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

Alberto Berardo, Hannelore De Maere, Despoina Angeliki Stavropoulou, Geert Van Royen, Frédéric Leroy, Stefaan De Smet

    Onderzoeksoutput: Bijdrage aan tijdschriftA1: Web of Science-artikelpeer review


    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.
    Oorspronkelijke taalEngels
    TijdschriftFOOD CHEMISTRY
    Pagina's (van-tot)1322-1332
    PublicatiestatusGepubliceerd - 5-nov-2016

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