Home |  English version |  Mappa |  Commenti |  Sondaggio |  Staff |  Contattaci Cerca nel sito  
Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2005

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Proteomic study of sarcoplasmic and myofibrillar proteins of dry cured hams

Anno di pubblicazione: 2005

Autori: Di Luccia A.; Picariello G.; Cacace G.; Scaloni A.; Faccia M.; Liuzzi V.; Alviti G.; Spagna Musso S.

Affiliazioni autori: Dipartimento di Produzione Animale, Universita` di Bari, via G. Amendola 165/A, 70126 Bari, Italy Istituto di Scienze dellAlimentazione-CNR, Consiglio Nazionale delle Ricerche, via Roma 52 A/C, 83100 Avellino, Italy IABBAM-CNR, via Argine 1085, 80147 Napoli, Italy Dipartimento di Scienza degli Alimenti, Universita` di Napoli ''Federico II'', via Universita` 100, 80055 Portici (NA), Italy

Autori CNR:

  • GIUSEPPINA CACACE
  • ALDO DI LUCCIA
  • GIANLUCA PICARIELLO

Lingua: inglese

Abstract: The myofibrillar fraction of raw ham muscles and dry-cured hams with different ripening times was extracted in denaturing and reducing conditions and subjected to two-dimensional gel electrophoresis. The two-dimensional maps gave overall pictures of the already noted progressive disappearance of actin, tropomyosin and myosin light chains during ripening. In addition, two fragments from Myosin Heavy Chain proteolysis, marked as myosin chain fragments MCF1 and MCF2, were identified by immunodetection and matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF MS). Furthermore, a new form of actin on two-dimensional gel was identified by MALDI-TOF peptide mapping. In 12-month-old dry-cured ham, most myofibrillar proteins were completely hydrolyzed. At this stage of ripening, in fact, in some Parma and S. Daniele dry-cured ham samples, myosin heavy chain fragments and other unidentified neo-formed spots were found. Some of the sarcoplasmic proteins in water extracts from pork meat markedly decreased in amount or disappeared totally, during ripening. Surprisingly, two-dimensional gel electrophoresis maps of the water soluble protein fraction from dry-cured ham showed the presence of two spots identified as tropomyosin alpha- and beta-chain. This result suggests that some of the saline soluble myofibrillar proteins can disappear from this fraction because of salt solubilization and not due to complete enzyme action. Two-dimensional gel electrophoresis (2-DGE) has proved a powerful toot to evaluate the enzymatic susceptibility of meat proteins and the evolution of protein map fragmentation throughout ripening process as well as a means of obtaining a standard fingerprinting map characterizing the final product

Lingua abstract: inglese

Pagine da: 479

Pagine a: 491

Rivista:

Meat science Applied Science Publishers.
Paese di pubblicazione: Regno Unito
Lingua: inglese
ISSN: 0309-1740

Numero volume: 69

DOI: 10.1016/j.meatsci.2004.10.004

Indicizzato da: ISI Web of Science (WOS) [000226443400014]

Altre informazioni: 1

Strutture CNR:

Moduli:

 
Torna indietro Richiedi modifiche Invia per email Stampa
Home Il CNR  |  I servizi News |   Eventi | Istituti |  Focus