcal bifunctional catalase-3 in a number of properties, particularly in its molecular structure and substrate affinity.

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농촌 소유역 축산폐수의 유역관리기법 개발 - 자연정화처리를 위한 완충대 적지분석 - (Watershed Scale Management Techniques of the Pollutants from Small Scale Livestock Ranches - Buffer Zone Selection for Natural Purification -)

  • 김성준;이남호;윤광식;홍성구;이윤아
    • 농촌계획
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    • 제6권2호
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    • pp.43-49
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    • 2000
  • Buffer zone selection technique for natural purification of livestock wastewater within a small agricultural watershed was developed using Geographic Information Systems. The technique was applied to $4.12\;km^2$ watershed located in Gosan-myun, Ansung-gun which have 20 livestock farmhouses. As a necessary data for selecting process, feedlot site map, digital Elevation Model (DEM), stream network, soil and land use map were prepared. By using these data, wastewater moving-path tracing program from each feedlot to the stream was developed to get the basic topographic factors; average slope through the paths, distance to the nearest stream and watershed outlet. To identify the vulnerable feedlots for storm event, the grid-based storm runoff model (Kim, 1998; Kim et al., 1998) was adopted. The result helps to narrow down the suitable area of buffer zone, and finally by using subjective but persuasive conditions related to elevation, slope and land use, the suitable buffer zones were selected.

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사람 탯줄로부터 추출된 Type I Collagen의 Telopeptide 제거에 대한 분석 (Analysis of Telopeptide Removal in Type I Collagen Purified From Human Umbilical Cords)

  • 서활;안수진;김요숙;이하규
    • 대한의용생체공학회:의공학회지
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    • 제17권3호
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    • pp.297-304
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    • 1996
  • Although collagen is still considered to be a poor immunogen, animals can produce antibodies to a number of different sites in the collagen molecule. In type I collagen, three classes of antigenic determinants have been described those are recogrlized as different degrees in different species. These are essentially composed of helical, conformation-dependent antigenic determinants and terminal, nonhelical antigenic determinants, and finally central antigenic determinants exposed only after denaturation of the collagen molecule. To utilize collagen as implantable biomateriall human e61bryonic collagen, ten immunological to body, was purified from human umbilical cords and found to contain [$\alpha$1(I)]$_2$. [$\alpha$2(I). Each step of purification were observed by polarized light microscope and analyzed through SDS-PAGE. The conclusious are follows; 1 . The purified collagen revealed gradual fiber indenties on each step of purification by polarized microscope. 2. The structual changes of extracted collagen as removed telopeptide were confirmed by SDS-PAGE.

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수산화라디칼과 오존에 의한 수중 천연 지방산 분해 제거 연구 (Purification of the Waste Water Containing Natural Fatty Oil by Hydroxy Radical and Ozone)

  • ;원정하;김용주;고장면;송근한;이창훈
    • Korean Chemical Engineering Research
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    • 제51권4호
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    • pp.523-526
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    • 2013
  • 본 연구에서는 수질정화 기술개발을 위하여 수산화라디칼 및 오존 발생기를 이용하여 수중에 존재하는 천연 지방산 분해 제거 연구를 수행하였다. 천연 지방산은 수산화라디칼 및 오존에 의하여 1차 분해반응 형태로 제거되었으며, 천연 지방산의 분해반응에서 수산화라디칼 단독으로 사용하는 것 보다 오존과 함께 사용한 경우 분해 효율을 크게 향상시킬 수 있음을 알 수 있었다. 또한, 천연 지방산이 수산화라디칼과 오존에 의해 분해되는 화학반응 기구를 제안하였다.

Purification and Characterization of a Catalase from Photosynthetic Bacterium Rhodospirillum rubrum S1 Grown under Anaerobic Conditions

  • Kang Yoon-Suk;Lee Dong-Heon;Yoon Byoung-Jun;Oh Duck-Chul
    • Journal of Microbiology
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    • 제44권2호
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    • pp.185-191
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    • 2006
  • The photosynthetic bacterium, Rhodospirillum rubrum S1, when grown under anaerobic conditions, generated three different types of catalases. In this study, we purified and characterized the highest molecular weight catalase from the three catalases. The total specific catalase activity of the crude cell extracts was 88 U/mg. After the completion of the final purification step, the specific activity of the purified catalase was 1,256 U/mg. The purified catalase evidenced an estimated molecular mass of 318 kDa, consisting of four identical subunits, each of 79 kDa. The purified enzyme exhibited an apparent Km value of 30.4 mM and a Vmax of 2,564 U against hydrogen peroxide. The enzyme also exhibited a broad optimal pH $(5.0{\sim}9.0)$, and remained stable over a broad temperature range $(20^{\circ}C{\sim}60^{\circ}C)$. It maintained 90% activity against organic solvents (ethanol/chloroform) known hydroperoxidase inhibitors, and exhibited no detectable peroxidase activity. The catalase activity of the purified enzyme was reduced to 19 % of full activity as the result of the administration of 10 mM 3-amino-1,2,4-triazole, a heme-containing catalase inhibitor. Sodium cyanide, sodium azide, and hydroxylamine, all of which are known heme protein inhibitors, inhibited catalase activity by 50 % at concentrations of $11.5{\mu}M,\;0.52{\mu}M,\;and\;0.11{\mu}M$, respectively. In accordance with these findings, the enzyme was identified as a type of monofunctional catalase.

Rhodotorula glutinis K-24에 의해 구성적으로 생산되는 세포외 Invertase의 정제 및 특성 (Purification and Characterization of the External Invertase Constitutively Produced by Rhodotorula glutinis K-24)

  • 최미정;김철;이상옥;이태호
    • 한국미생물·생명공학회지
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    • 제18권4호
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    • pp.368-375
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    • 1990
  • 세포내 및 세포벽 뿐만 아니라, 세포외에도 invertase를 구성적으로 생산하는 효모 Rh.glutinis K-24로 부터 세포외 invertase를 disc 전기 영동상으로 단일한 상태로까지 정제하였다. 정제 효소의 효소화학적 성질을 밝힌 후 이미 보고한 바 있는 세포내 및 세포벽 invertase와 그 개락적 성질을 비교 검토하였다.

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