gerald striedner

University Professor

University of Natural Resources and Life Sciences Vienna

Austria

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About

Gerald Striedner is a University Professor at the University of Natural Resources and Life Sciences in Vienna, Austria. His research focuses on bioprocessing, particularly the use of noncanonical amino acids and recombinant protein production in Escherichia coli. Recent articles include topics such as surrogate techno-economic modeling and the development of platforms for disulfide-bonded peptide production.

Articles (20)

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2025

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2021

Collaborators (8)

Andreas Weber

University College London

UNITED KINGDOM

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Bruce Turnbull

Professor at Faculty of Biological Sciences

University of Leeds

UNITED KINGDOM

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Irene González-Domínguez

UNITED STATES

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Prof. Jose Luis Toca-Herrera

Head / Professor

University of Natural Resources and Life Sciences

AUSTRIA

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Nico Lingg

Lecturer

Fachhochschule Campus Wien

AUSTRIA

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Benjamin Bayer

University Lecturer

Fachhochschule Campus Wien

AUSTRIA

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Winfried Römer

University of Freiburg

GERMANY

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Rainer Hahn

AUSTRIA

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gerald striedner

Research Interests

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About

Articles (20)

Scar-free tag removal by CASPON® enzyme with broad physicochemical stability in biomanufacturing – A case study of five proteins

BioProcessNexus: An open-source platform for surrogate techno economic models

Residue-Specific Incorporation of Noncanonical Amino Acids in Auxotrophic Hosts: Quo Vadis?

Site-Directed Genome Integration via Recombinase-Mediated Cassette Exchange (RMCE) in Escherichia coli

Purification of recombinantly produced somatostatin-28 comparing hydrochloric acid and polyethyleneimine as E. coli extraction aids

A production platform for disulfide-bonded peptides in the periplasm of Escherichia coli

Aligning fermentation conditions with non-canonical amino acid addition strategy is essential for Nε-((2-azidoethoxy)carbonyl)-L-lysine uptake and incorporation into the target protein

Manufacturing of the highly active thermophile PETases PHL7 and PHL7mut3 using Escherichia coli

Modifications of the 5’ region of the CASPON<sup>TM</sup> tag’s mRNA further enhance soluble recombinant protein production in Escherichia coli

RNA-seq reveals multifaceted gene expression response to Fab production in Escherichia coli fed-batch processes with particular focus on ribosome stalling

Scale‐related process heterogeneities change properties of high‐cell‐density fermentation broths demonstrated with Escherichia coli B and K‐12 strains

Recombinant Peptide Production Softens Escherichia coli Cells and Increases Their Size during C-Limited Fed-Batch Cultivation

Development and Validation of an Artificial Neural-Network-Based Optical Density Soft Sensor for a High-Throughput Fermentation System

In-Depth Characterization of a Re-Engineered Cholera Toxin Manufacturing Process Using Growth-Decoupled Production in <i>Escherichia coli</i>

Fusion Tag Design Influences Soluble Recombinant Protein Production in Escherichia coli

Bioprocess characterization of virus‐like particle production with the insect cell baculovirus expression system at nanoparticle level

Stable Sf9 cell pools as a system for rapid HIV‐1 virus‐like particle production

Digital Twin Application for Model-Based DoE to Rapidly Identify Ideal Process Conditions for Space-Time Yield Optimization

Advanced purification platform using circularly permuted caspase‐2 for affinity fusion‐tag removal to produce native fibroblast growth factor 2

Quantification of glycated IgG in CHO supernatants: A practical approach

Collaborators (8)

Andreas Weber

Bruce Turnbull

Irene González-Domínguez

Prof. Jose Luis Toca-Herrera

Nico Lingg

Benjamin Bayer

Winfried Römer

Rainer Hahn

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