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Modulation of Transaminase Activity by Encapsulation in Temperature‐Sensitive Poly(N‐acryloyl glycinamide) Hydrogels

ChemBioChem, vol. 22, pp. 3452–3461

Abstract

Smart hydrogels hold much potential for biocatalysis, not only for the immobilization of enzymes, but also for the control of enzyme activity. We investigated upper critical solution temperature-type poly N-acryloyl glycinamide (pNAGA) hydrogels as a smart matrix for the amine transaminase from Bacillus megaterium (BmTA). Physical entrapment of BmTA in pNAGA hydrogels results in high immobilization efficiency (>89 %) and high activity (97 %). The temperature-sensitiveness of pNAGA is preserved upon immobilization of BmTA and shows a gradual deswelling upon temperature reduction. While enzyme activity is mainly controlled by temperature, deactivation tended to be higher for immobilized BmTA (≈62-68 %) than for free BmTA (≈44 %), suggesting a deactivating effect due to deswelling of the pNAGA gel. Although the deactivation in response to hydrogel deswelling is not yet suitable for controlling enzyme activity sufficiently, it is nevertheless a good starting point for further optimization.

Authors 5

  1. Forschungszentrum Jülich · RWTH Aachen University

    Affiliation as printed

    Aachen Biology and Biotechnology (ABBt) RWTH Aachen University Worringerweg 1 52074 Aachen Germany

    Institute of Bio- and Geosciences – Biotechnology (IBG-1) Forschungszentrum Jülich GmbH Wilhelm-Johnen-Straße 52425 Jülich Germany

    Institute of Bio- and Geosciences – Biotechnology (IBG-1) Forschungszentrum Jülich GmbH Wilhelm-Johnen-Straße 52425 Jülich Germany

  2. Bavarian Polymer Institute · University of Bayreuth

    Affiliation as printed

    Macromolecular Chemistry Bavarian Polymer Institute University of Bayreuth Universitätsstrasse 30 95440 Bayreuth Germany

  3. Bavarian Polymer Institute · University of Bayreuth

    Affiliation as printed

    Macromolecular Chemistry Bavarian Polymer Institute University of Bayreuth Universitätsstrasse 30 95440 Bayreuth Germany

  4. Forschungszentrum Jülich · RWTH Aachen University

    Affiliation as printed

    Aachen Biology and Biotechnology (ABBt) RWTH Aachen University Worringerweg 1 52074 Aachen Germany

    Institute of Bio- and Geosciences – Biotechnology (IBG-1) Forschungszentrum Jülich GmbH Wilhelm-Johnen-Straße 52425 Jülich Germany

    Institute of Bio- and Geosciences – Biotechnology (IBG-1) Forschungszentrum Jülich GmbH Wilhelm-Johnen-Straße 52425 Jülich Germany

  5. Christiane Claaßen corresponding

    Forschungszentrum Jülich

    Affiliation as printed

    Institute of Bio- and Geosciences – Biotechnology (IBG-1) Forschungszentrum Jülich GmbH Wilhelm-Johnen-Straße 52425 Jülich Germany

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References 84