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Título

Novel ß-fructofuranosidases from non-conventional yeasts for the synthesis of novel fructosylated derivatives

AutorFernández Arrojo, Lucía; Gimeno-Pérez, María CSIC ORCID; Santos-Moriano, Paloma CSIC ORCID; Relaño, Sofía; Piedrabuena, David CSIC ORCID ; Ramírez-Escudero, Mercedes CSIC ORCID; Sanz-Aparicio, J. CSIC ORCID; Fernández Lobato, María CSIC ORCID; Plou Gasca, Francisco José CSIC ORCID
Palabras clavePrebiotics
Fructooligosaccharides
Fructosylation
GH32 enzymes
Fecha de publicación14-oct-2014
Citación4th International Conference on Novel Enzymes (2014)
ResumenApart from sucrose hydrolysis, beta-fructofuranosidases (beta-FFases) also catalyze the transfer of the fructose moiety from sucrose to other carbohydrates (called acceptors, including sucrose itself), thus forming homo- and hetero-fructooligosaccharides (FOS) with potential applications in functional foods (prebiotics), pharmaceutical and cosmeceutical industries. Most fungal beta-FFases catalyze the formation of beta(2¿1) linkages between fructose units (inulin-type 1F-FOS, e.g. 1-kestose or nystose). We have isolated, purified, characterized and crystallized several extracellular ¿-fructofuranosidases from cultures of the yeasts Xanthophyllomyces dendrorhous (formerly Phaffia rhodozyma), Schwanniomyces occidentalis and Rhodotorula dairenensis with novel specificities. The ¿-FFase from X. dendrorhous is able to synthesize FOS of the 6G-series (neoFOS, e.g. neokestose and neonystose), which contain a ¿(2¿6) linkage between a fructose and the glucosyl moiety of sucrose.1 In addition, this enzyme fructosylates other disaccharides that contain glucose (maltose, isomaltulose, isomaltose, trehalose) and higher size oligosaccharides (maltotriose, raffinose, maltotetraose).2 S. occidentalis ¿-FFase forms 6F-FOS, which contain ¿(2¿6)-linked fructose units (with a levan-type structure; e.g. 6-kestose).3 The ¿-FFase from R. dairenensis synthesizes a complex mixture of 1F-FOS, 6F-FOS and 6G-FOS.4 The immobilization of several FFases has been also investigated to improve the corresponding bioprocesses.
DescripciónTrabajo presentado en la 4th International Conference on Novel Enzymes, celebrada en Gante (Bélgica) del 14 al 17 de octubre de 2014.
URIhttp://hdl.handle.net/10261/188564
Aparece en las colecciones: (CBM) Comunicaciones congresos
(IQF) Comunicaciones congresos
(ICP) Comunicaciones congresos




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