Recombinant Protein Production and Purification Using Eukaryotic Cell Factories.


Journal

Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969

Informations de publication

Date de publication:
2021
Historique:
entrez: 19 5 2021
pubmed: 20 5 2021
medline: 23 6 2021
Statut: ppublish

Résumé

Cloning proteins enables their production and characterization for further studies. This requires inserting the gene of the studied protein to be inserted in a vector, which then will be transformed to the host cell used as "factory." Consequently, the "biomass" of host cells will be produced using bioreactors. Here we describe the production of Rhizomucor miehei lipase (RML) by cloning the corresponding genes in the yeast Pichia pastoris. This enzyme is used as a biocatalyst for biofuel production. The successfully produced recombinant proteins are then purified using ion exchange chromatography.

Identifiants

pubmed: 34009593
doi: 10.1007/978-1-0716-1323-8_15
doi:

Substances chimiques

Recombinant Proteins 0
Lipase EC 3.1.1.3

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

215-228

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Auteurs

Asmaa Missoum (A)

Paris-Saclay University, Orsay, France. amissoum93@gmail.com.

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