Michael Kotik
Academy of Sciences of the Czech Republic
39 Papers
320 Citations
Michael Kotik is an academic researcher from Academy of Sciences of the Czech Republic. The author has contributed to research in topics: Epoxide hydrolase & Epoxide. The author has an hindex of 15, co-authored 36 publications. Previous affiliations of Michael Kotik include Centre national de la recherche scientifique.
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Papers
Biodegradation of phenolic compounds by Basidiomycota and its phenol oxidases: A review
TL;DR: It is concluded that low-cost sources of these enzymes should be searched for and the benefits of enzymatic, biological and physico-chemical methods could be combined to make the processes fit for industrial use.
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Novel genes retrieved from environmental DNA by polymerase chain reaction: current genome-walking techniques for future metagenome applications.
TL;DR: This review covers the diverse array of genome-walking techniques, which were originally developed for genomic DNA and currently are also used for PCR-based recovery of entire genes from the metagenome.
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Access to enantiopure aromatic epoxides and diols using epoxide hydrolases derived from total biofilter DNA
TL;DR: Two recombinant EHs, Kau2 and Kau8, were retrieved from total DNA isolated from biofilter-derived biomass using PCR with EH-specific degenerate primers followed by genome-walking PCR and showed broad substrate specificity and preferentially hydrolyzed epoxides with S -configuration, and Kau2 showed enantioconvergent hydrolysis activity.
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Cloning of an epoxide hydrolase-encoding gene from Aspergillus niger M200, overexpression in E. coli, and modification of activity and enantioselectivity of the enzyme by protein engineering
TL;DR: It is underlines that single amino acid exchanges in the substrate tunnel region can lead to significant improvements in enantioselectivity and activity of the epoxide hydrolase from A. niger M200.
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Novel microbial epoxide hydrolases for biohydrolysis of glycidyl derivatives.
TL;DR: Out of 270 isolated strains, four were selected based on the enantioselectivities of their epoxide hydrolases determined in biotransformation reactions, the enzyme of Aspergillus niger M200 preferentially hydrolyses (S)-tert-butyl glycidyl ether to (S-3-terT-butoxy-1,2-propanediol with a relatively high enantiomeric ratio.
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