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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2014

Contributo in rivista

Tipo: Articolo in rivista

Titolo: In vitro digestion of Bresaola proteins and release of potential bioactive peptides

Anno di pubblicazione: 2014

Formato: Elettronico Cartaceo

Autori: Ferranti, Pasquale; Nitride, Chiara; Nicolai, Maria Adalgisa; Mamone, Gianfranco; Picariello, Gianluca; Bordoni, Alessandra; Valli, Veronica; Di Nunzio, Mattia; Babini, Elena; Marcolini, Elena; Capozzi, Francesco

Affiliazioni autori: University of Naples Federico II; Consiglio Nazionale delle Ricerche (CNR); University of Bologna; University of Bologna

Autori CNR:


Lingua: inglese

Abstract: Bresaola is traditionally produced by curing and air-drying entire anatomic cuts of lean bovine hindquarters. Because of its low-fat and high-protein content, Bresaola is increasingly appreciated for the nutritional properties and has become one of the best known and exported Italian meat products. Both sarcoplasmic and myofibrillar protein fractions of Bresaola are extensively hydrolyzed by endogenous proteases, since the early post mortem, releasing a large variety of peptides many of which can exert several biological activities in human body. When ingested, Bresaola proteins and (poly)peptides are further degraded by gastrointestinal (GI) proteases. With the aim to identify bovine muscle-derived proteins and peptides surviving digestion, two Bresaola samples (one with and one without the Protected Geographical Indication label) were subjected to a static in vitro model of digestion that included the sequential oral, gastric and duodenal phases. The "digestomes" were characterized by mass spectrometry-based proteomic and peptidomic strategies. Aside from slight differences, probably related to the different nature of the raw material and to different technological processes, the great part of the peptides released at the end of digestion was common to the two samples. Sarcoplasmic proteins were promptly degraded, whereas myofibrillar chains require a previous proteolytic release and are not completely hydrolyzed by gastro-duodenal proteases even after prolonged hydrolysis. More than 170 peptides liberated from the major structural (actin, myosin) and sarcoplasmic muscle proteins were identified. Several among these peptides are or are precursor of potentially antihypertensive or antioxidant sequences. (C) 2014 Published by Elsevier Ltd.

Lingua abstract: inglese

Pagine da: 157

Pagine a: 169

Pagine totali: 13


Food research international Elsevier Applied Science on behalf of the Canadian Institute of Food Science and Technology,
Paese di pubblicazione: Regno Unito
Lingua: inglese
ISSN: 0963-9969

Numero volume: 63

DOI: 10.1016/j.foodres.2014.02.008

Referee: Sė: Internazionale

Indicizzato da: ISI Web of Science (WOS) [000342552300006]

Parole chiave:

  • Bresaola
  • In vitro digestion
  • Proteomics
  • Bioactive peptides
  • Mass spectrometry

Strutture CNR:


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