Recombinants proteins for industrial uses: utilization of Pichia pastoris expression system

Abstract

The innovation in industrial process with impact in the efficient production is the major challenge for actual industry. A high numerous of enzymes are utilized in at different level of process; the search for new alternatives with better characteristic has become a field of study of great interest, the recombinant protein achievement in a different host system is an alternative widely assessed for production of this. The microorganism Pichia pastoris has been used like a successful expression system in diverse areas, improved the yield and extraction-recovery of the product expressed. The reported of diverse authors in the production of enzymes with different application in industry is varied, in this review the different industry areas and the characteristic of the enzymes produced are detailed.

Biotransformation of β‐hydroxypyruvate and glycolaldehyde to l‐erythrulose by Pichia pastoris strain GS115 overexpressing native transketolase

“…E. coli transketolase has been reported to be effective in production of L-erythrulose when in solution, 20 immobilized within a microreactor 17 and within living E. coli cells. 21 The methylotrophic budding yeast, Pichia pastoris (P. pastoris), is an established laboratory-scale recombinant protein production platform 22 and is gaining traction as an industrialscale platform for production of enzymes 23 and therapeutics. 24 Characteristically low specific yield does not prevent high volumetric yields of recombinant protein 25 as P. pastoris can grow rapidly to high biomass concentration, with 40% v/v WCW typically achieved.…”

Expression and purification of an engineered, yeast-expressedLeishmania donovaninucleoside hydrolase with immunogenic properties

“…This can obviate the need for a tag and ultimately allow for a more efficient, and thus less costly, scalable and reproducible purification process. [17][18][19] The eukaryote P. pastoris also provides a more consistent expression platform in terms of folding and posttranslational modifications with the native parasite-expressed LdNH36; however, the potential for hyperglycosylation leading to heterogeneous high-mannose glycoforms of the recombinant protein, which can adversely affect the ability to produce a consistent, well-characterized, purified protein, must be considered. 20 This concern can be mitigated using genetic engineering to modify putative N-glycosylation sites via asparagine (N)-toglutamine (Q) mutations, an approach used previously in protein vaccine development.…”

The secretome of Pichia pastoris in fed‐batch cultivations is largely independent of the carbon source but changes quantitatively over cultivation time

“…Komagataella spp .) is a methylotrophic yeast, which is commonly used as host platform for the production of recombinant secretory proteins of pharmaceutical (Weinacker, et al , ) and industrial interest (Rabert, et al , ; Love, et al , ; Zhu, et al , ). P. pastoris has been reclassified to the genus Komagataella in the recent years, which currently consists of seven species (including K. pastoris and K. phaffii ).…”