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