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Inclusion bodies of fuculose-1-phosphate aldolase as stable and reusable biocatalysts

Authors

  • Cristina Sans,

    1. Dept. d'Enginyeria Química, Escola d'Enginyeria, Unitat de Biocatàlisi Aplicada Associada al IQAC (CSIC), Universitat Autònoma de Barcelona, Edifici Q, 08193 Bellaterra, Spain
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  • Elena García-Fruitós,

    1. Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain
    2. CIBER de Bioingeniería, Biomateriales y Nanomedicina (CIBER-BBN), Bellaterra, 08193 Barcelona, Spain
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  • Rosa M. Ferraz,

    1. Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain
    Current affiliation:
    1. Bioingenium S.L.Edifici Hèlix, Parc Científic de Barcelona c/ Baldiri Reixac, 15-21, 08028 Barcelona, Spain
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  • Núria González-Montalbán,

    1. Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain
    Current affiliation:
    1. Center for Biomedical Engineering and Technology (BioMET), University of Maryland School of Medicine, 725 West Lombard Street, Room N370. Baltimore, MD 21201.
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  • Ursula Rinas,

    1. Helmholtz Centre for Infection Research, Inhoffenstr. 7, 38124 Braunschweig, Germany
    2. Leibniz University Hannover, Life Science—Technical Chemistry, Callinstr. 5, 30167 Hannover, Germany
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  • Josep López-Santín,

    Corresponding author
    1. Dept. d'Enginyeria Química, Escola d'Enginyeria, Unitat de Biocatàlisi Aplicada Associada al IQAC (CSIC), Universitat Autònoma de Barcelona, Edifici Q, 08193 Bellaterra, Spain
    • Dept. d'Enginyeria Química, Escola d'Enginyeria, Unitat de Biocatàlisi Aplicada Associada al IQAC (CSIC), Universitat Autònoma de Barcelona, Edifici Q, 08193 Bellaterra, Spain
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  • Antonio Villaverde,

    1. Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain
    2. CIBER de Bioingeniería, Biomateriales y Nanomedicina (CIBER-BBN), Bellaterra, 08193 Barcelona, Spain
    3. Dept. de Genètica i de Microbiologia, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain
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  • Gregorio Álvaro

    1. Dept. d'Enginyeria Química, Escola d'Enginyeria, Unitat de Biocatàlisi Aplicada Associada al IQAC (CSIC), Universitat Autònoma de Barcelona, Edifici Q, 08193 Bellaterra, Spain
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Abstract

Fuculose-1-phosphate aldolase (FucA) has been produced in Escherichia coli as active inclusion bodies (IBs) in batch cultures. The activity of insoluble FucA has been modulated by a proper selection of producing strain, culture media, and process conditions. In some cases, when an optimized defined medium was used, FucA IBs were more active (in terms of specific activity) than the soluble protein version obtained in the same process with a conventional defined medium, supporting the concept that solubility and conformational quality are independent protein parameters. FucA IBs have been tested as biocatalysts, either directly or immobilized into Lentikat® beads, in an aldolic reaction between DHAP and (S)-Cbz-alaninal, obtaining product yields ranging from 65 to 76%. The production of an active aldolase as IBs, the possibility of tailoring IBs properties by both genetic and process approaches, and the reusability of IBs by further entrapment in appropriate matrices fully support the principle of using self-assembled enzymatic clusters as tunable mechanically stable and functional biocatalysts. © 2012 American Institute of Chemical Engineers Biotechnol. Prog., 2012

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