Combinatorial optimization of the hybrid cellulase complex structure designed from modular libraries.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
28 Sep 2024
28 Sep 2024
Historique:
received:
08
11
2023
accepted:
18
09
2024
medline:
29
9
2024
pubmed:
29
9
2024
entrez:
28
9
2024
Statut:
epublish
Résumé
Cellulase selectively recognizes cellulose surfaces and cleaves their β-1,4-glycosidic bonds. Combining hydrolysis using cellulase and fermentation can produce alternative fuels and chemical products. However, anaerobic bacteria produce only low levels of highly active cellulase complexes so-called cellulosomes. Therefore, we designed hybrid cellulase complexes from 49 biotinylated catalytic domain (CD) and 30 biotinylated cellulose-binding domain (CBD) libraries on streptavidin-conjugated nanoparticles to enhance cellulose hydrolysis by mimicking the cellulosome structure. The hybrid cellulase complex, incorporating both native CD and CBD, significantly improved reducing sugar production from cellulose compared to free native modular enzymes. The optimal CBD for each hybrid cellulase complex differed from that of the native enzyme. The most effective hybrid cellulase complex was observed with the combination of CD
Identifiants
pubmed: 39342015
doi: 10.1038/s41598-024-73541-2
pii: 10.1038/s41598-024-73541-2
doi:
Substances chimiques
Cellulase
EC 3.2.1.4
Cellulose
9004-34-6
Bacterial Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
22429Subventions
Organisme : MEXT | Japan Society for the Promotion of Science (JSPS)
ID : 22K18911
Organisme : MEXT | Japan Society for the Promotion of Science (JSPS)
ID : 16H04570
Organisme : MEXT | Japan Science and Technology Agency (JST)
ID : Advanced Low Carbon Technology Research and Development Program Grant
Informations de copyright
© 2024. The Author(s).
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