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Enzyme and Microbial Technology|December 12, 2017
Baeyer-Villiger monooxygenases from Yarrowia lipolytica catalyze preferentially sulfoxidationsSven Bordewick, Andy Beier, Kathleen Balke, et al.Applied Microbiology and Biotechnology|November 24, 2007
Functional expression, purification, and characterization of the recombinant Baeyer-Villiger monooxygenase MekA from Pseudomonas veronii MEK700Anne Völker, Anett Kirschner, Uwe T Bornscheuer, et al.AMB Express|October 14, 2014
Metabolism of alkenes and ketones by Candida maltosa and related yeastsAndy Beier, Veronika Hahn, Uwe T Bornscheuer, et al.Methods and Protocols|August 27, 2025
Expression of Recombinant Hirudin in Bacteria and Yeast: A Comparative ApproachZhongjie Wang, Dominique Böttcher, Uwe T Bornscheuer, et al.Chembiochem : a European Journal of Chemical Biology|February 7, 2024
Systematic Analysis of the MIO-forming Residues of Aromatic Ammonia LyasesYannik Brack, Chenghai Sun, Dong Yi, et al.Chembiochem : a European Journal of Chemical Biology|March 30, 2022
Discovery of Novel Tyrosine Ammonia Lyases for the Enzymatic Synthesis of p-Coumaric AcidYannik Brack, Chenghai Sun, Dong Yi, et al.Methods in Molecular Biology (Clifton, N.J.)|December 1, 2016
A Microtiter Plate-Based Assay to Screen for Active and Stereoselective Hydrolytic Enzymes in Enzyme LibrariesDominique Böttcher, Patrick Zägel, Marlen Schmidt, et al.Journal of Biotechnology|September 28, 2015
The effect of disulfide bond introduction and related Cys/Ser mutations on the stability of a cyclohexanone monooxygenaseSandy Schmidt, Maika Genz, Kathleen Balke, et al.Analytical Chemistry|February 13, 2010
Conductometric method for the rapid characterization of the substrate specificity of amine-transaminasesSebastian Schätzle, Matthias Höhne, Karen Robins, et al.Molecules (Basel, Switzerland)|January 11, 2022
Biochemical and Structural Analysis of a Glucose-Tolerant β-Glucosidase from the Hemicellulose-Degrading Thermoanaerobacterium saccharolyticumIn Jung Kim, Uwe T Bornscheuer, Ki Hyun NamPageof 556