Enhanced secretion of a methyl parathion hydrolase in Pichia pastoris using a combinational strategy

摘要

BackgroundAlthough Pichia pastoris has been successfully used to produce various recombinant heterologous proteins, the efficiency varies. In this study, we used methyl parathion hydrolase (MPH) from Ochrobactrum sp. M231 as an example to study the effect of protein amino acid sequence on secretion from P. pastoris.