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http://hdl.handle.net/10261/24934
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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Linde, Dolores | - |
dc.contributor.author | Macías Borrego, Isabel | - |
dc.contributor.author | Fernández Arrojo, Lucía | - |
dc.contributor.author | Plou Gasca, Francisco José | - |
dc.contributor.author | Antonio, Jiménez | - |
dc.contributor.author | Fernández Lobato, María | - |
dc.date.accessioned | 2010-06-01T14:36:10Z | - |
dc.date.available | 2010-06-01T14:36:10Z | - |
dc.date.issued | 2009-02 | - |
dc.identifier.citation | Appl Environ Microbiol.75(4):1065-73 (2009) | en_US |
dc.identifier.issn | 0099-2240 | - |
dc.identifier.uri | http://hdl.handle.net/10261/24934 | - |
dc.description.abstract | An extracellular β-fructofuranosidase from the yeast Xanthophyllomyces dendrorhous was characterized biochemically, molecularly, and phylogenetically. This enzyme is a glycoprotein with an estimated molecular mass of 160 kDa, of which the N-linked carbohydrate accounts for 60% of the total mass. It displays optimum activity at pH 5.0 to 6.5, and its thermophilicity (with maximum activity at 65 to 70°C) and thermostability (with a T50 in the range 66 to 71°C) is higher than that exhibited by most yeast invertases. The enzyme was able to hydrolyze fructosyl-β-(21)-linked carbohydrates such as sucrose, 1-kestose, or nystose, although its catalytic efficiency, defined by the kcat/Km ratio, indicates that it hydrolyzes sucrose approximately 4.2 times more efficiently than 1-kestose. Unlike other microbial β-fructofuranosidases, the enzyme from X. dendrorhous produces neokestose as the main transglycosylation product, a potentially novel bifidogenic trisaccharide. Using a 41% (wt/vol) sucrose solution, the maximum fructooligosaccharide concentration reached was 65.9 g liter–1. In addition, we isolated and sequenced the X. dendrorhous β-fructofuranosidase gene (Xd-INV), showing that it encodes a putative mature polypeptide of 595 amino acids and that it shares significant identity with other fungal, yeast, and plant β-fructofuranosidases, all members of family 32 of the glycosyl-hydrolases. We demonstrate that the Xd-INV could functionally complement the suc2 mutation of Saccharomyces cerevisiae and, finally, a structural model of the new enzyme based on the homologous invertase from Arabidopsis thaliana has also been obtained. | en_US |
dc.description.sponsorship | This study was supported by grants from the Plan Nacional CICYT (BIO2004-03773-C04-01/03 and BIO2007-67708-C04-01/03), by Genoma España (National Foundation for Promoting Genomics and Proteomics), and by an institutional grant from the Fundación Ramón Areces to the Centro de Biología Molecular Severo Ochoa. D.L. was supported by a Spanish FPU fellowship from the Ministerio de Educación y Ciencia. | en_US |
dc.format.extent | 659190 bytes | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | en_US |
dc.publisher | American Society for Microbiology | en_US |
dc.rights | openAccess | en_US |
dc.subject | Xanthophyllomyces dendrorhous | en_US |
dc.subject | thermophilicity | en_US |
dc.title | Molecular and Biochemical Characterization of a β-Fructofuranosidase from Xanthophyllomyces dendrorhous | en_US |
dc.type | artículo | en_US |
dc.identifier.doi | 10.1128/AEM.02061-08 | - |
dc.description.peerreviewed | Peer reviewed | en_US |
dc.relation.publisherversion | http://dx.doi.org/10.1128/AEM.02061-08 | en_US |
dc.contributor.funder | Comisión Interministerial de Ciencia y Tecnología, CICYT (España) | - |
dc.contributor.funder | Fundación Genoma España | - |
dc.contributor.funder | Fundación Ramón Areces | - |
dc.contributor.funder | Ministerio de Educación y Ciencia (España) | - |
dc.identifier.funder | http://dx.doi.org/10.13039/100008054 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100007273 | es_ES |
dc.identifier.pmid | 19088319 | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairetype | artículo | - |
item.grantfulltext | open | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | With Fulltext | - |
item.languageiso639-1 | en | - |
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MFdez-Lobato_App.Env.Microbiol.pdf | 643,74 kB | Adobe PDF | Visualizar/Abrir |
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