• 제목/요약/키워드: C-H amination

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有機 Halides 와 Amines 間의 光反應에 關한 硏究 (A Study on the Photoreaction between Organic Halides and Amines)

  • 김유선;박용자
    • 대한화학회지
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    • 제6권2호
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    • pp.148-154
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    • 1962
  • The reactions between organic halides$(CCl_4,\;C_6H_5Br,\;C_6H_5Cl,\;C_6H_5I)$ and amines $(C_6H_5NH_2,\;R_2NH,\;R_3N,\;(CH_2)_5NH,\;pyridine)$ were studied under mixed u.v. irradiation. The modes of reactions were examined by means of gas chromatography and product-reactant ratio determination. The reaction of $CCl_4$ with amines give chloroform and hexachloroethanes, and the reaction of aromatic halides with amines gave biphenyl and benzene. In each series of reaction there obtained mainly corresponding amine hydrohalides, but no amination products. The reactivity was in the order of the basicity of amines and of the reactivity of organic hahides, except in the case of cyclic tertiary amine. The result was interpreted as a non-chain photodecomposition process. A competitive proton abstraction reaction path via the formation of a change transfer complex was proposed as the reaction mechanism.

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The Kinetic Parameters of Hafnia alvei Aspartase from pH Studies

  • Kim, Sung-Kun;Choi, Jung-Hoon;Yoon, Moon-Young
    • BMB Reports
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    • 제28권3호
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    • pp.204-209
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    • 1995
  • The pH dependence of kinetic parameters in the amination direction of the aspartase from Hafnia alvei has been determined. The V/K for fumarate is bell shaped with pK values of 6.4 and 8.7. The maximum velocity for fumarate is also bell shaped with pK values of 7.2 and 9.1. The pH dependence of 1/K, for potassium (competitive inhibitor of ammonia) decreases at low pH with pK 7.6. Together with data [Yoon and Cook (1994) Korean J. Biochem. 27, 1-5] on the deamination direction of the aspartase, these results are consistent with two enzyme groups which are necessary for catalysis. An enzymatic group that must be deprotonated has been identified. Another enzyme group must be protonated for substrate binding. Both the general base and general acid group are in a protonation state opposite that in which they started when aspartate was bound. A proton is abstracted from C-3 of the monoanionic form of L-aspartate by an enzyme general base with, a pK of 6.3~6.6 in the absence and presence of $Mg^{2+}$ Ammonia is then expelled with the assistance of a general acid group giving $NH_{4+}$ as the product.

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Optimized Conditions for In Situ Immobilization of Lipase in Aldehyde-silica Packed Columns

  • Seo Woo Yong;Lee Kisay
    • Biotechnology and Bioprocess Engineering:BBE
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    • 제9권6호
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    • pp.465-470
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    • 2004
  • Optimal conditions for the in situ immobilization of lipase in aldehyde-silica packed columns, via reductive amination, were investigated. A reactant mixture, containing lipase and sodium borohydride (NaCBH), was recirculated through an aldehyde-silica packed column, such that the covalent bonding of the lipase, via amination between the amine group of the enzyme and the aldehyde terminal of the silica, and the reduction of the resulting imine group by NaCBH, could occur inside the bed, in situ. Mobile phase conditions in the ranges of pH $7.0{\~}7.8$, temperatures between $22{\~}28^{circ}C$ and flow rates from $0.8{\~}1.5\;BV/min$ were found to be optimal for the in situ immobilization, which routinely resulted in an immobilization of more than 70 mg­lipase/g-silica. Also, the optimal ratio and concentration for feed reactants in the in situ immobilization: mass ratio [NaCBH]/[lipase] of 0.3, at NaCBH and lipase concentrations of 0.75 and 2.5 g/L, respectively, were found to display the best immobilization characteristics for concentrations of up to 80 mg-lipase/g-silica, which was more than a 2-fold increase in immobilization compared to that obtained by batch immobilization. For tributyrin hydrolysis, the in situ immobilized lipase displayed lower activity per unit mass of enzyme than the batch-immobilized or free lipase, while allowing more than a $45\%$ increase in lipase activity per unit mass of silica compared to batch immobilization, because the quantity of the immobilization on silica was aug­mented by the in situ immobilization methodology used in this study.

초임계 암모니아를 이용한 p-Phenylenediamine(PPD) 합성 및 특성연구 (Synthesis of p-Phenylenediamine (PPD) using Supercritical Ammonia)

  • 조항규;임종성
    • Korean Chemical Engineering Research
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    • 제53권1호
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    • pp.53-56
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    • 2015
  • 초임계 암모니아 분위기와 CuI 촉매 하에서 p-Diiodobenzene(PDIB)를 아민화 반응시켜 p-Phenylenediamine(PPD)를 합성하는 방법을 연구하였다. 본 연구에서는 여러 가지 공정변수들이 PPD 생성 수율에 미치는 영향을 알아보기 위하여 반응 온도, 암모니아 초기 주입 양에 따른 반응 압력, 촉매의 유무 및 촉매 주입량, 반응 시간 등을 변화시키면서 이에 따른 PPD 수율 변화를 GC 분석을 통하여 조사하였다. 그 결과, 무촉매 반응 시에는 PPD가 전혀 생성되지 않음을 알 수 있었으며, 반응온도, 반응 압력, 촉매 주입량 및 반응시간이 증가함에 따라 PPD 생성 수율이 증가하는 것을 확인할 수 있었다 단, 반응온도의 경우 $250^{\circ}C$ 이상에서는 열분해에 의해 PPD가 감소하여 $200^{\circ}C$가 최적의 온도임을 알 수 있었다. 또한, FT-IR과 $^1H$-NMR 분석을 통하여 아민기의 결합 특성과 PPD의 구조를 확인하였다.

알지네이트계 고분자 계면활성제의 합성 (Synthesis of Alginate-derived Polymeric Surfactants)

  • 강현아
    • KSBB Journal
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    • 제15권4호
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    • pp.375-379
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    • 2000
  • 자연물 유래의 생고분자 (biopolymer) 인 알지네이트를 이용하여 천연물 소재의 고분자 계면활성제를 합성하고자 하였 으며, 이를 위해 얄지네이트를 화학반응을 통해 변형시켰다. 합성된 알지네이트계 고분자 계면활성제 (APSs)의 특성을 파 악하기 위해 표면장력, 유기불 용해 실험 (azobenzene) , 및 회 분식 방법에 의한 중급속(Pb, Co) 제거 실험을 수행하였다 그 결과, APSs는 순수한 알지네이트에는 없었던 표면활성능 력을 가지고 있었으며, 또한 Pb, Co 제거율이 순수한 알지네 이트와 상응하는 높은 값을 나타냈다. 유기물 제거 실험 결 과는 일반적인 경향을 보이지는 않았는데 이는 고분자 골격 이 존재함으로 인해 미셀 형성에 영향을 미치는 것으로 보인다. 40%산화된 얄지네이트에 C8 (octyl amine)을 도입한 계 면활성제의 경우, 상용되고 있는 당류계 고분자 계면활성제 인 APG 와 유사한 제거능을 보였다 결과 APSs 에 의해 유 기불과 중금속이 제거되었으며 이것으로 볼 때 순수한 알지 네이트에 소수성기를 도입해 줌으로서 새로운 기능이 부여된 세정제로서의 APSs가 합성되었음을 알 수 있었다.

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Purification and Biochemical Characterization of Recombinant Alanine Dehydrogenase fvom Thermus caldophilux GK24

  • Bae, Jung-Don;Cho, Youn-Jeung;Kim, Doo-Il;Lee, Dae-Sil;Shin, Hyun-Jae
    • Journal of Microbiology and Biotechnology
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    • 제13권4호
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    • pp.628-631
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    • 2003
  • The recombinant alanine dehydrogenase (ADH) from E. coli containing Thermus caldophilus ADH was purified to homogeneity from a cell-free extract. The enzyme was purified 38-fold with a yield of 68% from the starting cell-free extract. The purified enzyme gave a single band in polyacrylamide gel electrophoresis, and its molecular weight was estimated to be 45 kDa. The pH optimum was 8.0 for reductive amination of pyruvate and 12.0 for oxidative deamination of L-alanine. The enzyme was stable up to $70^{\circ}C$. The activity of the enzyme was inhibited by 1 mM $Zn^{2+}$, 20% hexane, and 20% $CHCl_3$. However, 10 mM $Mg^{2+}$ and 40% propanol had no effect on the enzyme activity. The Michaelis constants ($K_m$) for the substrates were $50\;\mu\textrm{M}$ for NADH, 0.2 mM for pyruvate, 39.4 mM for $NH_4+$, 2.6 mM for L-alanine, and 1.8 mM for $NAD^+$.

E-beam 전조사에 의한 $NO_{3} ^{-}$ 선택 흡착용 아민화 PP-g-GMA 섬유 이온교환체의 합성과 그 특성에 관한 연구 (Studies on the Synthesis of Aminated PP-g-GMA Fibrous ion Exchanger by E-beam Pre-irradiation and Their Properties of Selective Adsorption for $NO_{3} ^{-}$)

  • 황택성;이선아;이면주
    • 폴리머
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    • 제26권2호
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    • pp.153-159
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    • 2002
  • 본 연구에서는 지하수 중의 NO$_{3}^{-}$ 이온을 선택적으로 흡착 제거시키기 위하여 E-beam 전조사법에 의해 GMA 단량체를 폴리프로필렌 섬유 기재에 그라프트 반응시켜 PP-g-GMA 공중합체를 제조한 후 아민화 반응을 통하여 강염기성 APP-g-GMA 음이온교환수지를 합성하였다. 공중합체의 그라프트율 및 TMA에 의한 아민화율은 반응온도가 증가할수록 증가하였으며, $60^{\circ}C$일 때 각각 133%, 88% 최대치를 나타내었고, 이때의 팽윤율과 이온교환용량은 각각 86%, 2.5 meq/g으로 IMAC HP555, Amberlite IRA 400와 같은 상용 이온교환수지 보다 높게 나타났다. $NO_3;^-$ 이온흡착의 최적 조건은 pH 5~6이었으며, trimethylammonium 기를 갖는 -Cl형의 APP-g-GMA 이온교환체가 가장 높은 선택 흡착성을 나타냈다.