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Background  Although  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 .    Results  The results indicated that the protein N-terminal sequence, the endoplasmic reticulum (ER) retention signal (KKXX) at the protein C-terminus, and the acidic stability of the protein could affect its secretion from  P. pastoris . Mutations designed based on these sequence features markedly improved secretion from  P. pastoris . In addition, we found that the secretion properties of a protein can be cumulative when all of the above strategies are combined. The final mutant (CHBD-DQR) designed by combining all of the strategies greatly improved secretion and the secreted MPH activity of CHBD-DQR was enhanced up to 195-fold compared with wild-type MPH without loss of catalytic efficiency.    Conclusions  These results demonstrate that the secretion of heterologous proteins from  P. pastoris  could be improved by combining changes in multiple protein sequence features.    Electronic supplementary material  The online version of this article (doi:10.1186/s12934-015-0315-4) contains supplementary material, which is available to authorized users.

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