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      Optimization of Ethanol Production Process from Cassava Starch by Surface Response

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          Abstract

          This work shows the study of the optimization process for producing ethanol from cassava starch based on 2² experimental designs with three central points and using statistical software. This methodology was applied to the stage of saccharification of cassava starch by acid hydrolysis as well as to the stage of fermentation using Socchoromyces cerevisioe. From the experimental data of acid hydrolysis, we proposed a first-order kinetic model which presented an average error of 1.87 % compared to the quadratic regression obtained. The development of a semicontinuous process showed a 89.84 % conversion of starch initially considered, yielding an ethanol concentration of 49.76 % Alc/vol.

          Translated abstract

          En este trabajo muestra el estudio del proceso optimización de obtención de etanol a partir del almidón de yuca, mediante el planteamiento de un diseño 2² con tres puntos centrales y usando un software estadístico para analizar los resultados. Esta metodología fue aplicada tanto para la etapa de sacarificación del almidón de yuca mediante hidrólisis ácida como para la etapa de fermentación empleando Socchoromyces cerevisioe. A partir de los datos experimentales de la hidrólisis ácida, se propone un modelo cinético de primer orden el cual presentó un error promedio del 1.87 % con respecto a la regresión cuadrática obtenida. El desarrollo de un proceso semi-contínuo mostró una conversión del 89.84 % del almidón inicialmente considerado, obteniéndose una concentración final de etanol del 49.76 % Alc/vol.

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          Most cited references38

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          Modulating enzyme activity using ionic liquids or surfactants.

          One of the important strategies for modulating enzyme activity is the use of additives to affect their microenvironment and subsequently make them suitable for use in different industrial processes. Ionic liquids (ILs) have been investigated extensively in recent years as such additives. They are a class of solvents with peculiar properties and a "green" reputation in comparison to classical organic solvents. ILs as co-solvents in aqueous systems have an effect on substrate solubility, enzyme structure and on enzyme-water interactions. These effects can lead to higher reaction yields, improved selectivity, and changes in substrate specificity, and thus there is great potential for IL incorporation in biocatalysis. The use of surfactants, which are usually denaturating agents, as additives in enzymatic reactions is less reviewed in recent years. However, interesting modulations in enzyme activity in their presence have been reported. In the case of surfactants there is a more pronounced effect on the enzyme structure, as can be observed in a number of crystal structures obtained in their presence. For each additive and enzymatic process, a specific optimization process is needed and there is no one-fits-all solution. Combining ILs and surfactants in either mixed micelles or water-in-IL microemulsions for use in enzymatic reaction systems is a promising direction which may further expand the range of enzyme applications in industrial processes. While many reviews exist on the use of ILs in biocatalysis, the present review centers on systems in which ILs or surfactants were able to modulate and improve the natural activity of enzymes in aqueous systems.
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            A microplate-based evaluation of complex denaturation pathways: structural stability of Escherichia coli transketolase.

            We have previously developed a rapid microplate-based approach for measuring the denaturation curves by intrinsic tryptophan fluorescence for simple monomeric and two-state unfolding proteins. Here we demonstrate that it can accurately resolve the multiple conformational transitions that occur during the denaturation of a complex multimeric and cofactor associated protein. We have also analyzed the effect of two active-site mutations, D381A and Y440A upon the denaturation pathway of transketolase using intrinsic fluorescence measurements, and we compare the results from classical and microplate-based instrumentation. This work shows that the rapid assay is able to identify changes in the denaturation pathway, due to mutations or removal of cofactors, which affect the stability of the native and intermediate states. This would be of significant benefit for the directed evolution of protein stability, optimizing enzyme stability under biocatalytic process conditions, and also for engineering specific transitions in protein unfolding pathways. Copyright 2007 Wiley Periodicals, Inc.
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              Bioresour. Technol.

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                Author and article information

                Journal
                jmcs
                Journal of the Mexican Chemical Society
                J. Mex. Chem. Soc
                Sociedad Química de México A.C. (México, DF, Mexico )
                1870-249X
                December 2010
                : 54
                : 4
                : 198-203
                Affiliations
                [01] Orizaba Veracruz orgnameInstituto Tecnológico de Orizaba orgdiv1Departamento de Posgrado e Investigación México llopezz02@ 123456yahoo.com.mx
                Article
                S1870-249X2010000400004 S1870-249X(10)05400400004
                2988c624-9a07-4ead-977c-e9c6857f8cf1

                This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.

                History
                : 20 August 2010
                : 26 April 2010
                Page count
                Figures: 0, Tables: 0, Equations: 0, References: 27, Pages: 6
                Product

                SciELO Mexico

                Categories
                Articles

                etanol,superficie de respuesta,fermentación levadura,hidrólisis ácida,Almidón yuca,ethanol,response surface,yeast fermentation,acid hydrolysis,Cassava starch

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