Assessment of Differential Proteome Profiles for the Wild Strain Yarrowia lipolytica Po1f and Based on Its Transformant of Po1f pUV3-Op with Integrated Intracellular Phytase

A comparative assay of 2D gels of extracts from the Yarrowia lipolytica Po1f strain and its transformant of Y. lipolytica Po1f pUV3-Op with integrated intracellular histidine acid phytase from the Obesumbacterium proteus enterobacteria was performed. Upon the identification of protein profiles with MALDI-TOF mass spectrometry to determine differentially expressed proteins, seventeen protein zones were identified with some change in expression. Among the proteins with the decreased expression in the transformant of Y. lipolytica Po1f pUV3-Op, there were noted Peptidase M20, Carboxypeptidase, Proteasome assembly proteins Proteasome chaperone 2, and YALI0C01221p. The proteins with increased expression in the Po1f transformant pUV3-Op contained Nucleoside diphosphate kinase, proteins with chaperone properties of YALI0B15840p, glycerol kinase acetylated at the N-terminal edge of the molecule. Using the analysis of the proteomic profiles of two strains of the Y. lipolytica yeast we concluded that the protein composition of the transformant of Y. lipolytica Polf pUV3-Op carrying the phytase gene microencapsulated in a yeast cell possesses some metabolic features that let it, on the one hand, successfully synthesize and accumulate a heterologous functional target enzyme in the cells, and, on the other one, induce the response to endogenous stress caused by active synthesis and folding of a heterologous protein due to moderate suppression of proteasome degradation and promotion of chaperone protection.