Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Jan Brummund"'
Publikováno v:
Organic Process Research & Development. 26:2021-2029
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7dcc1b8e884e4308007dba53d3d9bf7f
https://doi.org/10.1021/acs.oprd.1c00415
https://doi.org/10.1021/acs.oprd.1c00415
Publikováno v:
Applied Biocatalysis. :281-331
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::25b414bc82c5a811afa5713c97b8d64f
https://doi.org/10.1002/9781119487043.ch8
https://doi.org/10.1002/9781119487043.ch8
Publikováno v:
ACS Sustainable Chemistry & Engineering
Fe(II)- and α-ketoglutarate dependent dioxygenases have emerged as important catalysts for the preparation of non-natural amino acids. The stoichiometric supply of the cosubstrate α-ketoglutarate (αKG) is an important cost factor. A combination of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9bd0cdd88b5994498b58695ca2d3452
https://doi.org/10.1021/acssuschemeng.0c01122
https://doi.org/10.1021/acssuschemeng.0c01122
Publikováno v:
Recercat. Dipósit de la Recerca de Catalunya
instname
Digital.CSIC. Repositorio Institucional del CSIC
Recercat: Dipósit de la Recerca de Catalunya
Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Dipòsit Digital de Documents de la UAB
Universitat Autònoma de Barcelona
instname
Digital.CSIC. Repositorio Institucional del CSIC
Recercat: Dipósit de la Recerca de Catalunya
Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Dipòsit Digital de Documents de la UAB
Universitat Autònoma de Barcelona
Optimization and scaling up of the Baeyer-Villiger oxidation of 3,3,5-trimethyl-cyclohexanone to trimethyl-ϵ-caprolactones (CHLs) were studied to demonstrate this technology on a 100 L pilot plant scale. The reaction was catalyzed by a cyclohexanone
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62cc2ab64e9176bd6128cbe064adb2d5
http://hdl.handle.net/2072/438636
http://hdl.handle.net/2072/438636
Autor:
Jan Brummund, Andreas Vogel, Sebastian Bartsch, Harrie Straatman, Sabrina Köpke, Martin Schürmann
Publikováno v:
Biotechnology journal. 15(11)
Alcohol dehydrogenases (ADH) are widely used to enantioselectively reduce ketones to chiral alcohols, but their application in industrial scale oxidations is rare. Reasons are the need for an NAD(P)+ cofactor regeneration system, often low performanc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c9c3f62049bac7bb825535e5e72b866
https://pubmed.ncbi.nlm.nih.gov/32846049
https://pubmed.ncbi.nlm.nih.gov/32846049
Autor:
Peter W. Sutton, Jan Brummund, Gregorio Álvaro, Harrie Straatman, Marina Guillén, Miquel García-Bofill, Martin Schürmann
Publikováno v:
Applied Catalysis A: General. 610:117934
Vanilla is the second most expensive spice in the world. This issue triggered the necessity to obtain its flavour compound, vanillin, by alternative methods, most of which have focused on biosynthesis since it can be labelled as “natural” and sol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::854efcdceace1c435829c658a4d26aa1
https://doi.org/10.1016/j.apcata.2020.117934
https://doi.org/10.1016/j.apcata.2020.117934
Autor:
Iwona Kaluzna, Jan Brummund, Daniel Mink, Andreas Liese, Monika Müller, Lutz Hilterhaus, Thomas Schmitges
Publikováno v:
Journal of Biotechnology. 233:143-150
Cytochrome P450 monooxygenases are a unique family of enzymes that are able to catalyze regio- and stereospecific oxidations for a broad substrate range. However, due to limited enzyme activities and stabilities, hydrophobicity of substrates, as well
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a4326c1c77cb6dcbe1bfaaf5c64dbec
https://doi.org/10.1016/j.jbiotec.2016.07.002
https://doi.org/10.1016/j.jbiotec.2016.07.002
Publikováno v:
Organic Process Research & Development. 19:1590-1595
Alcohol dehydrogenases are able to catalyze the conversion of alcohols to aldehydes or ketones, simultaneously reducing the cofactor NAD+ or NADP+ to NAD(P)H. Because of the high costs of these pyridine cofactors, in situ cofactor regeneration is req
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dcd600a3aef5f31c5999a2670ac6d255
https://doi.org/10.1021/op500307e
https://doi.org/10.1021/op500307e
Publikováno v:
Dipòsit Digital de Documents de la UAB
Universitat Autònoma de Barcelona
Recercat. Dipósit de la Recerca de Catalunya
instname
Recercat: Dipósit de la Recerca de Catalunya
Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Digital.CSIC. Repositorio Institucional del CSIC
Universitat Autònoma de Barcelona
Recercat. Dipósit de la Recerca de Catalunya
instname
Recercat: Dipósit de la Recerca de Catalunya
Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Digital.CSIC. Repositorio Institucional del CSIC
An often associated drawback with Baeyer-Villiger monooxygenases, is its poor operational stability. Furthermore, these biocatalysts frequently suffer from substrate/product inhibition. In this work, a thermostable cyclohexanone monooxygenase (TmCHMO
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0170ed3a853860de5c33145f0a27a731
https://doi.org/10.1016/j.apcata.2019.117187
https://doi.org/10.1016/j.apcata.2019.117187
Publikováno v:
Biotechnology and bioengineering. 108(11)
Solvent free biotransformation of polyglycerol-3 and lauric acid yields polyglycerol-3-laurate and water. This conversion can be catalyzed by Novozym 435. However, the performance is limited by the viscosity of polyglycerol as well as of polyglycerol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45bfdbc22aaf8c29d91bcfa80ef25ee6
https://pubmed.ncbi.nlm.nih.gov/21656709
https://pubmed.ncbi.nlm.nih.gov/21656709