Induction and characterization of an unusual alpha-D-galactosidase from Talaromyces flavus (Articolo in rivista)

Type
Label
  • Induction and characterization of an unusual alpha-D-galactosidase from Talaromyces flavus (Articolo in rivista) (literal)
Anno
  • 2007-01-01T00:00:00+01:00 (literal)
Alternative label
  • Simerska P., Monti D., Cechova I., Pelantova H., Mackova M., Bezouska K., Riva S., Kren V. (2007)
    Induction and characterization of an unusual alpha-D-galactosidase from Talaromyces flavus
    in Journal of biotechnology
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Simerska P., Monti D., Cechova I., Pelantova H., Mackova M., Bezouska K., Riva S., Kren V. (literal)
Pagina inizio
  • 61 (literal)
Pagina fine
  • 71 (literal)
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  • 128 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Institute of Microbiology, Academy of Sciences of the Czech Republic, V?denska 1083, CZ-142 20 Prague 4, Czech Republic. Istituto di Chimica del Riconoscimento Molecolare, CNR, Via Mario Bianco 9, I 201 31 Milan, Italy. Department of Biochemistry and Microbiology, Institute of Chemical Technology, Technicka 5, CZ 168 20 Prague 6, Czech Republic. Department of Biochemistry, Faculty of Science, Charles University Prague, Hlavova 8, CZ-12840 Prague 2, Czech Republic (literal)
Titolo
  • Induction and characterization of an unusual alpha-D-galactosidase from Talaromyces flavus (literal)
Abstract
  • An extracellular alpha-D-galactosidase from Talaromyces flavus CCF 2686 with extremely broad and unusual acceptor specificity is produced exclusively in the presence of the specific inducer--6-deoxy-d-glucose (quinovose). The procedure for the preparation of this very expensive substance has been modified and optimized. Surprisingly, any of other common alpha-D-galactosidase inducers or substrates, e.g., d-galactose, melibiose and raffinose, did not stimulate its production. The crude alpha-D-galactosidase preparation was purified by anion-exchange chromatography and three isoenzymes with different substrate specificities were identified. The main isoenzyme ( alpha-Gal1) was further purified by cation-exchange chromatography and fully characterized. When compared with other alpha-galactosidases and also with other isoenzymes produced by T. flavus, it showed a markedly different regioselectivity and also negligible hydrolytic activity towards melibiose. Moreover, it was active on polymeric substrates (locust bean gum, guar gum) and significantly inhibited by alpha-D-galactopyranosyl azide, D-galactose, D-xylose, melibiose, methyl alpha- and beta-D-galactopyranoside and lactose. (literal)
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