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  • 1. Steffen-Munsberg, Fabian
    et al.
    Vickers, Clare
    Thontowi, Ahmad
    Schaetzle, Sebastian
    Meinhardt, Tina
    Humble, Maria Svedendahl
    Stockholm University, Faculty of Science, Department of Organic Chemistry.
    Land, Henrik
    Berglund, Per
    Bornscheuer, Uwe T.
    Hoehne, Matthias
    Revealing the structural basis of promiscuous amine transaminase activity2013In: ChemCatChem, ISSN 1867-3880, E-ISSN 1867-3899, Vol. 5, no 1, p. 154-157Article in journal (Refereed)
  • 2. Steffen-Munsberg, Fabian
    et al.
    Vickers, Clare
    Thontowi, Ahmad
    Schaetzle, Sebastian
    Tumlirsch, Tony
    Humble, Maria Svedendahl
    Stockholm University, Faculty of Science, Department of Organic Chemistry.
    Land, Henrik
    Berglund, Per
    Bornscheuer, Uwe T.
    Hoehne, Matthias
    Connecting unexplored protein crystal structures to enzymatic function2013In: ChemCatChem, ISSN 1867-3880, E-ISSN 1867-3899, Vol. 5, no 1, p. 150-153Article in journal (Refereed)
  • 3.
    Wikmark, Ylva
    et al.
    Stockholm University, Faculty of Science, Department of Organic Chemistry.
    Humble, Maria Svedendahl
    Stockholm University, Faculty of Science, Department of Organic Chemistry.
    Bäckvall, Jan-E.
    Stockholm University, Faculty of Science, Department of Organic Chemistry.
    Combinatorial Library Based Engineering of Candida antarctica Lipase A for Enantioselective Transacylation of sec-Alcohols in Organic Solvent2015In: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 54, no 14, p. 4284-4288Article in journal (Refereed)
    Abstract [en]

    A method for determining lipase enantioselectivity in the transacylation of sec-alcohols in organic solvent was developed. The method was applied to a model library of Candida antarctica lipase A (CalA) variants for improved enantioselectivity (E values) in the kinetic resolution of 1-phenylethanol in isooctane. A focused combinatorial gene library simultaneously targeting seven positions in the enzyme active site was designed. Enzyme variants were immobilized on nickel-coated 96-well microtiter plates through a histidine tag (His6 -tag), screened for transacylation of 1-phenylethanol in isooctane, and analyzed by GC. The highest enantioselectivity was shown by the double mutant Y93L/L367I. This enzyme variant gave an E value of 100 (R), which is a dramatic improvement on the wild-type CalA (E=3). This variant also showed high to excellent enantioselectivity for other secondary alcohols tested.

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