Alanine dehydrogenases from four different microorganisms: characterization and their application in L-alanine production.
Alanine dehydrogenase
Escherichia coli
L-alanine
Metabolic engineering
Journal
Biotechnology for biofuels and bioproducts
ISSN: 2731-3654
Titre abrégé: Biotechnol Biofuels Bioprod
Pays: England
ID NLM: 9918300888906676
Informations de publication
Date de publication:
03 Aug 2023
03 Aug 2023
Historique:
received:
16
04
2023
accepted:
20
07
2023
medline:
4
8
2023
pubmed:
4
8
2023
entrez:
3
8
2023
Statut:
epublish
Résumé
Alanine dehydrogenase (AlaDH) belongs to oxidoreductases, and it exists in several different bacteria species and plays a key role in microbial carbon and nitrogen metabolism, spore formation and photosynthesis. In addition, AlaDH can also be applied in biosynthesis of L-alanine from cheap carbon source, such as glucose. To achieve a better performance of L-alanine accumulation, system evaluation and comparison of different AlaDH with potential application value are essential. In this study, enzymatic properties of AlaDH from Bacillus subtilis 168 (BsAlaDH), Bacillus cereus (BcAlaDH), Mycobacterium smegmatis MC Enzyme assay, biochemical characterization and structure analysis of BsAlaDH, BcAlaDH, MsAlaDH and GsAlaDH were carried out. In addition, application potential of these four AlaDHs in L-alanine productions were explored. The strategies here can be applied for developing L-alanine producing strains with high titers.
Sections du résumé
BACKGROUND
BACKGROUND
Alanine dehydrogenase (AlaDH) belongs to oxidoreductases, and it exists in several different bacteria species and plays a key role in microbial carbon and nitrogen metabolism, spore formation and photosynthesis. In addition, AlaDH can also be applied in biosynthesis of L-alanine from cheap carbon source, such as glucose.
RESULTS
RESULTS
To achieve a better performance of L-alanine accumulation, system evaluation and comparison of different AlaDH with potential application value are essential. In this study, enzymatic properties of AlaDH from Bacillus subtilis 168 (BsAlaDH), Bacillus cereus (BcAlaDH), Mycobacterium smegmatis MC
CONCLUSIONS
CONCLUSIONS
Enzyme assay, biochemical characterization and structure analysis of BsAlaDH, BcAlaDH, MsAlaDH and GsAlaDH were carried out. In addition, application potential of these four AlaDHs in L-alanine productions were explored. The strategies here can be applied for developing L-alanine producing strains with high titers.
Identifiants
pubmed: 37537629
doi: 10.1186/s13068-023-02373-5
pii: 10.1186/s13068-023-02373-5
pmc: PMC10401832
doi:
Types de publication
Journal Article
Langues
eng
Pagination
123Subventions
Organisme : National Natural Science Foundation of China
ID : 32270093
Organisme : National Natural Science Foundation of China
ID : 32070111
Organisme : Key R&D Program of Shandong Province, China
ID : 2022SFGC0102
Organisme : Rizhao Science and Technology Innovation Project
ID : 2020CXZX1206
Organisme : the Science and Technology Program of the University of Jinan
ID : XKY2028
Organisme : the Higher Educational Science and Technology Program of Jinan City
ID : 2021GXRC088
Organisme : the Innovation Capability Improvement Project of technology-based medium and small enterprises in Shandong Province
ID : 2021TSGC1247
Informations de copyright
© 2023. BioMed Central Ltd., part of Springer Nature.
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