BACKGROUND Pichia pastoris is one of the most important cell factories for production of industrial enzymes and heterogenous proteins. The genome-scale metabolic model of high quality is crucial for comprehensive understanding of the P. pastoris metabolism. METHODS In this paper, we upgraded P. pastoris genome-scale metabolic model based on the combination of latest genome annotations and lit...

BACKGROUND: Pichia pastoris is a well established yeast host for heterologous protein expression, however, the physiological and genetic information about this yeast remains scanty. The lack of a published genome sequence renders DNA arrays unavailable, thereby hampering more global investigations of P. pastoris from the beginning. Here, we examine the suitability of Saccharomyces cerevisiae DN...

Pichia pastoris is commonly used for the production of recombinant proteins due to its preferential secretion of recombinant proteins, resulting in lower production costs and increased yields of target proteins. However, not all recombinant proteins can be successfully secreted in P. pastoris. A computational method that predicts the likelihood of a protein being secreted into the supernatant w...

background: leishmania major lmsti1 is a conserved protein among different species of leishmania, and expressed in both amastigote and promastigote forms of l. major life cycle. it has previously been expressed in bacterial systems. m aterials and methods: to express lmsti1 in the methylotrophic yeast         pichia pastoris ( p. pastoris ), the shuttle vector ppicza containing gene lmsti1 was ...

The gene encoding mature enterocin P (EntP), an antimicrobial peptide from Enterococcus faecium P13, was cloned into the pPICZalphaA expression vector to generate plasmid pJC31. This plasmid was integrated into the genome of P. pastoris X-33, and EntP was heterologously secreted from the recombinant P. pastoris X-33t1 derivative at a higher production and antagonistic activity than from E. faec...

Pichia pastoris is a widely used host organism for the recombinant production of proteins. It is attracting increasing interest for the production of biopharmaceuticals, due to its capability of performing posttranslational modifications. Traditionally, production processes with P. pastoris describe fed-batch processes based on feed forward regimes with a constant specific growth rate. However,...

Pichia pastoris is commonly used to express and secrete target proteins, although not all recombinant proteins can be successfully produced. In this study, we used methyl parathion hydrolase (MPH) from Ochrobactrum sp. M231 as a model to study the importance of the N-terminus of the protein for its secretion. While MPH can be efficiently expressed intracellularly in P. pastoris, it is not secre...

Gene replacement in yeast is often accomplished by using a counterselectable marker such as URA3. Although ura3 strains of Pichia pastoris have been generated, these strains are inconvenient to work with because they grow slowly, even in the presence of uracil. To overcome this limitation, we have developed an alternative counterselectable marker that can be used in any P. pastoris strain. This...

results escherichia coli phytase was expressed in p. pastoris under different cultivation conditions (post-induction temperature, methanol concentration, and post-induction ph). the optimized conditions by rsm using face centered central composite design were 1% (v/v) methanol, ph = 5.8, and 24.5°c. under the optimized conditions, appa was successfully expressed in p. pastoris and the maximum p...

A gene homologous to Saccharomyces cerevisiae PMR1 has been cloned in the methylotrophic yeast Pichia pastoris. The entire P. pastoris PMR1 gene (PpPMR1) codes a protein of 924 amino acids. Sequence analysis of the PpPMR1 cDNA and the genomic DNA revealed that there is no intron in the coding region. The putative gene product contains all of the conserved regions observed in P-type ATPases and ...