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2 results on '"Lutz Wobbe"'

1. A novel, robust and mating-competent Chlamydomonas reinhardtii strain with an enhanced transgene expression capacity for algal biotechnology

Author

Polina Dementyeva, Robert A. Freudenberg, Thomas Baier, Kristin Rojek, Lutz Wobbe, Bernd Weisshaar, and Olaf Kruse

Subjects
Chlamydomonas reinhardtii, Algal biotechnology, Transgene expression, Industrial strains, Robustness traits, Biotechnology, TP248.13-248.65
Abstract

In the future, algae biotechnology could play an important role in sustainable development, especially with regard to the production of valuable chemicals. Among the established laboratory strains with efficient transgene expression, there are none that have demonstrated the required robustness for industrial applications, which generally require growth at larger scale. Here, we created a robust and mating-competent cell line of the green microalga Chlamydomonas reinhardtii, which also possesses a high transgene expression capacity. This strain shows a comparably high resistance to shear stress by accumulating increased amounts of biomass under these conditions. As a proof-of-concept, a high phototrophic productivity of cadaverine from CO2 and nitrate was demonstrated by efficiently expressing a bacterial l-lysine decarboxylase. In contrast to other established strains, this novel chassis strain for phototrophic production schemes is equipped with the traits required for industrial applications, by combining mating-competence, cell wall-mediated robustness and high level transgene expression.

Published
2021
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2. Type II flavoprotein monooxygenase PsFMO_A from the bacterium Pimelobacter sp. Bb-B catalyzes enantioselective Baeyer-Villiger oxidations with a relaxed cofactor specificity

Author

Lutz Wobbe, Thomas Baier, Jana Löwe, Olaf Kruse, Olga Blifernez-Klassen, and Harald Gröger

Subjects
0106 biological sciences, 0301 basic medicine, Stereochemistry, Flavoprotein, Bioengineering, Formate dehydrogenase, 01 natural sciences, Applied Microbiology and Biotechnology, Cofactor, Mixed Function Oxygenases, Bridged Bicyclo Compounds, 03 medical and health sciences, chemistry.chemical_compound, Bacterial Proteins, 010608 biotechnology, Escherichia coli, Botryococcus braunii, Formate, chemistry.chemical_classification, Flavoproteins, biology, Chemistry, Substrate (chemistry), Stereoisomerism, General Medicine, Monooxygenase, biology.organism_classification, Camphor, Actinobacteria, 030104 developmental biology, Enzyme, biology.protein, Oxidation-Reduction, Biotechnology
Abstract

Microbial consortia, which degrade branched, long-chain hydrocarbons, can be regarded as a promising source of novel enzymes for the stereo- and regio-selective oxyfunctionalization of hydrocarbons. The hydrocarbon-degrading bacterium Pimelobacter sp. Bb-B was isolated from the consortium associated with the colonial hydrocarbon-excreting microalga Botryococcus braunii. Three new type II flavoprotein monooxygenases (type II FMOs) from this bacterium have been made available in recombinant form through cloning and overexpression in an E. coli host organism. These enzymes (PsFMO_A-C) were characterized in terms of their capability of catalyzing Baeyer-Villiger oxidations with distinct substrates. The highest activity was detected when utilizing camphor and bicyclo[3.2.0]hept-2-en-6-one as substrate in combination with PsFMO_A as the most promising enzyme. Furthermore, synthetic biotransformations with 5 mM of the substrate bicyclo[3.2.0]hept-2-en-6-one, formate and formate dehydrogenase for in situ-cofactor recycling were conducted with this enzyme, leading to a substrate consumption of 85% after 66 h and excellent enantioselectivity of 99% ee for the (1R,5S)-enantiomer. Additionally, an alternative in situ-cofactor recycling based on the use of microalgae for in situ-production of formate from carbon dioxide, water and light together with a formate dehydrogenase was combined successfully with the enzyme PsFMO_A, leading to a substrate consumption of 94% and an enantioselectivity of >99% ee for the so-called “normal lactone”-enantiomer with the absolute configuration 1R,5S.

Published
2019

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