Actin proteolysis during ripening of dry fermented sausages at different pH values

Alberto Berardo, Bart Devreese, H. De Maere, Despoina Angeliki Stavropoulou, G. Van Royen, Frederic Leroy, S. De Smet

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

In dry fermented sausages, myofibrillar proteins undergo intense proteolysis generating small peptides and free amino acids that play a role in flavour generation. This study aimed to identify small peptides arising from actin proteolysis, as influenced by the type of processing. Two acidification profiles were imposed, in order to mimic the pH normally obtained in southern-type and northern-type dry fermented sausages. The identification of peptides was done by liquid chromatography coupled to mass spectrometry
in a data-independent positive mode of acquisition (LC-MSE). During manufacturing of the dry fermented sausages, actin was highly proteolysed, especially in nine regions of the sequence. After fermentation, 52 and 42 actin-derived peptides were identified at high and low pH, respectively, which
further increased to 66 and 144 peptides, respectively, at the end of ripening. Most peptides were released at the cleavage sites of cathepsins B and D, which thus play an important role.
Original languageEnglish
Pages (from-to)1322-1332
Number of pages11
JournalFood Chemistry
Volume221
DOIs
Publication statusPublished - 15 Apr 2017

Keywords

  • Actin
  • Cathepsins
  • Dry fermented sausages
  • Mass spectrometry
  • Proteolysis

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