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An evaluation of genetically encoded FRET-based biosensors for quantitative metabolite analyses in vivo

Autor: Victoria Steffen, T. Kubitzki, Wolfgang Wiechert, Anna Baierl, Martina Pohl, Roland Moussa

Publikováno v: Journal of Biotechnology. 191:250-259

A broad range of genetically-encoded fluorescence biosensors has been developed, allowing the detection of signaling intermediates and metabolites in real time. Many of these biosensors are based on Foerster Resonance Energy Transfer (FRET). The two

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5524f82759cfb463c236a02fb131f58
https://doi.org/10.1016/j.jbiotec.2014.07.007

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An Efficient Route to Both Enantiomers of allo-Threonine by Simultaneous Amino Acid Racemase-Catalyzed Isomerization of Threonine and Crystallization

Autor: Stephan Lütz, Susanne Wilhelm, Martina Pohl, Ursula Mackfeld, T. Kubitzki, Kerstin Würges, Wolfgang Wiechert

Publikováno v: Advanced Synthesis & Catalysis. 353:2431-2438

We present an efficient method for the production of D- and L-allo-threonine (allo-Thr) with very high purity by enzymatic isomerization of L- or D-threonine (Thr) and simultaneous crystallization. Isomerization of Thr to allo-Thr is catalyzed by a p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::17e9760af8926c06cf10fe657f8f07de
https://doi.org/10.1002/adsc.201100051

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Application of immobilized bovine enterokinase in repetitive fusion protein cleavage for the production of MUC1

Autor: T. Kubitzki, Stephan Lütz, Thomas Noll, Marco Oldiges, D. Minör, Ursula Mackfeld

Publikováno v: Biotechnology Journal
Biotechnology Journal, Wiley-VCH Verlag, 2009, 4 (11), pp.1610. ⟨10.1002/biot.200900049⟩

International audience; Bovine enterokinase is a serine protease catalyzing the hydrolysis of peptide bonds, which plays a key role in mammalian metabolism. Because of its high specificity towards the amino acid sequence (Asp)4-Lys, enterokinase is a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7891ceaa85c34c5ef5636f3ef387336d
https://hal.archives-ouvertes.fr/hal-00508906

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Immobilisation of bovine enterokinase and application of the immobilised enzyme in fusion protein cleavage

Autor: Stephan Lütz, Thomas Noll, T. Kubitzki

Publikováno v: Bioprocess and biosystems engineering. 31(3)

Two immobilisation methods for enterokinase were developed, which yielded high remaining activities for the cleavage of the fusion protein MUC1-IgG Fc. Different carrier materials were compared regarding remaining enzyme activity and storage stabilit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::652bdc816d5f8d4fd473edbb63b2d198
https://pubmed.ncbi.nlm.nih.gov/18183425

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