Výsledky vyhledávání - "Waander Riethorst"

Akademický článek

An Industrial View on Enzymes for the Cleavage of Cephalosporin C

Publikováno v: CHIMIA, Vol 53, Iss 12 (1999)

The enzymatic cleavage of cephalosporin C (CephC) into 7-aminocephalosporanic acid (7-ACA) and deacetyl-7-aminocephalosporanic acid (HACA), both key intermediates for cephalosporin antibiotics, has now been commercialized on an industrial scale. This

Externí odkaz: https://doaj.org/article/dd826b394ae647838d194eb6fb4b5cc9

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Dynamic Kinetic Resolution of 2-Phenylpropanal Derivatives to Yield β-Chiral Primary Amines via Bioamination

Autor: Christine S. Fuchs, Wolfgang Kroutil, Joost N. H. Reek, Ferdinand Zepeck, Robert C. Simon, Tatiana Besset, Manuel Hollauf, Maximilian Meissner, Waander Riethorst

Publikováno v: Advanced Synthesis and Catalysis
Advanced Synthesis and Catalysis, Wiley-VCH Verlag, 2014, 356 (10), pp.2257-2265. ⟨10.1002/adsc.201400217⟩
Advanced Synthesis & Catalysis, 356(10), 2257-2265. Wiley-VCH Verlag

The amination of racemic alpha-chiral aldehydes, 2-phenylpropanal derivatives, was investigated employing omega-transaminases. By medium and substrate engineering the optical purity of the resulting β-chiral chiral amine could be enhanced to reach o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::702ea1eacc4c67c023ca70d4deafc38b
https://dare.uva.nl/personal/pure/en/publications/dynamic-kinetic-resolution-of-2phenylpropanal-derivatives-to-yield-chiral-primary-amines-via-bioamination(6f7d27b4-c82b-4cdf-a3dd-3301c2e08aa6).html

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Intraparticle concentration gradients for substrate and acidic product in immobilized cephalosporin C amidase and their dependencies on carrier characteristics and reaction parameters

Autor: Bernd Nidetzky, Torsten Mayr, Caterina Boniello, Burghard Koenig, Ingo Klimant, Waander Riethorst

Publikováno v: Biotechnology and Bioengineering. 106:528-540

Cephalosporin C amidase was covalently attached using a protein loading of 7.0-200 mg protein/g dry carrier on four epoxy-activated Sepabeads differing in particle size and pore diameter. Initial-rate kinetic analysis showed that for Sepabeads with s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::637e93e9f4901e8e5bc8480f25c79306
https://doi.org/10.1002/bit.22694

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Study of the thermal stability of D-amino acid oxidase fromTrigonopsis variabilisreveals enzyme inactivation via multiple steps

Autor: Pavel Ačai, Waander Riethorst, Bernd Nidetzky, Anita Slavica

Publikováno v: Biocatalysis and Biotransformation. 24:426-436

The thermal stability of a highly purified preparation of D-amino acid oxidase from Trigonopsis variabilis (TvDAO), which does not show microheterogeneity due to the partial oxidation of Cys-108, was studied based on dependence of temperature (20–6

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4bb99c631e26f3ffac29b282dbc33a45
https://doi.org/10.1080/10242420601034025

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Reaction of Trigonopsis variabilis d-amino acid oxidase with 2,6-dichloroindophenol: kinetic characterisation and development of an oxygen-independent assay of the enzyme activity

Autor: Bernd Nidetzky, Anita Slavica, Waander Riethorst, Christian Trampitsch

Publikováno v: Journal of Molecular Catalysis B: Enzymatic. 32:271-278

2,6-Dichloroindophenol (DCIP) is shown to be utilised efficiently as electron acceptor replacing dioxygen in the reaction of Trigonopsis variabilis d -amino acid oxidase (TvDAO) with d -methionine as the substrate. The specificity constant for DCIP r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::553e12dc499587a76bd4da15caa31638
https://doi.org/10.1016/j.molcatb.2004.12.011

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Synthesis of (R)- or (S)-valinol using ω-transaminases in aqueous and organic media

Autor: Christine S. Fuchs, Waander Riethorst, Robert C. Simon, Wolfgang Kroutil, Ferdinand Zepeck

Publikováno v: Bioorganicmedicinal chemistry. 22(20)

Valinol is part of numerous pharmaceuticals and has various other important applications. Optically pure valinol (ee >99%) was prepared employing different ω-transaminases from the corresponding prochiral hydroxy ketone. By the choice of the enzyme

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de2eb13f0173eb7baa2a344f25a9dc54
https://pubmed.ncbi.nlm.nih.gov/24951100

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