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      Supercritical carbon dioxide pasteurization to reduce the activity of muscle protease and its impact on physicochemical properties of Nile tilapia

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      Research Ideas and Outcomes
      Pensoft Publishers

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          Abstract

          The studies of the effect of supercritical carbon dioxide (scCO2) pasteurization on solid food from fish origin are scarcely available. This study was intended to address that gap by investigating the effect of scCO2 on the reduction of muscle protease activity and its impact on physicochemical properties of the Nile tilapia. Tilapia were exposed to CO2 pressure at 70, 75, 80, 85, and 90 bar; temperature at 40 °C; and holding time for 15 min. This study discovered that 80 bar was the minimum pressure to achieve half residual activity of muscle protease and two logs reductions of microbial counts. The applications of 80 and 85 bar were found to achieve significant reduction of tilapia muscle protease activity while still maintained acceptable textural properties. Both 80 and 85 bar were found to be effective to inhibit softening development of tilapia fillet during 14 days of chilled storage. Eighty-five bar and 15 min CO2 pasteurization was considered as maximum level of CO2 pressure that tilapia could withstand without degrading its texture significantly.

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          The CIEDE2000 color-difference formula: Implementation notes, supplementary test data, and mathematical observations

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            Food preservation by high pressure

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              Dynamic cycling of eIF2 through a large eIF2B-containing cytoplasmic body

              The eukaryotic translation initiation factor 2B (eIF2B) provides a fundamental controlled point in the pathway of protein synthesis. eIF2B is the heteropentameric guanine nucleotide exchange factor that converts eIF2, from an inactive guanosine diphosphate–bound complex to eIF2-guanosine triphosphate. This reaction is controlled in response to a variety of cellular stresses to allow the rapid reprogramming of cellular gene expression. Here we demonstrate that in contrast to other translation initiation factors, eIF2B and eIF2 colocalize to a specific cytoplasmic locus. The dynamic nature of this locus is revealed through fluorescence recovery after photobleaching analysis. Indeed eIF2 shuttles into these foci whereas eIF2B remains largely resident. Three different strategies to decrease the guanine nucleotide exchange function of eIF2B all inhibit eIF2 shuttling into the foci. These results implicate a defined cytoplasmic center of eIF2B in the exchange of guanine nucleotides on the eIF2 translation initiation factor. A focused core of eIF2B guanine nucleotide exchange might allow either greater activity or control of this elementary conserved step in the translation pathway.
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                Author and article information

                Journal
                Research Ideas and Outcomes
                RIO
                Pensoft Publishers
                2367-7163
                July 31 2020
                July 31 2020
                : 6
                Article
                10.3897/rio.6.e56887
                fd353d3d-e5e2-4b3b-94d8-cc581755fea0
                © 2020

                http://creativecommons.org/licenses/by/4.0/

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