Pichia pastoris: A highly successful expression system for optimal synthesis of heterologous proteins.
Pichia pastoris
expression system
optimization
recombinant proteins
subunit vaccines
Journal
Journal of cellular physiology
ISSN: 1097-4652
Titre abrégé: J Cell Physiol
Pays: United States
ID NLM: 0050222
Informations de publication
Date de publication:
09 2020
09 2020
Historique:
received:
04
06
2019
accepted:
09
01
2020
pubmed:
15
2
2020
medline:
12
3
2021
entrez:
15
2
2020
Statut:
ppublish
Résumé
One of the most important branches of genetic engineering is the expression of recombinant proteins using biological expression systems. Nowadays, different expression systems are used for the production of recombinant proteins including bacteria, yeasts, molds, mammals, plants, and insects. Yeast expression systems such as Saccharomyces cerevisiae (S. cerevisiae) and Pichia pastoris (P. pastoris) are more popular. P. pastoris expression system is one of the most popular and standard tools for the production of recombinant protein in molecular biology. Overall, the benefits of protein production by P. pastoris system include appropriate folding (in the endoplasmic reticulum) and secretion (by Kex2 as signal peptidase) of recombinant proteins to the external environment of the cell. Moreover, in the P. pastoris expression system due to its limited production of endogenous secretory proteins, the purification of recombinant protein is easy. It is also considered a unique host for the expression of subunit vaccines which could significantly affect the growing market of medical biotechnology. Although P. pastoris expression systems are impressive and easy to use with well-defined process protocols, some degree of process optimization is required to achieve maximum production of the target proteins. Methanol and sorbitol concentration, Mut forms, temperature and incubation time have to be adjusted to obtain optimal conditions, which might vary among different strains and externally expressed protein. Eventually, optimal conditions for the production of a recombinant protein in P. pastoris expression system differ according to the target protein.
Identifiants
pubmed: 32057111
doi: 10.1002/jcp.29583
pmc: PMC7228273
doi:
Substances chimiques
Fungal Proteins
0
Recombinant Proteins
0
Saccharomyces cerevisiae Proteins
0
Proprotein Convertases
EC 3.4.21.-
KEX2 protein, S cerevisiae
EC 3.4.21.61
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
5867-5881Informations de copyright
© 2020 Wiley Periodicals, Inc.
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