A novel thermophilic Enzyme for trehalose production (Articolo in rivista)

Type
Label
  • A novel thermophilic Enzyme for trehalose production (Articolo in rivista) (literal)
Anno
  • 2002-01-01T00:00:00+01:00 (literal)
Alternative label
  • De Pascale D., Di Lernia I., Sasso M.P., Furia A., De Rosa M., Rossi M. (2002)
    A novel thermophilic Enzyme for trehalose production
    in Extremophiles (Tokyo, Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • De Pascale D., Di Lernia I., Sasso M.P., Furia A., De Rosa M., Rossi M. (literal)
Pagina inizio
  • 463 (literal)
Pagina fine
  • 468 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 6 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Titolo
  • A novel thermophilic Enzyme for trehalose production (literal)
Abstract
  • In recent years a number of hyperthermophilic micro-organisms of Sulfolobales have been found to produce trehalose from starch and dextrins. In our laboratory genes encoding the trehalosyl dextrin forming enzyme (TDFE) and the trehalose forming enzyme (TFE) of S. solfataricus MT4 have been cloned and expressed in E. coli (Rb791). Here we report the construction of a new protein obtained by fusion of TFE and TDFE coding sequences which is able to produce trehalose from dextrins at high temperature by sequential enzymatic steps. We demonstrate that the bifunctional fusion enzyme is able to produce trehalose starting from malto-oligosaccharides at 75 degrees C. Furthermore we partially purified the recombinant fusion protein from bacterial cell free extracts and from insoluble fractions in which the fusion protein was also found as aggregate in inclusion bodies. (literal)
Prodotto di
Autore CNR

Incoming links:


Autore CNR di
Prodotto
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
data.CNR.it