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Kinetic analysis of batch ethanol acetylation in isothermal non-stationary multiphase systems by lyophilized mycelium of Aspergillus oryzae BJM
Palazzi,Emilio; Molinari,Francesco; Fabiano,Bruno; Pessoa Jr,Adalberto; Converti,Attilio.
A relatively complex network of reactions has been investigated, using as a network model the isothermal batch esterification of acetic acid with ethanol in n-heptane catalyzed by lyophilized mycelium of Aspergillus oryzae. The kinetic analysis was firstly carried out on the whole system, without any simplification, by means of the well-known integral method. Owing to the poor results obtained by this way, we developed an alternative approach, combining initial rates and integral analysis and reducing the number of empirical parameters to be determined by the use of equilibrium data. All the values of the parameters calculated according to this "composite" approach to kinetic analysis well correlate with experimental data.
Tipo: Info:eu-repo/semantics/article Palavras-chave: Aspergillus oryzae; Complex network; Enzyme reactions; Esterification; Organic solvent.
Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822011000100048
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Cloning and characterization of newly isolated lipase from Enterobacter sp. Bn12 BJM
Farrokh,Parisa; Yakhchali,Bagher; Asghar Karkhane,Ali.
A mesophilic Enterobacter sp. Bn12 producing an alkaline thermostable lipase was isolated from soil in Tehran, Iran. The lipase gene (ELBn12) was identified from a genomic library. Sequence analysis of the DNA fragment revealed an open reading frame of 879 bp encoding a lipase with a molecular mass of 31.3 kDa. The deduced amino acid sequence showed 96% identity with a lipase of Enterobacter sp. Ag1 and the identity of their DNA sequences was 88.9%. ELBn12 belongs to the lipase subfamily I.1 and its catalytic triad consists of Ser82, Asp237 and His259. The lipase was expressed in Escherichia coli (BL21) pLysS and partially purified by anion exchange chromatography. The maximum activity of ELBn12 was obtained at temperature of 60 °C and pH 8.0 towards...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Enterobacter; Thermostable lipase; Alkaline; Organic solvent.
Ano: 2014 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822014000200042
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The role of organic solvent amount in the lipase-catalyzed biodiesel production Ciênc. Tecnol. Aliment.
Dalla Rosa,Clarissa; Oliveira,Débora de; Oliveira,José Vladimir.
This research note addresses the role of organic solvent amount in the production of fatty acid ethyl esters from soybean oil. N-hexane was chosen as solvent and two commercial immobilized lipases as catalysts, Novozym 435 and Lipozyme IM. The reactions were conducted in 6 hours, varying the solvent to oil ratio from zero to 50 (v/wt) and adopting adopting for Novozym 435: 65 ºC, enzyme concentration (E, wt%) = 5, oil to ethanol molar ratio (R) = 1:10, water addition (H, wt%) = 0, and for Lipozyme IM: 35 ºC, E = 5 wt%, R = 1:3, H = 10 wt%. For Lipozyme IM, an increase in solvent amount is shown to lead to an enhancement of reaction conversion, while a negligible effect was found for Novozym 435. When using 30 mL of solvent the reaction conversions were 88%...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Biodiesel; Lipases; Organic solvent; Soybean oil.
Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612010000100011
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