Characterization and stabilization of the α-L-fucosidase set from Lacticaseibacillus rhamnosus INIA P603.
2′-Fucosyllactose
AlfB
Lacticaseibacillus rhamnosus
Lactose transfucosylation
α-L-Fucosidase
Journal
Applied microbiology and biotechnology
ISSN: 1432-0614
Titre abrégé: Appl Microbiol Biotechnol
Pays: Germany
ID NLM: 8406612
Informations de publication
Date de publication:
Dec 2022
Dec 2022
Historique:
received:
16
08
2022
accepted:
23
10
2022
revised:
20
10
2022
pubmed:
13
11
2022
medline:
15
12
2022
entrez:
12
11
2022
Statut:
ppublish
Résumé
This study describes the molecular identification, biochemical characterization, and stabilization of three recombinant AlfA, AlfB, and AlfC fucosidases from Lacticaseibacillus rhamnosus INIA P603. Even though previous studies revealed the presence of fucosidase activity in L. rhamnosus extracts, the identification of the fucosidases, their physicochemical properties, and the substrate spectrum remained unknown. Although the presence of alfB is not common in strains of L. rhamnosus, fucosidases from L. rhamnosus INIA P603 were selected because this strain exhibited higher fucosidase activity in culture and the complete set of fucosidases. A high yield of purified recombinant AlfA, AlfB, and AlfC fucosidases was obtained (8, 12, and 18 mg, respectively). AlfA, AlfB, and AlfC showed their optimal activities at pH 5.0 and 4.0 at 60 °C, 40 °C, and 50 °C, respectively. Unlike 3-fucosyllactose, all three recombinant fucosidases were able to hydrolyze 2'-fucosyllactose (2'-FL), and their activities were improved through their immobilization on agarose supports. Nevertheless, immobilized AlfB exhibited the highest hydrolysis, releasing 39.6 µmol of fucose mg enzyme
Identifiants
pubmed: 36370158
doi: 10.1007/s00253-022-12262-w
pii: 10.1007/s00253-022-12262-w
doi:
Substances chimiques
alpha-L-Fucosidase
EC 3.2.1.51
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
8067-8077Subventions
Organisme : Ministerio de Ciencia e Innovación
ID : PID2020-119630RB-I00
Organisme : Ministerio de Ciencia e Innovación
ID : RYC2019-026368-I
Informations de copyright
© 2022. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.
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