Purification and partial characterization of a peroxidase from plant cell cultures of Cassia didymobotrya and biotransformation studies (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Purification and partial characterization of a peroxidase from plant cell cultures of Cassia didymobotrya and biotransformation studies (Articolo in rivista) (literal)

Anno

• 1998-01-01T00:00:00+01:00 (literal)

Alternative label

• A Vitali; B Botta; G Delle Monache; S Zappitelli; P Ricciardi; S Melino; R Petruzzelli; B Giardina (1998)
  Purification and partial characterization of a peroxidase from plant cell cultures of Cassia didymobotrya and biotransformation studies
  in Biochemical journal (Lond., 1984)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• A Vitali; B Botta; G Delle Monache; S Zappitelli; P Ricciardi; S Melino; R Petruzzelli; B Giardina (literal)

Pagina inizio

• 513 (literal)

Pagina fine

• 519 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 331 (literal)

Rivista

• Biochemical journal (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Vitali, Giardina, Delle Monache: Istituto Chimica del Riconoscimento Molecolre-uos Roma Melino S, Petruzzelli R: Università di Chieti (literal)

Titolo

• Purification and partial characterization of a peroxidase from plant cell cultures of Cassia didymobotrya and biotransformation studies (literal)

Abstract

• An acidic peroxidase (EC 1.11.1.7) produced by cell suspension cultures of Cassia didymobotrya (wild senna) was purified from culture medium collected on the 29th day. The enzyme was shown to be a glycoprotein with a pI of 3.5, a molecular mass of approx. 43 kDa by SDS/PAGE and 50 kDa by gel filtration. The N-terminal sequence was very similar to those of other plant peroxidases. The peroxidase was characterized by a high specificity towards coniferyl alcohol and other natural phenolics such as guaiacol and ferulic and caffeic acids. These findings suggest that the enzyme is involved in lignification processes of the cell wall. Moreover, the enzyme was able to catalyse the oxidation of 4,3',4'-trihydroxychalcone and 4, 3',4'-trihydroxy-3-methoxychalcone to the corresponding 3, 3'-biflavanones, as mixtures of racemic and meso forms. (literal)

Prodotto di

• Istituto di chimica del riconoscimento molecolare (ICRM) (Istituto)

Autore CNR

• BRUNO GIARDINA (Unità di personale esterno)
• ALBERTO VITALI (Unità di personale interno)

Incoming links:

Autore CNR di

• ALBERTO VITALI (Unità di personale interno)
• BRUNO GIARDINA (Unità di personale esterno)

Prodotto

• Istituto di chimica del riconoscimento molecolare (ICRM) (Istituto)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Biochemical journal (Rivista)