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        Alcoholic fermentation with high sugar and cell concentration at moderate temperatures using flocculant yeasts

        Ana Carolina Tolentino Brandão,Miriam Maria de Resende,Eloízio Júlio Ribeiro 한국화학공학회 2020 Korean Journal of Chemical Engineering Vol.37 No.10

        This paper studied bioethanol production at very high gravity (VHG) conditions using flocculent Saccharomyces cerevisiae, evaluating the response yield, ethanol concentration, productivity, and residual sugar through a central composite design (CCD). This CCD was evaluated at 12 and 24 h fermentation times. In the CCD evaluated for 12 h of fermentation, the best condition for alcoholic fermentation was 27 oC, 260 g/L substrate concentration and a 30% v/v cell concentration; a maximum overall desirability of 0.937 was achieved. For CCD at 24 h of fermentation, the best condition was 27 oC, 300 g/L substrate concentration, and a 26% v/v cell concentration. The desirability achieved was 0.811. These conditions allowed us to verify, experimentally, that the CCD models described the fermentation behavior well. VHG alcoholic fermentation in fed-batch with the reuse of cells without chemical treatment was performed using the optimum conditions obtained from the desirability function (27 oC, 300 g/L, 26% v/v). This resulted in favorable alcohol content 132.90 g/L in comparison to the conventional fermentation process.

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        Immobilization of commercial acid phosphatases from wheat germ and potato onto ion exchangers

        Lima Frederico Alves,Martins Pedro Alves,Wilson Galvão de Morais Júnior,Ribeiro Eloízio Júlio,Guisán José Manuel,de Resende Miriam Maria 한국화학공학회 2023 Korean Journal of Chemical Engineering Vol.40 No.9

        A very simple and fast immobilization technique based on ion exchange was investigated to improve the thermal stability of acid phosphatase from wheat germ and potato. Immobilization was not efficient for the DEAE-sepharose, and MANAE-agarose supports. On the other hand, Toyopearl DEAE-650s proved to be a promising support, with immobilization yield above 95% and recovery of activity above 85% for both enzymes. A second step was introduced in the immobilization protocol to improve the thermal stability of these biocatalysts. For this, oxidation and reduction of glycosidic chains of acid phosphatase were carried out, allowing the formation of aldehyde groups and subsequent interaction with the amine groups to further stabilize the different forms (free and immobilized). Both biocatalysts showed residual activity after 1 hour of inactivation at the temperature of 60 °C, a fact not observed for the free enzyme. The wheat germ acid phosphatase derivative was the most stable, with residual activity of 66.7% for the only immobilized derivative and 76.2% for the oxidized/reduced derivative. Also, the derivatives prepared by ion exchange adsorption on Toyopearl (TOYO), followed by oxidation/reduction and intramolecular crosslinking, were approximately 15 and 41 times more stable than the free enzyme from wheat germ.

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