Microbial α-L-Rhamnosidases of Glycosyl Hydrolase Families GH78 and GH106 Have Broad Substrate Specificities toward α-L-Rhamnosyl- and α-L-Mannosyl-Linkages.
glycosyl hydrolase family 106
glycosyl hydrolase family 78
α-L-mannosidase
α-L-rhamnosidase
Journal
Journal of applied glycoscience
ISSN: 1880-7291
Titre abrégé: J Appl Glycosci (1999)
Pays: Japan
ID NLM: 101167786
Informations de publication
Date de publication:
2020
2020
Historique:
received:
29
04
2020
accepted:
10
06
2020
entrez:
6
8
2021
pubmed:
7
8
2021
medline:
7
8
2021
Statut:
epublish
Résumé
α-L-Rhamnosidases (α-L-Rha-ases, EC 3.2.1.40) are glycosyl hydrolases (GHs) that hydrolyze a terminal α-linked L-rhamnose residue from a wide spectrum of substrates such as heteropolysaccharides, glycosylated proteins, and natural flavonoids. As a result, they are considered catalysts of interest for various biotechnological applications. α-L-rhamnose (6-deoxy-L-mannose) is structurally similar to the rare sugar α-L-mannose. Here we have examined whether microbial α-L-Rha-ases possess α-L-mannosidase activity by synthesizing the substrate 4-nitrophenyl α-L-mannopyranoside. Four α-L-Rha-ases from GH78 and GH106 families were expressed and purified from
Identifiants
pubmed: 34354534
doi: 10.5458/jag.jag.JAG-2020_0005
pmc: PMC8132073
doi:
Types de publication
Journal Article
Langues
eng
Pagination
87-93Informations de copyright
2020 by The Japanese Society of Applied Glycoscience.
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