Combined mass mapping and biochemical characterization of grape beta-glycosidase-enriched extract.
Protein J
; 27(4): 258-66, 2008 Jun.
Article
em En
| MEDLINE
| ID: mdl-18459038
ABSTRACT
A beta-glucosidase enzyme activity was enriched from skins of ripe grape berry by cell wall fractionation, hydrophobic interaction and cation-exchange chromatographies. This enriched enzyme extract contained several beta-glycosidase activities hydrolyzing a wide range of synthetic and natural monoglycosides and diglycosides, as well as a beta-fructosidase activity. The enzyme extract was further characterized by two-dimensional gel electrophoresis coupled to peptide mass fingerprinting of eight spots using MALDI-TOF mass spectrometry. No beta-glucosidase but a beta-fructosidase associated to the relevant spot at 66 kDa/pI 5.1 was identified. Taken together all results issued from the biochemical characterization, the substrate specificity and the mass spectrometry-based identification of this enriched enzyme extract, we propose that this protein could be a specific beta-fructosidase isoform associated with a broad spectrum of beta-glycosidase activities in grape berry skin and involved in cell wall modifications which occur during the ripening-induced thickness of the grape.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Vitis
/
Beta-Frutofuranosidase
Idioma:
En
Ano de publicação:
2008
Tipo de documento:
Article