Signal peptides are essential for the secretion of recombinant proteins using Komagataella phaffii. The N-terminal signal peptide is removed by proteases during the translocation process. However, this processing is not always complete, resulting in an N-terminal extension which is problematic for some proteins. In this chapter, we present a straightforward approach to evaluate signal peptide processing by a high-throughput solid-phase agar plate assay.

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Lytic Polysaccharide Monooxygenases as Reporters for Signal Peptide Evaluation in Pichia pastoris

  • Andrea K. Hönikl,
  • Lukas Rieder

摘要

Signal peptides are essential for the secretion of recombinant proteins using Komagataella phaffii. The N-terminal signal peptide is removed by proteases during the translocation process. However, this processing is not always complete, resulting in an N-terminal extension which is problematic for some proteins. In this chapter, we present a straightforward approach to evaluate signal peptide processing by a high-throughput solid-phase agar plate assay.