http://www.cnr.it/ontology/cnr/individuo/prodotto/ID168885
Lipoxygenase involvement in ripening strawberry (Articolo in rivista)
- Type
- Label
- Lipoxygenase involvement in ripening strawberry (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1021/jf061457g (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Leone A; Bleve-Zacheo T; Gerardi C; Melillo MT; Leo L; Zacheo G; (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
- http://pubs.acs.org/doi/abs/10.1021/jf061457g (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
- Note
- PubMe (literal)
- ISI Web of Science (WOS) (literal)
- Scopu (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto per la Protezione delle Piante, CNR, Bari, Italy
Istituto di Scienze delle Produzioni Alimentari, CNR, 73100 Lecce, Italy (literal)
- Titolo
- Lipoxygenase involvement in ripening strawberry (literal)
- Abstract
- The enzymatic activity, subcellular localization, and immunolocalization of plant lipoxygenase (LOX)
in strawberry fruits (Fragaria ?ananassa, Duch) were investigated. Chemical and enzymatic properties
of LOX have been characterized, and the LOX capability of oxygenating free and esterified unsaturated
fatty acids into C6 volatile aldehydes has been confirmed. Fruits at unripe, turning, and ripe stages
were analyzed for LOX activity and protein localization by Western blots, two-dimensional electrophoresis,
and immunolocalization analyses. The ability of strawberry tissues to in vivo metabolize
linolenic acid or linoleic acid into C6 volatile aldehydes and the LOX products was also analyzed.
Analysis of strawberry proteins showed that a number of LOX forms, corresponding to at least two
mobility groups of approximately 100 and 98 kDa and pI values ranging between 4.4 and 6.5, were
present. Confocal and electron microscopy analyses support the idea that LOX proteins are associated
to lipid-protein aggregates. Both exogenously supplied linoleate and linolenate were converted into
hexanal and trans-2-hexenal at the three fruit-ripening stages. Our experiments suggest the presence
of different LOX isoforms in strawberry fruits and that the lipoxygenase-hydroperoxide lyase pathway
plays a role in converting lipids to C6 volatiles during ripening. (literal)
- Prodotto di
- Autore CNR
- Insieme di parole chiave
Incoming links:
- Autore CNR di
- Prodotto
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
- Insieme di parole chiave di