• Title/Summary/Keyword: acid/base two-step catalyzed

Search Result 6, Processing Time 0.025 seconds

Microwave Assisted Energy Efficient Biodiesel Production from Crude Pongamia pinnata (L.) Oil Using Homogeneous Catalyst

  • Kumar, Ritesh;Sethy, A.K.
    • Journal of Forest and Environmental Science
    • /
    • v.31 no.1
    • /
    • pp.1-6
    • /
    • 2015
  • Microwave assisted biodiesel production from crude Pongamia pinnata oil using homogeneous base catalyst (KOH) was unsuccessful because of considerable soap formation. Therefore, a two step process of biodiesel production from high free fatty acid (FFA) oil was investigated. In first step, crude P. pinnata oil was acid catalyzed using $H_2SO_4$ and acid value of oil was reduced to less than 4 mg KOH/g. Effect of sulfuric acid concentration, alcohol-oil molar ratio and microwave irradiation time on acid value of oil was studied. Result suggested that 1.5% $H_2SO_4$ (w/w), 6:1 methanol oil molar ratio and 3 min microwave irradiation time was sufficient to reduce the acid value of oil from 12 and 22 mg KOH/g to 2.9 and 3.9 mg/KOH/g, respectively. Oil obtained after pretreatment was subsequently used for microwave assisted alkali catalyzed transesterification. A higher biodiesel yield (99.0%) was achieved by adopting two step processes. Microwave energy efficiency during alkali catalyzed transesterification was also investigated. The results suggested a significant energy saving because of reduced reaction time under microwave heating.

Improvement of Performance of Anti-reflective Coating Film Using Methyltrimethoxysilane (Methyltrimethoxysilane을 이용한 반사방지 코팅막의 성능 향상)

  • Keum, Young-Sub;Kim, Hyo-Sub;Park, Chu-Sik;Kim, Young-Ho
    • Applied Chemistry for Engineering
    • /
    • v.26 no.4
    • /
    • pp.400-405
    • /
    • 2015
  • Traditional anti-reflective (AR) coating films prepared using tetraethylorthosilicate (TEOS) as a precursor absorbs water easily in addition to having a weak abrasion resistance. To improve the transmittance, hydrophobicity and abrasion resistance of AR coating film, various AR coating films were prepared using methyltrimethoxysilane (MTMS) as a precursor in addition to introducing a fluoroalkylsilane, acid catalyst, base catalyst and acid-base two step catalyst. The prepared AR coating films were then characterized by UV-Vis spectroscopy, contact angle analyzer, atomic force microscope (AFM), pencil scratch hardness test and cross-cut test. As a result, the transmittance of bare glass was 90.5%, while that of AR coating glass increased to 94.8% at curing temperature of $300^{\circ}C$. When the fluoroalkylsilane was added, the water contact angle of AR coating film increased from $96.3^{\circ}$ to $108^{\circ}$, indicating that the hydrophobicity of the film was greatly improved. The abrasion resistance of AR coating film was also improved by the acid catalyst, whereas the transmittance increased by the base catalyst. In the case of AR coating film prepared using an acid-base two step catalyzed reaction, both the transmittance and abrasion resistance of the film was synergistically enhanced as compared with those of AR coating films prepared without introduction of a catalyst.

Mechanism of the Electrode Reduction of Cupferron in Neutral and Alkaline Media (중성 및 알카리성수용액에서 Cupferron 의 전극환원메카니즘)

  • Hwang, Kum-Sho;Hwang, Jung-Ui
    • Journal of the Korean Society of Fisheries and Ocean Technology
    • /
    • v.11 no.1
    • /
    • pp.32-55
    • /
    • 1975
  • The ammonium salt of N-Nitrosophenylhydroxiamine, namely Cupferron, is a well-known analytical reagent which precipitates a great number of metal ions in acid medium. Various structures of electrode reduction for N-Nitrosophenylhydroxiamine have been suggested in acid and alkaline media by many researchers, but not in neutral medium. So the mechanism of electrode reaction of Cupferron was investigated by both chronopotentiometric and polarographic methods. It was estimated that the reduction of Cupferron occurs in a three-step mechanism through which a chemical step is interposed between two charge transfer, the ECE (charge transfer-chemical reaction-charge transfer) mechanism, over a range of neutral and alkaline media. The chemical reaction of the process was assumed to be acid-base catalyzed from the fact that kapp (over all rate constant) of chemical reaction is pH dependent.

  • PDF

Identification of Amino Acid Residues Involved in Feedback Inhibition of the Anthranilate Synthase in Escherichia coli

  • Kwak, Joon-Hyeok;Hong, Kwang-Won;Lee, Sung-Haeng;Hong, Jin-Han;Lee, Se-Yong
    • BMB Reports
    • /
    • v.32 no.1
    • /
    • pp.20-24
    • /
    • 1999
  • The first step of the branch pathway in tryptophan biosynthesis is catalyzed by anthranilate synthase, which is subjected to feedback inhibition by the end product of the pathway. The $trpE^{FBR}$ gene from a mutant Escherichia coli strain coding for anthranilate synthase that was insensitive to feedback inhibition by tryptophan has been cloned. To identify the amino acid changes involved in the feedback regulation of anthranilate synthase, the nucleotide sequence of the mutant $trpE^{FBR}$ gene was determined. Sequence analysis of the $trpE^{FBR}$ gene revealed that four bases were changed in the structural gene while alteration was not found in the 5' control region. Among these base changes, only two base substitutions caused the alterations in amino acid sequences. From the results of restriction fragment exchange mapping, the 61st nucleotide, C to A substitution, that changed $Pro^{21}{\rightarrow}Ser$ was identified as the cause of the desensitization to feedback inhibition by tryptophan. Additional feedback-resistant enzymes of the E. coli anthranilate synthases were constructed by site-directed mutagenesis to examine the effect of the $Ser^{40}\;{\rightarrow}\;Arg^{40}$ change found in the $trpE^{FBR}$ gene of Brevibacterium lactofermentum. From the feedback inhibition analysis, the $Pro^{21}{\rightarrow}Ser$ and $Ser^{40}{\rightarrow}Arg$ mutants maintained about 50% and 90% of their maximal activities, respectively, even at the extreme concentration of 10 mM tryptophan. From these results, we suggest that the $Pro^{21}$ and $Ser^{40}$ residues are involved in the tryptophan binding in the E. coli enzyme.

  • PDF

Theoretical Evaluation of the Electrophilic Catalyses in Successive Enolization and Reketonization Reactions by Δ5-3-Ketosteroid Isomerase

  • Park, Hwang-Seo;Seh, Jung-Hun;Lee, Sang-Youb
    • Bulletin of the Korean Chemical Society
    • /
    • v.23 no.6
    • /
    • pp.837-845
    • /
    • 2002
  • Based on ab initio calculations at the MP2(FULL)/6-31+G**//RHF/6-31G** level, we compare the energetic and mechanistic features of a model reaction for catalytic action of Δ?-3-ketosteroid isomerase (KSL,E.C.5.3,3.1) with those of a corresponding nonenzymatic reaction in aqueous solution. The results show that the two catalytic acid residues,Tyr14 and Asp99, can lower the free energy of activation by 8.6kcal/mol, which is in good agreement with the experimentally predicted~9 kcal/mol,contribution of electrophilic catalyses to the whole enzymatic rate enhancement. The dienolate intermediate formed by proton transfer from the substrate carbon acid to the catalytic base residue (Asp38) ins predicted to be stabilized by 12.0 kcal/mol in the enzymatic reaction, making its formation thermodynamically favorable. It has been argued that enzymes catalyzing the reactions of carbon acids should resolve the thermodynamic problem of stabilizing the enolate intermediate as well as the kinetic porblem of lowering the free energy of activation for porton abstraction. We find that KSI can successfully overcome the thermodynamic difficulty ingerent in the nonenzymatic reaction through the electrophilic catalyses of the two acid residues. Owing to the stabilization of dienolate intermediate, the reketonization step could influence the overall reaction rate more significantly in the KSI- catalyzed reaction than in the nonenzymatic reaction, further supporting the previous experimental findings. However, the electrophilic catalyses alone cannot account for the whole catalygic capability (12-13 kcal/mol), confiming the earlier experimental implications for the invement of additional catalytic components. The present computational study indicates clearly how catalytic residues of KSI resolve the fundamental problems associated with the entropic penalty for forming the rate-limiting transition state and its destabilization in the bulk solvation environment.

Immobilization of Burkholderia cepacia Lipase on Weak Base Styrene Resin Using Polyethyleneimine with Cross-linking (PEI(Polyethyleneimine)를 이용하여 음이온계 레진에 고정화된 Lipase AH 제조 및 효소적 Interesterification을 통한 반응 특성 연구)

  • Lee, Chi Woo;Lee, Ki Teak
    • Journal of the Korean Society of Food Science and Nutrition
    • /
    • v.43 no.7
    • /
    • pp.1025-1035
    • /
    • 2014
  • This study assessed the effect of immobilized lipase on weak base styrene resin using polyethyleneimine (PEI) with cross-linking. Two procedures were used in this study. The first one, "mono-layer" lipase immobilization, involves washing PEI after adsorption. The second procedure, "multi-layer" lipase immobilization, has no washing before the cross-linking step. Treverlite XS-100200 (weak base styrene resin) was immersed with PEI solution (2.2 mg/mL). Lipase AH (from Burkholderia cepacia) was adsorbed onto the support coated with PEI before cross-linking with glutaraldehyde. Structured lipid was synthesized by immobilized lipase-catalyzed interesterification using canola oil, palmitic ethyl ester (PEE), and stearic ethyl ester (StEE). Total fatty acid contents of triacylglycerol (TAG) in structured lipids were analyzed to investigate activity, properties, and reusability of immobilized lipases. Activities of immobilized lipases on the multi-layer and mono-layer increased at a high concentration (8 mg/mL) of lipase solution used for immobilization. The results show that immobilized lipase with the mono-layer method at pH 8.0 on resin had the highest total saturated fatty acid content (26.17 area%). Activity of immobilized lipase with the multi-layer method at pH 7.5 on support was lower than that of the mono-layer, but total saturated fatty acid content was 16.79 area% higher than that of lipase AH (15.01 area%).