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dc.contributor.author
Mazzaferro, Laura
dc.contributor.author
Piñuel, Maria Lucrecia
dc.contributor.author
Minig, Paola Marisol
dc.contributor.author
Breccia, Javier Dario
dc.date.available
2019-08-16T14:08:14Z
dc.date.issued
2010-05
dc.identifier.citation
Mazzaferro, Laura; Piñuel, Maria Lucrecia; Minig, Paola Marisol; Breccia, Javier Dario; Extracellular monoenzyme deglycosylation system of 7-O-linked flavonoid β-rutinosides and its disaccharide transglycosylation activity from Stilbella fimetaria; Springer; Archives of Microbiology; 192; 5; 5-2010; 383-393
dc.identifier.issn
0302-8933
dc.identifier.uri
http://hdl.handle.net/11336/81705
dc.description.abstract
We screened for microorganisms able to use flavonoids as a carbon source; and one isolate, nominated Stilbella fimetaria SES201, was found to possess a disaccharide-specific hydrolase. It was a cell-bound ectoenzyme that was released to the medium during conidiogenesis. The enzyme was shown to cleave the flavonoid hesperidin (hesperetin 7-O-α-rhamnopyranosyl-β- glucopyranoside) into rutinose (α-rhamnopyranosyl-β-glucopyranose) and hesperetin. Since only intracellular traces of monoglycosidase activities (β-glucosidase, α-rhamnosidase) were produced, the disaccharidase α-rhamnosyl-β-glucosidase was the main system utilized by the microorganism for hesperidin hydrolysis. The enzyme was a glycoprotein with a molecular weight of 42224 Da and isoelectric point of 5.7. Even when maximum activity was found at 70°C, it was active at temperatures as low as 5°C, consistent with the psychrotolerant character of S. fimetaria. Substrate preference studies indicated that the enzyme exhibits high specificity toward 7-O-linked flavonoid β-rutinosides. It did not act on flavonoid 3-O-β-rutinoside and 7-O-β-neohesperidosides, neither monoglycosylated substrates. In an aqueous medium, the α-rhamnosyl-β-glucosidase was also able to transfer rutinose to other acceptors besides water, indicating its potential as biocatalyst for organic synthesis. The monoenzyme strategy of S. fimetaria SES201, as well as the enzyme substrate preference for 7-O-β-flavonoid rutinosides, is unique characteristics among the microbial flavonoid deglycosylation systems reported.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Diglycosidase
dc.subject
Glycoside Hydrolase
dc.subject
Hesperidin
dc.subject
Α-Rhamnosyl-Β- Glucosidase
dc.subject.classification
Biología Celular, Microbiología
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Extracellular monoenzyme deglycosylation system of 7-O-linked flavonoid β-rutinosides and its disaccharide transglycosylation activity from Stilbella fimetaria
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-08-14T20:13:20Z
dc.journal.volume
192
dc.journal.number
5
dc.journal.pagination
383-393
dc.journal.pais
Alemania
dc.journal.ciudad
Berlin
dc.description.fil
Fil: Mazzaferro, Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Ciencias de la Tierra y Ambientales de La Pampa. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Instituto de Ciencias de la Tierra y Ambientales de La Pampa; Argentina
dc.description.fil
Fil: Piñuel, Maria Lucrecia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Departamento de Química; Argentina
dc.description.fil
Fil: Minig, Paola Marisol. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Departamento de Química; Argentina
dc.description.fil
Fil: Breccia, Javier Dario. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Ciencias de la Tierra y Ambientales de La Pampa. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Instituto de Ciencias de la Tierra y Ambientales de La Pampa; Argentina
dc.journal.title
Archives of Microbiology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s00203-010-0567-7
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s00203-010-0567-7
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