B
Bettina Lingen
Researcher at University of Düsseldorf
Publications - 7
Citations - 575
Bettina Lingen is an academic researcher from University of Düsseldorf. The author has contributed to research in topics: Benzoylformate decarboxylase & Site-directed mutagenesis. The author has an hindex of 5, co-authored 7 publications receiving 552 citations.
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Journal ArticleDOI
Development of a donor-acceptor concept for enzymatic cross-coupling reactions of aldehydes: the first asymmetric cross-benzoin condensation.
Pascal Dünkelmann,Doris Kolter-Jung,Adam Nitsche,Ayhan S. Demir,Petra Siegert,Bettina Lingen,Martin Baumann,Martina Pohl,Michael Müller +8 more
TL;DR: Highly enantioenriched mixed benzoins are obtained selectively through a biocatalytical cross-coupling reaction of aromatic aldehydes using ThDP-dependent enzymes.
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Thiamin-diphosphate-dependent enzymes: new aspects of asymmetric C-C bond formation.
TL;DR: A selective donor-acceptor concept was established leading to the first asymmetric cross-benzoin condensation, and a kinetic racemic resolution through C-C bond cleavage was developed that approached the synthesis of new chiral building blocks on a preparative scale.
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Improving the carboligase activity of benzoylformate decarboxylase from Pseudomonas putida by a combination of directed evolution and site-directed mutagenesis.
TL;DR: Surprisingly, all L476 mutants catalyze the formation of 2-hydroxy-1-phenyl-propanone with significantly higher enantioselectivity than the wild-type enzyme although enantiOSElectivity was not a selection parameter.
Journal ArticleDOI
Alteration of the substrate specificity of benzoylformate decarboxylase from Pseudomonas putida by directed evolution.
Bettina Lingen,Doris Kolter-Jung,Pascal Dünkelmann,Ralf Feldmann,Joachim Grötzinger,Martina Pohl,Michael Müller +6 more
TL;DR: Reduction of the side chain size at position L461 probably results in an enlarged substrate binding site and facilitates the initial binding of ortho‐substituted benzaldehyde derivatives to the cofactor ThDP.
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High-throughput assay of (R)-phenylacetylcarbinol synthesized by pyruvate decarboxylase
TL;DR: A novel assay, using 2,3,5-triphenyltetrazolium chloride, enables high-throughput photometric analysis of the activity of the enzyme thus avoiding time-consuming chromatographic procedures.