Forty years of study on the thermostable β-glycosidase from S. solfataricus: Production, biochemical characterization and biotechnological applications.
S. solfataricus
bioprocesses
broad substrate specificity
extremozymes
transglycosilation
β-glycosidase
Journal
Biotechnology and applied biochemistry
ISSN: 1470-8744
Titre abrégé: Biotechnol Appl Biochem
Pays: United States
ID NLM: 8609465
Informations de publication
Date de publication:
Jul 2020
Jul 2020
Historique:
pubmed:
6
7
2020
medline:
27
5
2021
entrez:
5
7
2020
Statut:
ppublish
Résumé
The aim of this paper is to make the point on the fortieth years study on the β-glycosidase from Sulfolobus solfataricus. This enzyme represents one of the thermophilic biocatalysts, which is more extensively studied as witnessed by the numerous literature reports available since 1980. Comprehensive biochemical studies highlighted its broad substrate specificity for β-d-galacto-, gluco-, and fuco-sides and also showed its remarkable exo-glucosidase and transglycosidase activities. The enzyme demonstrated to be active and stable over a wide range of temperature and pHs, withstanding to several drastic conditions comprising solvents and detergents. Over the years, a great deal of studies were focused on its homotetrameric tridimensional structure, elucidating several structural features involved in the enzyme stability, such as ion pairs and post-translational modifications. Several β-glycosidase mutants were produced in the years in order to understand its peculiar behavior in extreme conditions and/or to improve its functional properties. The β-glycosidase overproduction was also afforded reporting numerous studies dealing with its production in the mesophilic host Escherichia coli, Saccharomyces cerevisiae, Pichia pastoris, and Lactococcus lactis. Relevant applications in food, beverages, bioenergy, pharmaceuticals, and nutraceutical fields of this enzyme, both in free and immobilized forms, highlighted its biotechnological relevance.
Substances chimiques
Archaeal Proteins
0
Glucosidases
EC 3.2.1.-
Sulfolobus solfataricus beta-glycosidase
EC 3.2.1.-
Types de publication
Historical Article
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
602-618Informations de copyright
© 2020 International Union of Biochemistry and Molecular Biology, Inc.
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