High-yield secretory production of stable, active trypsin through engineering of the N-terminal peptide and self-degradation sites in Pichia pastoris

摘要

Graphical abstractDisplay OmittedHighlights?Introducing hydrophobic mutation and replacing propeptide improved the expression of trypsin.?An efficient signal peptide was designed inPichia pastoris.?The key autolysis residue K101 was identified from SGT trypsin.?The production of trypsin was 227.65±6.51U·mL?1and a yield of 185.71±5.68mg·L?1.AbstractStreptomyces griseustrypsin (SGT) possesses enzymatic properties similar to mammalian trypsins and has great potential applications in the leather processing,