A Whole-Process Visible Strategy for the Preparation of Rhizomucor miehei Lipase with Escherichia coli Secretion Expression System and the Immobilization.
Immobilization
RM lipase
Secretion expression
sfGFP
Journal
Microbial cell factories
ISSN: 1475-2859
Titre abrégé: Microb Cell Fact
Pays: England
ID NLM: 101139812
Informations de publication
Date de publication:
27 May 2024
27 May 2024
Historique:
received:
13
12
2023
accepted:
20
05
2024
medline:
28
5
2024
pubmed:
28
5
2024
entrez:
27
5
2024
Statut:
epublish
Résumé
Rhizomucor miehei (RM) lipase is a regioselective lipase widely used in food, pharmaceutical and biofuel industries. However, the high cost and low purity of the commercial RM lipase limit its industrial applications. Therefore, it is necessary to develop cost-effective strategies for large-scale preparation of this lipase. The present study explored the high-level expression of RM lipase using superfolder green fluorescent protein (sfGFP)-mediated Escherichia coli secretion system. The sfGFP The present study established a highly efficient strategy for large-scale preparation of RM lipase. This innovative technique not only provides high-purity RM lipase at a low cost but also has great potential as a platform for the preparation of lipases in the future.
Sections du résumé
BACKGROUND
BACKGROUND
Rhizomucor miehei (RM) lipase is a regioselective lipase widely used in food, pharmaceutical and biofuel industries. However, the high cost and low purity of the commercial RM lipase limit its industrial applications. Therefore, it is necessary to develop cost-effective strategies for large-scale preparation of this lipase. The present study explored the high-level expression of RM lipase using superfolder green fluorescent protein (sfGFP)-mediated Escherichia coli secretion system.
RESULTS
RESULTS
The sfGFP
CONCLUSION
CONCLUSIONS
The present study established a highly efficient strategy for large-scale preparation of RM lipase. This innovative technique not only provides high-purity RM lipase at a low cost but also has great potential as a platform for the preparation of lipases in the future.
Identifiants
pubmed: 38802857
doi: 10.1186/s12934-024-02432-y
pii: 10.1186/s12934-024-02432-y
doi:
Substances chimiques
Lipase
EC 3.1.1.3
Enzymes, Immobilized
0
Green Fluorescent Proteins
147336-22-9
Recombinant Fusion Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
155Subventions
Organisme : National Key R&D Program of China
ID : 2021YFC2100400
Organisme : Hubei Technological innovation talents program
ID : 2023DJC123
Informations de copyright
© 2024. The Author(s).
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