Lisa Wenzel

Lisa Wenzel
Max Planck Institute for Dynamics of Complex Technical Systems | MPI · Group of Bioprocess Engineering (BPE)

Master of Science

About

2
Publications
178
Reads
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12
Citations
Citations since 2017
2 Research Items
12 Citations
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201720182019202020212022202301234567
201720182019202020212022202301234567
201720182019202020212022202301234567
Additional affiliations
December 2016 - February 2018
Otto-von-Guericke-Universität Magdeburg
Position
  • Master's Student
Description
  • Identifizierung von neu-synthetisierten, mikrobiellen Proteinen in Biogasanlagenproben in Abhängigkeit verschiedener Substrate mittels Klick-Chemie und Metaproteomanalyse
Education
October 2015 - February 2018
Otto-von-Guericke-Universität Magdeburg
Field of study
  • Biosystemtechnik
October 2011 - August 2015
Otto-von-Guericke-Universität Magdeburg
Field of study
  • Biosystemtechnik

Publications

Publications (2)
Article
A wide range of glycoproteins can be recombinantly expressed in aglycosylated forms in bacterial and cell-free production systems. To investigate the effect of glycosylation of these proteins on receptor binding, stability, efficacy as drugs, pharmacodynamics and pharmacokinetics, an efficient glycosylation platform is required. Here, we present a...
Article
Metaproteomics represent an important tool for the taxonomic and functional investigation of microbial communities in humans, environment, and technical applications. Due to the high complexity of the microbial communities, protein and peptide fractionation is applied to improve our characterization of taxonomic and functional composition of microb...

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Projects

Projects (2)
Project
http://www.mpi-magdeburg.mpg.de/glycobiotec2019
Project
Many viral membrane proteins are glycosylated and potential vaccine candidates. The low-cost expression of these proteins should be done in bacterial or insect cell expression systems. The glycan structure of purified recombinant membrane proteins is modified in vitro via enzymatic reactions with purified glycosyltransferases and nucleotide sugars.