L
Lasse Greiner
Researcher at RWTH Aachen University
Publications - 74
Citations - 2097
Lasse Greiner is an academic researcher from RWTH Aachen University. The author has contributed to research in topics: Catalysis & Ionic liquid. The author has an hindex of 26, co-authored 74 publications receiving 1994 citations. Previous affiliations of Lasse Greiner include Forschungszentrum Jülich & DECHEMA.
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Ionic liquids in biotechnology: applications and perspectives for biotransformations
TL;DR: The overview reveals that the exploration and mapping of ionic liquids with respect to biocatalysis is still sketchy, but it is apparent that advantages can be gained in view of activity, stability and selectivity.
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Benzoylformate Decarboxylase from Pseudomonas putida as Stable Catalyst for the Synthesis of Chiral 2‐Hydroxy Ketones
Hans Iding,Thomas Dünnwald,Lasse Greiner,Andreas Liese,Michael Müller,Petra Siegert,Joachim Grötzinger,Ayhan S. Demir,Martina Pohl +8 more
TL;DR: A new enzyme tool comprising a vast applicability for stereoselective synthesis and a simple way to increase the enantiomeric excess of (S)-2-hydroxy-1-phenyl-propanone from 90% to 95% by skillful choice of the reaction parameters is presented.
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Substrate dependent synergetic and antagonistic interaction of ammonium halide and polyoxometalate catalysts in the synthesis of cyclic carbonates from oleochemical epoxides and CO2
TL;DR: In this article, organic halides and polyoxometalates (POMs) were used as catalysts for the insertion of carbon dioxide into epoxides originating from plant oils as biogenic feedstock.
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Practical applications of hydrogenase I from Pyrococcus furiosus for NADPH generation and regeneration
TL;DR: It could be demonstrated, that this hyperthermophilic hydrogenase exhibits a high stability under reaction conditions and generation as well as regeneration of NADPH were performed in batch and repetitive batch experiments with recycling of the biocatalyst.
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Continuous Application of Chemzymes in a Membrane Reactor: Asymmetric Transfer Hydrogenation of Acetophenone
TL;DR: In this paper, a transfer hydrogenation catalyst was attached to a polymer and the resulting homogeneously soluble, polymer-bound catalyst (chemzyme) can now be retained by ultrafiltration membranes like enzymes.