Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Sebastian, Bormann"'
Publikováno v:
MicrobiologyOpen, Vol 10, Iss 6, Pp n/a-n/a (2021)
Abstract The filamentous fungus Magnaporthe oryzae has the potential to be developed as an alternative platform organism for the heterologous production of industrially important enzymes. M. oryzae is easy to handle, fast‐growing and unlike yeast,
Externí odkaz:
https://doaj.org/article/28d8ca00166e404ebae781f13f396c42
Autor:
Sebastian Bormann, Harald Kellner, Johanna Hermes, Robert Herzog, René Ullrich, Christiane Liers, Roland Ulber, Martin Hofrichter, Dirk Holtmann
Publikováno v:
Antioxidants, Vol 11, Iss 2, p 223 (2022)
Unspecific peroxygenases (UPOs) catalyze the selective transfer of single oxygen atoms from peroxides to a broad range of substrates such as un-activated hydrocarbons. Since specific oxyfunctionalizations are among the most-desired reactions in synth
Externí odkaz:
https://doaj.org/article/1bff03c566074b75a0007d89c5039128
Autor:
Frederic Perz, Paul Bubenheim, Miguel Alcalde, Roland Ulber, Andreas Liese, Sebastian Bormann, Dirk Holtmann, Frank Hollmann
Publikováno v:
ChemCatChem 14 (12): 3666-3669 (2020)
ChemCatChem, 12(14)
ChemCatChem, 12(14)
Unspecific peroxygenases have recently gained significant interest due to their ability to catalyse the hydroxylation of non-activated C−H bonds using only hydrogen peroxide as a co-substrate. However, the development of preparative processes has s
Publikováno v:
MicrobiologyOpen, Vol 10, Iss 6, Pp n/a-n/a (2021)
MicrobiologyOpen
MicrobiologyOpen
The filamentous fungus Magnaporthe oryzae has the potential to be developed as an alternative platform organism for the heterologous production of industrially important enzymes. M. oryzae is easy to handle, fast‐growing and unlike yeast, posttrans
Autor:
Jonathan Z. Bloh, Sabrina Schneider, Roland Ulber, Antje C. Spiess, Dominik Hertweck, Dirk Holtmann, Sebastian Bormann
Publikováno v:
Biotechnology and bioengineeringREFERENCES. 118(1)
Unspecific peroxygenases have attracted interest due to their ability to catalyze the oxygenation of various types of C-H bonds using only hydrogen peroxide as a cosubstrate. Due to the instability of these enzymes at even low hydrogen peroxide conce
Autor:
Max Steinhagen, Angelika E.W. Horst, Sebastian Bormann, Anja Drews, Janine Meyer, Dirk Holtmann, Roland Ludwig, Marion B. Ansorge-Schumacher
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 133:S137-S142
The unspecific peroxygenase from the fungus Agrocybe aegerita (AaeUPO) is an up-and-coming biocatalyst that is able to perform specific oxyfunctionalizations of various substrates. Due to inactivation at excess concentrations of its co-substrate H2O2
Autor:
Zachary C. Baer, Adam Grippo, Douglas S. Clark, Sebastian Bormann, Sanil Sreekumar, Harvey W. Blanch, F. Dean Toste
Publikováno v:
Biotechnology and Bioengineering. 113:2079-2087
The fermentation of simple sugars to ethanol has been the most successful biofuel process to displace fossil fuel consumption worldwide thus far. However, the physical properties of ethanol and automotive components limit its application in most case
Autor:
Frank Hollmann, H.-G. Hennemann, Andreas Liese, Paul Bubenheim, Sebastian Bormann, F. Nissen, F. Perz, Dirk Holtmann
Publikováno v:
Chemie Ingenieur Technik. 92:1211-1211
Publikováno v:
Molecular Catalysis. 492:110999
Unspecific peroxygenases (UPOs) catalyze oxidation and oxygenation reactions using only hydrogen peroxide as a co-substrate. Especially their ability to oxygenate unactivated C–H bonds has attracted interest in their synthetic application. Due to t
Autor:
Wuyuan Zhang, Sebastian Bormann, Sabrina R. de Boer, Jonathan Z. Bloh, Dirk Holtmann, Frank Hollmann, Miguel Alcalde, Bastien O. Burek, Florian Tieves, Detlef W. Bahnemann, Morten M. C. H. van Schie
Publikováno v:
ChemCatChem, 11(13)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Digital.CSIC. Repositorio Institucional del CSIC
instname
[EN] Photoenzymatic cascades can be used for selective oxygenation of C−H-Bonds under mild conditions circumventing the hydrogen peroxide mediated peroxygenase inactivation via in situ HO generation. Here, we report the “on demand” production o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::029c2e59d5a4737460d6872aeda68f16
http://resolver.tudelft.nl/uuid:7da96064-c9fe-40b0-b97b-9e72f4707759
http://resolver.tudelft.nl/uuid:7da96064-c9fe-40b0-b97b-9e72f4707759