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Sökning: WFRF:(S. Humble Maria)

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1.
  • Cassimjee, Karim Engelmark, et al. (författare)
  • Streamlined Preparation of Immobilized Candida antarctica Lipase B
  • 2017
  • Ingår i: ACS Omega. - : American Chemical Society (ACS). - 2470-1343. ; 2:12, s. 8674-8677
  • Tidskriftsartikel (refereegranskat)abstract
    • Candida antarctica lipase B (CalB) was efficiently expressed (6.2 g L-1) in Escherichia coli by utilizing an N-terminal tag cassette and the XylS/Pm expression system in a fed-batch bioreactor; subsequent direct binding to EziG from crude extracts resulted in an immobilized catalyst with superior activity to Novozym 435.
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3.
  • Ruggieri, Federica, 1990-, et al. (författare)
  • Insight into the dimer dissociation process of the Chromobacterium violaceum (S)-selective amine transaminase
  • 2019
  • Ingår i: Scientific Reports. - : Nature Publishing Group. - 2045-2322.
  • Tidskriftsartikel (refereegranskat)abstract
    • One of the main factors hampering the implementation in industry of transaminase-based processes for the synthesis of enantiopure amines is their often low storage and operational stability. Our still limited understanding of the inactivation processes undermining the stability of wild-type transaminases represents an obstacle to improving their stability through enzyme engineering. In this paper we present a model describing the inactivation process of the well-characterized (S)-selective amine transaminase from Chromobacterium violaceum. The cornerstone of the model, supported by structural, computational, mutagenesis and biophysical data, is the central role of the catalytic lysine as a conformational switch. Upon breakage of the lysine-PLP Schiff base, the strain associated with the catalytically-active lysine conformation is dissipated in a slow relaxation process capable of triggering the known structural rearrangements occurring in the holo-to-apo transition and ultimately promoting dimer dissociation. Due to the occurrence in the literature of similar PLP-dependent inactivation models valid for other non-transaminase enzymes belonging to the same fold-class, the role of the catalytic lysine as conformational switch might extend beyond the transaminase enzyme group and offer new insight to drive future non-trivial engineering strategies.
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