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Transesterifications and Peracid-Assisted Oxidations in Aqueous Media Catalyzed by Mycobacterium smegmatis Acyl Transferase

Authors

  • Lotte Wiermans,

    1. Institut für Technische und Makromolekulare Chemie (ITMC), RWTH Aachen University, Worringer Weg 1, 52074 Aachen (Germany), Fax: (+49) 241-8022177
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  • Sebastian Hofzumahaus,

    1. Junior Professorship for Biocatalysis, Institute of Biotechnology, RWTH Aachen University, Helmertweg 3, 52074 Aachen (Germany)
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  • Christiane Schotten,

    1. Institut für Technische und Makromolekulare Chemie (ITMC), RWTH Aachen University, Worringer Weg 1, 52074 Aachen (Germany), Fax: (+49) 241-8022177
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  • Lisa Weigand,

    1. Institut für Technische und Makromolekulare Chemie (ITMC), RWTH Aachen University, Worringer Weg 1, 52074 Aachen (Germany), Fax: (+49) 241-8022177
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  • Marcus Schallmey,

    1. Forschungszentrum Jülich GmbH, Institute of Bio- and Geosciences, IBG-1: Biotechnology, 52425 Jülich (Germany)
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  • Dr. Anett Schallmey,

    1. Junior Professorship for Biocatalysis, Institute of Biotechnology, RWTH Aachen University, Helmertweg 3, 52074 Aachen (Germany)
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  • Dr. Pablo Domínguez de María

    Corresponding author
    1. Institut für Technische und Makromolekulare Chemie (ITMC), RWTH Aachen University, Worringer Weg 1, 52074 Aachen (Germany), Fax: (+49) 241-8022177
    • Institut für Technische und Makromolekulare Chemie (ITMC), RWTH Aachen University, Worringer Weg 1, 52074 Aachen (Germany), Fax: (+49) 241-8022177

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Abstract

Hydrolases catalyze synthetic reactions in nonaqueous media, whereas they perform hydrolysis under aqueous solutions. An acyl transferase from Mycobacterium smegmatis (MsAcT) is able to catalyze synthetic reactions in buffer because of its highly hydrophobic active site, which enables efficient transesterification reactions even at 99.9 % v/v buffer solution. This unique feature of MsAcT among hydrolases may open new opportunities to conduct synthetic (bio)catalysis in aqueous media. With these goals in mind, this paper explores some evidence of such potential: MsAcT can perform enantioselective transesterifications (e.g., (S)-2-octanol), which could be combined with other aqueous multistep (asymmetric) reactions; 5-hydroxymethylfurfural (HMF) can be esterified to produce more hydrophobic and easily extractable HMF esters (e.g., for downstream processing or wastewater treatment); and upon addition of dilute H2O2, MsAcT works efficiently as a perhydrolase to form in situ peracids—in bulk water—that can be used for oxidations (e.g., furfural to furoic acid oxidation). Overall, these and many other new applications can be envisaged by using MsAcT in aqueous solutions.

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