Random mutagenesis and disulfide bond formation improved thermostability in microbial transglutaminase.
Disulfide bridge
Heat resistance
Microbial transglutaminase
Random mutation
X-ray crystallography
Journal
Applied microbiology and biotechnology
ISSN: 1432-0614
Titre abrégé: Appl Microbiol Biotechnol
Pays: Germany
ID NLM: 8406612
Informations de publication
Date de publication:
01 Oct 2024
01 Oct 2024
Historique:
received:
02
07
2024
accepted:
03
09
2024
revised:
30
08
2024
medline:
3
10
2024
pubmed:
3
10
2024
entrez:
1
10
2024
Statut:
epublish
Résumé
Microbial transglutaminase (MTG) from Streptomyces mobaraensis is widely used in the food and pharmaceutical industries for cross-linking and post-translational modification of proteins. It is believed that its industrial applications could be further broadened by improving its thermostability. In our previous study, we showed that the introduction of structure-based disulfide bonds improved the thermostability of MTG, and we succeeded in obtaining a thermostable mutant, D3C/G283C, with a T
Identifiants
pubmed: 39354113
doi: 10.1007/s00253-024-13304-1
pii: 10.1007/s00253-024-13304-1
doi:
Substances chimiques
Transglutaminases
EC 2.3.2.13
Disulfides
0
Bacterial Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
478Informations de copyright
© 2024. The Author(s).
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