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

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    Authors
    Sans, Cristina
    García-Fruitós, Elena
    Ferraz, Rosa M
    González-Montalbán, Núria
    Rinas, Ursula
    López-Santín, Josep
    Villaverde, Antonio
    Álvaro, Gregorio
    Issue Date
    2012-07-24
    
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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.
    Citation
    Inclusion bodies of fuculose-1-phosphate aldolase as stable and reusable biocatalysts., 28 (2):421-7 Biotechnol. Prog.
    Affiliation
    Dept. d'Enginyeria Química, Escola d'Enginyeria, Unitat de Biocatàlisi Aplicada Associada al IQAC (CSIC), Universitat Autònoma de Barcelona, Edifici Q, 08193 Bellaterra, Spain.
    Journal
    Biotechnology progress
    URI
    http://hdl.handle.net/10033/235575
    DOI
    10.1002/btpr.1518
    PubMed ID
    22275283
    Type
    Article
    Language
    en
    ISSN
    1520-6033
    ae974a485f413a2113503eed53cd6c53
    10.1002/btpr.1518
    Scopus Count
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    publications of the research group recombinant protein expression (RPEX)

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