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    Item type:Publication, Access status: with files ,
    Non-canonical amino acids as a useful synthetic biological tool for lipase-catalysed reactions in hostile environments
    (Royal Society of Chemistry (RSC), 2013)
    Acevedo-Rocha, Carlos G.
    ;
    Hoesl, Michael G.
    ;
    Nehring, Sebastian
    ;
    Royter, Maryna
    ;
    Wolschner, Christina
    The incorporation of several non-canonical amino acids into the Thermoanaerobacter thermohydrosulfuricus lipase confers not only activity enhancement upon treatment with organic solvents (by up to 450%) and surfactants (resp. 1630%), but also protective effects against protein reducing (resp. 140%), alkylating (resp. 160%), and denaturing (resp.190%) agents as well as inhibitors (resp. 40%). This approach offers novel chemically diversified biocatalysts for hostile environments. © 2013 The Royal Society of Chemistry.
    Publicationtype: Journal Article
      110  9
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    Item type:Publication, Access status: without files ,
    Lipase congeners designed by genetic code engineering
    (Wiley-VCH, 2011)
    Hoesl, Michael G.
    ;
    Acevedo-Rocha, Carlos G.
    ;
    Nehring, Sebastian
    ;
    Royter, Maryna
    ;
    Wolschner, Christina
    Classical enzyme optimization exploits the chemistry confined to the 20 canonical amino acids encoded by the standard genetic code. 'Genetic code engineering' allows the global substitution of particular residues with synthetic analogues, endowing proteins with chemical diversity not found in nature. These proteins are congeners of the parent protein because they originate from the same gene sequence, but contain a fraction of noncanonical amino acids. Global substitutions of methionine, proline, phenylalanine, and tyrosine have been carried out with related analogues in Thermoanaerobacter thermohydrosulfuricus lipase. This study represents the first extensive report of an important biocatalyst substituted with a high number of noncanonical amino acids. The generated lipase congeners displayed special features such as enhanced activation, elevated enzyme activity (by up to 25%) and substrate tolerance (by up to 40%), and changes in optimal temperature (by up to 20°C) and pH (by up to 3). These emergent features achieved by genetic code engineering might be important not only for academic research, but also for numerous economical applications in the food, detergent, chemical, pharmaceutical, leather, textile, cosmetic, and paper industries. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
    Publicationtype: Journal Article
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