Identification and characterization of inulinases by bioinformatics analysis of bacterial glycoside hydrolases family 32 (GH32).
EC number
Glycoside Hydrolase 32
bacteria
inulin
inulinase
Journal
Engineering in life sciences
ISSN: 1618-0240
Titre abrégé: Eng Life Sci
Pays: Germany
ID NLM: 101193313
Informations de publication
Date de publication:
Aug 2023
Aug 2023
Historique:
received:
17
01
2023
revised:
15
05
2023
accepted:
26
06
2023
medline:
3
8
2023
pubmed:
3
8
2023
entrez:
3
8
2023
Statut:
epublish
Résumé
The glycoside hydrolase family contains enzymes that break the glycosidic bonds of carbohydrates by hydrolysis. Inulinase is one of the most important industrial enzymes in the family of Glycoside Hydrolases 32 (GH32). In this study, to identify and classify bacterial inulinases initially, 16,002 protein sequences belonging to the GH32 family were obtained using various databases. The inulin-effective enzymes (endoinulinase and exoinulinase) were identified. Eight endoinulinases (EC 3.2.1.7) and 4318 exoinulinases (EC 3.2.1.80) were found. Then, the localization of endoinulinase and exoinulinase enzymes in the cell was predicted. Among them, two extracellular endoinulinases and 1232 extracellular exoinulinases were found. The biochemical properties of 363 enzymes of the genus
Identifiants
pubmed: 37533727
doi: 10.1002/elsc.202300003
pii: ELSC1590
pmc: PMC10390659
doi:
Types de publication
Journal Article
Langues
eng
Pagination
e2300003Informations de copyright
© 2023 The Authors. Engineering in Life Sciences published by Wiley‐VCH GmbH.
Déclaration de conflit d'intérêts
The authors declare no conflicts of interest.
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