Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Petra Staudigl"'
Publikováno v:
Biomolecules, Vol 3, Iss 3, Pp 535-552 (2013)
Pyranose dehydrogenase (PDH) is a flavin-dependent sugar oxidoreductase that is limited to a rather small group of litter-degrading basidiomycetes. The enzyme is unable to utilize oxygen as an electron acceptor, using substituted benzoquinones and (o
Externí odkaz:
https://doaj.org/article/228d3b9cae21483c9bbe05260195735d
Autor:
Iris Krondorfer, Katharina Lipp, Dagmar Brugger, Petra Staudigl, Christoph Sygmund, Dietmar Haltrich, Clemens K Peterbauer
Publikováno v:
PLoS ONE, Vol 9, Iss 3, p e91145 (2014)
Pyranose dehydrogenase (PDH), a member of the GMC family of flavoproteins, shows a very broad sugar substrate specificity but is limited to a narrow range of electron acceptors and reacts extremely slowly with dioxygen as acceptor. The use of substit
Externí odkaz:
https://doaj.org/article/5900f04c2c2548ffa3ba856c3907b1fa
Autor:
Regina Paukner, Petra Staudigl, Withu Choosri, Christoph Sygmund, Petr Halada, Dietmar Haltrich, Christian Leitner
Publikováno v:
PLoS ONE, Vol 9, Iss 6, p e100116 (2014)
A gene coding for galactose 6-oxidase from Fusarium oxysporum G12 was cloned together with its native preprosequence and a C-terminal His-tag, and successfully expressed both in Escherichia coli and Pichia pastoris. The enzyme was subsequently purifi
Externí odkaz:
https://doaj.org/article/ed887376952544538ef504d4d7709ac0
Publikováno v:
Biomolecules
Biomolecules; Volume 3; Issue 3; Pages: 535-552
Biomolecules, Vol 3, Iss 3, Pp 535-552 (2013)
Biomolecules; Volume 3; Issue 3; Pages: 535-552
Biomolecules, Vol 3, Iss 3, Pp 535-552 (2013)
Pyranose dehydrogenase (PDH) is a flavin-dependent sugar oxidoreductase that is limited to a rather small group of litter-degrading basidiomycetes. The enzyme is unable to utilize oxygen as an electron acceptor, using substituted benzoquinones and (o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f66bdfa7a22f6b14a817e83ba16738fa
http://europepmc.org/articles/PMC4030953
http://europepmc.org/articles/PMC4030953
Publikováno v:
Journal of Agricultural and Food Chemistry
The L-arabinose isomerase (L-AI) and the D-xylose isomerase (D-XI) encoding genes from Lactobacillus reuteri (DSMZ 17509) were cloned and overexpressed in Escherichia coli BL21 (DE3). The proteins were purified to homogeneity by one-step affinity chr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9b8f4d752f23d09919c26c30ae25f6ee
https://pubmed.ncbi.nlm.nih.gov/24443973
https://pubmed.ncbi.nlm.nih.gov/24443973
Autor:
Regina Paukner, Petra Staudigl, Withu Choosri, Christoph Sygmund, Petr Halada, Dietmar Haltrich, Christian Leitner
Publikováno v:
PLoS ONE
PLoS ONE, Vol 9, Iss 6, p e100116 (2014)
PLoS ONE, Vol 9, Iss 6, p e100116 (2014)
A gene coding for galactose 6-oxidase from Fusarium oxysporum G12 was cloned together with its native preprosequence and a C-terminal His-tag, and successfully expressed both in Escherichia coli and Pichia pastoris. The enzyme was subsequently purifi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::24876095819611394c70d2ec108a755c
https://pubmed.ncbi.nlm.nih.gov/24967652
https://pubmed.ncbi.nlm.nih.gov/24967652
Autor:
Miriam Klausberger, Lo Gorton, Roland Ludwig, Petra Staudigl, Nikos Pinotsis, Kristina Djinović-Carugo, Christoph Sygmund, Dietmar Haltrich
Publikováno v:
Microbial Cell Factories, Vol 10, Iss 1, p 106 (2011)
Microbial Cell Factories
Microbial Cell Factories
Background FAD dependent glucose dehydrogenase (GDH) currently raises enormous interest in the field of glucose biosensors. Due to its superior properties such as high turnover rate, substrate specificity and oxygen independence, GDH makes its way in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e19f1023628397c77bf6e5a4eb29a0e3
http://www.microbialcellfactories.com/content/10/1/106
http://www.microbialcellfactories.com/content/10/1/106