Development of an efficient expression system for human chaperone BiP in Pichia pastoris: production optimization and functional validation.

ABSTRACT:

Background

Human BiP, or GRP78, is a molecular chaperone mainly found in the endoplasmic reticulum (ER). However, a growing amount of data also associates BiP with many distinct functions in subcellular locations outside the ER. Notably, several diseases have been BiP-related, so the protein could potentially be used for therapeutic purposes. This study aimed to optimize a high cell-density fermentation process for the production of recombinant human BiP (rhBiP) in yeast Pichia pastoris in a mineral medium.

Results

P. pastoris cells successfully synthesized and secreted full-length rhBiP protein in a complex growth medium. However, secreted rhBiP titer was considerably lower when P. pastoris was cultivated in a defined mineral basal salt medium (BSM). During rhBiP synthesis

SUBMITTER: Zitkus E 

PROVIDER: S-EPMC11917157 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature