Publications by authors named "Verena Looser"

To take full advantage of recombinant Pichia pastoris (Komagataella phaffii) as a production system for heterologous proteins, the complex protein secretory process should be understood and optimised by circumventing bottlenecks. Typically, little or no attention has been paid to the fate of newly synthesised protein inside the cell, or its passage through the secretory pathway, and only the secreted product is measured. However, the system's productivity (i.

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As Pichia pastoris (syn. Komagataella sp.) yeast can secrete pure recombinant proteins at high rates, it is a desirable production system.

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Health and safety concerns, enhanced quality criteria, and environmental sustainability, have prompted investigations into production using recombinant yeasts as a feasible alternative for isolation of proteins from natural animal or plant sources, as well as for processes utilising either mammalian cell cultures or bacterial systems. An overview of recent research papers and review articles provides readers with a comprehensive insight into the field of next-generation yeast expression systems. Major breakthroughs in recombinant yeast technology linked to Pichia pastoris are (i) the public availability of tools to generate proteins with tailored and highly homogenous N-glycan structures, similar to the forms assembled in humans, (ii) the recent accomplishment of the annotation of its genome sequence, and finally, (iii) the presence of the first few (non-glycosylated) therapeutic proteins in Pichia on the market.

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Article Synopsis
  • Matching the construction of recombinant strains with target protein characteristics can boost bioprocess efficiency and consistency.
  • Individual cell analysis of Pichia pastoris strains revealed wide variations in cell vitality (5-95%) influenced by protein production, pH levels, and high densities.
  • By excluding stress factors like low pH or high cell density, cell vitality improved, allowing for innovative bioprocess development based on individualized cell physiology rather than the traditional uniform cell population approach.
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Highly active variants of minimal hammerhead ribozymes are generated by the replacement of substantial parts of stem-loop structures with pyrene building blocks.

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