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

ABSTRACT:

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

SUBMITTER: Wang P 

PROVIDER: S-EPMC4551668 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature