Biochemical properties of a Flavobacterium johnsoniae dextranase and its biotechnological potential for Streptococcus mutans biofilm degradation.
Streptococcus mutans
Dextranase
GH66
Oral biofilms
Synergy
Journal
World journal of microbiology & biotechnology
ISSN: 1573-0972
Titre abrégé: World J Microbiol Biotechnol
Pays: Germany
ID NLM: 9012472
Informations de publication
Date de publication:
13 May 2024
13 May 2024
Historique:
received:
24
12
2023
accepted:
06
05
2024
medline:
13
5
2024
pubmed:
13
5
2024
entrez:
12
5
2024
Statut:
epublish
Résumé
Cariogenic biofilms have a matrix rich in exopolysaccharides (EPS), mutans and dextrans, that contribute to caries development. Although several physical and chemical treatments can be employed to remove oral biofilms, those are only partly efficient and use of biofilm-degrading enzymes represents an exciting opportunity to improve the performance of oral hygiene products. In the present study, a member of a glycosyl hydrolase family 66 from Flavobacterium johnsoniae (FjGH66) was heterologously expressed and biochemically characterized. The recombinant FjGH66 showed a hydrolytic activity against an early EPS-containing S. mutans biofilm, and, when associated with a α-(1,3)-glucosyl hydrolase (mutanase) from GH87 family, displayed outstanding performance, removing more than 80% of the plate-adhered biofilm. The mixture containing FjGH66 and Prevotella melaninogenica GH87 α-1,3-mutanase was added to a commercial mouthwash liquid to synergistically remove the biofilm. Dental floss and polyethylene disks coated with biofilm-degrading enzymes also degraded plate-adhered biofilm with a high efficiency. The results presented in this study might be valuable for future development of novel oral hygiene products.
Identifiants
pubmed: 38736020
doi: 10.1007/s11274-024-04014-x
pii: 10.1007/s11274-024-04014-x
doi:
Substances chimiques
Dextranase
EC 3.2.1.11
Glycoside Hydrolases
EC 3.2.1.-
Recombinant Proteins
0
Bacterial Proteins
0
exo-1,3-alpha-glucanase
EC 3.2.1.84
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
201Subventions
Organisme : Fundação de Amparo à Pesquisa do Estado de São Paulo
ID : 2023/10037-0
Organisme : Fundação de Amparo à Pesquisa do Estado de São Paulo
ID : 2023/10037-0
Organisme : Fundação de Amparo à Pesquisa do Estado de São Paulo
ID : 2021/08780-1
Organisme : Conselho Nacional de Desenvolvimento Científico e Tecnológico
ID : 306852/2021-7
Informations de copyright
© 2024. The Author(s), under exclusive licence to Springer Nature B.V.
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