• 제목/요약/키워드: alcohol oxidation

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황이 포함된 중형기공성 탄소에 화학적으로 고정화된 H5PMo10V2O40 촉매 상에서 Benzyl Alcohol 산화반응 (Benzyl Alcohol Oxidation over H5PMo10V2O40 Catalyst Chemically Immobilized on Sulfur-containing Mesoporous Carbon)

  • 김민영;강태훈;최정호;송인규
    • Korean Chemical Engineering Research
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    • 제54권3호
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    • pp.419-424
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    • 2016
  • 황이 포함된 중형기공성 탄소 담체(S-MC)에 화학적으로 고정화된 $H_5PMo_{10}V_2O_{40}$ ($PMo_{10}V_2$) 촉매를 제조하고, 이를 Benzyl alcohol 산화반응에 적용해보았다. 먼저 주형물질로 SBA-15, 탄소 전구체로 p-Toluenesulfonic acid를 이용하여 S-MC 지지체를 제조하였다. 이후, $PMo_{10}V_2$ 촉매가 화학적으로 고정화될 수 있는 위치를 제공하기 위해 S-MC 지지체의 표면이 양전하를 띠도록 개질시켰다. 전체적으로 음전하를 띠는 $[PMo_{10}V_2O4_{40}]^{5-}$를 이용함으로써 $PMo_{10}V_2$를 양이온을 띠는 S-MC 표면에 화학적으로 고정화하였다. 화학적 고정화를 통해 $PMo_{10}V_2$가 분자수준으로 균일하게 분산되었음을 확인하였다. Benzyl alcohol의 기상 산화반응에서 $PMo_{10}V_2$/S-MC 촉매는 무담지 상태의 $PMo_{10}V_2$보다 높은 전화율 및 수율을 나타냈다. $PMo_{10}V_2$/S-MC 촉매의 반응 활성이 향상된 이유는 화학적 고정화를 통해 $PMo_{10}V_2$이 S-MC 지지체에 고르게 분산되었기 때문이다.

호기성 벤질 알코올 산화반응을 위한 팔라듐 이산화티타늄 촉매 개발 (Synthesis of Pd/TiO2 Catalyst for Aerobic Benzyl Alcohol Oxidation)

  • 조태준;유계상
    • 공업화학
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    • 제25권3호
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    • pp.281-285
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    • 2014
  • 호기성 벤질 알코올 산화반응용 촉매로 팔라듐이 담지된 이산화티타늄 입자를 제조하였다. 우선 합성한 이산화티타늄입자에 10 wt% 팔라듐을 함침한 후, 다양한 온도에서 소성하여 촉매를 제조하였다. 촉매의 비표면적은 소성온도에 따라 변하였는데, $300^{\circ}C$에서 소성한 촉매의 비표면적이 가장 높게 측정되었다. 제조된 촉매의 반응 결과 $300^{\circ}C$에서 소성한 입자가 가장 우수한 반응성능을 보였다. 또한 팔라듐의 농도를 5 wt%에서 15 wt%까지 조절하여 함침한 후 $300^{\circ}C$에서 소성하여 촉매를 합성하였다. 팔라듐의 농도가 10 wt%인 $Pd/TiO_2$ 입자가 벤질알코올 산화반응에 최적의 촉매로 규명되었다. 이는 상대적으로 높은 촉매의 비표면적 및 팔라듐 분산도에 기인한다.

저온연소조건에서 n-heptane/alcohol 혼합연료의 냉염과 열염에 대한 착화지연 관찰 (Observation on the Ignition Delay Time of Cool and Thermal Flame of n-heptane/alcohol Blended Fuel at Low Temperature Combustion Regime)

  • 송재혁;강기중;류승협;최경민;김덕줄
    • 한국연소학회지
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    • 제18권4호
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    • pp.12-20
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    • 2013
  • The ignition delay time is an important factor to understand the combustion characteristics of internal combustion engine. In this study, ignition delay times of cool and thermal flame were observed separately in homogeneous charge compression ignition(HCCI) engine. This study presents numerical investigation of ignition delay time of n-heptane and alcohol(ethanol and n-butanol) binary fuel. The $O_2$ concentration in the mixture was set 9-10% to simulate high exhaust gas recirculation(EGR) rate condition. The numerical study on the ignition delay time was performed using CHEMKIN codes with various blending ratios and EGR rates. The results revealed that the ignition delay time increased with increasing the alcohol fraction in the mixture due to a decrease of oxidation of n-heptane at the low temperature. From the numerical analysis, ethanol needed more radical and higher temperature than n-butanol for oxidation. In addition, thermal ignition delay time is sharply increasing with decreasing $O_2$ fraction, but cool flame ignition delay time changes negligibly for both binary fuels. Also, in high temperature regime, the ignition delay time showed similar tendency with both blends regardless of blending ratio and EGR rate.

[Hmim][PF6]를 사용한 벤질 알코올의 호기성 산화반응용 팔라듐-은 차콜 촉매 제조 (Synthesis of Pd-Ag on Charcoal Catalyst for Aerobic Benzyl Alcohol Oxidation Using [Hmim][PF6])

  • 추연준;유계상
    • 공업화학
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    • 제25권4호
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    • pp.425-429
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    • 2014
  • 호기성 벤질 알코올 산화반응용 상용촉매 개발을 위하여 팔라듐이 담지된 차콜 입자를 제조하였다. 특히 촉매의 팔라듐 분산도를 높이기 위해서 상온 이온성액체 중 하나인 [Hmim][$PF_6$]을 기능성 용매로 사용하여 입자를 합성하였다. 다양한 농도의 팔라듐을 함침하여 제조된 입자의 반응성을 측정한 결과 7.5 wt%의 촉매가 가장 우수한 반응 활성과 안정성을 나타내었다. 또한 조촉매로서 다양한 농도의 은입자를 합침하여 촉매를 제조하였다. 동일한 반응조건에서 팔라듐과 은의 질량 비율이 9 : 1인 촉매가 높은 금속 분산도로 인하여 가장 반응성이 우수하였다.

Purification and Characterization of a Cyclohexanol Dehydrogenase from Rhodococcus sp. TK6

  • Kim, Tae-Kang;Choi, Jun-Ho;Rhee, In-Koo
    • Journal of Microbiology and Biotechnology
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    • 제12권1호
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    • pp.39-45
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    • 2002
  • Activity staining on the native polyacrylamide gel electrophoresis (PAGE) of a cell-free extract of Rhodococcus sp. TK6, grown in media containing alcohols as the carbon source, revealed at least seven isozyme bands, which were identified as alcohol dehydrogenases that oxidize cyclohexanol to cyclohexanone. Among the alcohol dehydrogenases, cyclohexanol dehydrogenase II (CDH II), which is the major enzyme involved in the oxidation of cyclohexanol, was purified to homogeneity. The molecular mass of the CDH II was determined to be 60 kDa by gel filtration, while the molecular mass of each subunit was estimated to be 28 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The CDH II was unstable in acidic and basic pHs, and rapidly inactivated at temperatures above $40^{\circ}C$ . The CDH II activity was enhanced by the addition of divalent metal ions, like $Ba^2+\;and\;Mg^{2+}$. The purified enzyme catalyzed the oxidation of a broad range of alcohols, including cyclohexanol, trans-cyclohexane-1,2-diol, trans-cyclopentane-l,2-diol, cyclopentanol, and hexane-1,2-diol. The $K_m$ values of the CDH II for cyclohexanol, trans-cyclohexane-l,2-diol, cyclopentanol, trans-cyclopentane-l,2-diol, and hexane-l,2-diol were 1.7, 2.8, 14.2, 13.7, and 13.5 mM, respectively. The CDH II would appear to be a major alcohol dehydrogenase for the oxidation of cyclohexanol. The N-terminal sequence of the CDH II was determined to be TVAHVTGAARGIGRA. Furthermore, based on a comparison of the determined sequence with other short chain alcohol dehydrogenases, the purified CDH II was suggested to be a new enzyme.

여러 가지 형태에 따른 Alcohol-Oxidase의 특성 비교 (Comparison of the Characteristics of Alcohol-Oxidase by the Various Forms)

  • 이명숙
    • 한국식품영양과학회지
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    • 제22권6호
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    • pp.797-802
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    • 1993
  • The properties of the alcohol-oxidase from yeasts assimilating of methanol(Hansenula polymorpha CBS 4732, Pichia pastoris CBS 2612 and Candida boidinii CBS 8106) as free(cellules, purified enzymes) and immobilized forms(immobilized cellules, immobilized enzymes) were investigated. Immobilization enhanced the activity and stability of alcohol-oxidase to a certain degree. The optimum temperature of the immobilized alcohol-oxidase was lower than those of the free forms. The pH / activi쇼 profiles of alcohol-oxidase did not change by immobilization, but changed by the microorganisms. When the immobilized cellules were stocked at 4$^{\circ}C$ in 10mM potassium phosphate buffer(pH 7.5 or 8.0), alcohol-oxidase was more stable than those were stocked in potassium phosphate buffer containing 0.65M sucrose. The immobilization modifies the conditions of oxidation on the various substrates. alcohol-oxidase in immobilized forms showed some with higher Km value for methanol than that in free ones.

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