M
Martina Pohl
Researcher at Forschungszentrum Jülich
Publications - 207
Citations - 6655
Martina Pohl is an academic researcher from Forschungszentrum Jülich. The author has contributed to research in topics: Benzoylformate decarboxylase & Pyruvate decarboxylase. The author has an hindex of 44, co-authored 206 publications receiving 6024 citations. Previous affiliations of Martina Pohl include Hamburg University of Technology & University of Düsseldorf.
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Journal ArticleDOI
Improved biocatalysts by directed evolution and rational protein design.
Uwe T. Bornscheuer,Martina Pohl +1 more
TL;DR: The efficient application of biocatalysts requires the availability of suitable enzymes with high activity and stability under process conditions, desired substrate selectivity and high enantioselectivity, which often need to be optimized to fulfill these requirements.
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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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Effect of Oxygen Limitation and Medium Composition on Escherichia coli Fermentation in Shake‐Flask Cultures
TL;DR: The results suggest that the length of fermentation, choice of medium, and aeration do not normally satisfy the requirements for unlimited growth in shake flasks, and variation of medium composition and oxygen supply can be evaluated by the measurement of the respiratory activity.
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Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directed mutagenesis of cysteine residues.
TL;DR: Initial results in initial tests concerning the application of the enzyme for regeneration of NADH in biotransformation of trimethyl pyruvate to Ltert leucine were obtained with two mutants, FDHC23S and FDHC 23S/C262A, which are significantly more stable than the wt enzyme.
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A new perspective on thiamine catalysis.
TL;DR: The three-dimensional structures of ThDP-dependent enzymes seem to be highly similar, and an ever-expanding range of reactions that they are able to catalyze and see increased amino acid sequence heterogeneity are found.