Nine single cysteine TmArgBP mutants were created and labeled with three different environmentally sensitive fluorescent probes.
Seven CYP24A1 mutants were created and studied by mammalian cell transfection and CYP24A1 activity assay.
For six most frequently occurring mutations, the corresponding single mutants were created to dissect the effects of these mutations.
Moreover, T. atroviride mutants were created by mutagenesis using N-methyl-N'-nitro-N-nitrosoguanidine (NTG) as well as UV-light.
Considering the possibility of a further improvement in thermostability, eleven mutants were created in the present study via site-directed mutagenesis using XynA as a template.
In order to gain insight into the structural stability and folding of mitoNEET's iron sulfur clusters, mutants were created using site-directed mutagenesis.
A number of engineered Trichoderma reesei endo-β-1,4-xylanase (Xyn II) mutants were created and activity tests were performed for increased stability.
Starting from the strictly NADH specific water-forming Streptococcus mutans NADH oxidase 2 several rationally designed cofactor binding site mutants were created and kinetic values for NADH and NADPH conversion were determined.
In the first of two approaches, the feasibility of shielding the A-domain by N-linked glycans was evaluated, whereas in the second approach C-strain mutants were created with targeted deletions in the A-domain.
Finally, with the integration of the alcohol dehydrogenase gene (adhE1 or adhE2) to replace cat1 (the key gene responsible for butyrate production and previously could not be deleted), two mutants were created for n-butanol production, with the butanol titer reached historically record high of 26.2 g/L in a batch fermentation.
GLTP point mutants were created by QuikChange mutagenesis (Stratagene).
