Actin proteolysis during ripening of dry fermented sausages at different pH values. (15th April 2017)

• Record Type: Journal Article
• Authors: Berardo, A.; Devreese, B.; De Maere, H.; Stavropoulou, D.A.; Van Royen, G.; Leroy, F.; De Smet, S.
• Is Part Of: Food chemistry. Volume 221(2017)
• Page Start: 1322
• Page End: 1332
• Publication Date: 2017-04-15
• Subjects: Actin -- Proteolysis -- Dry fermented sausages -- Cathepsins -- Mass spectrometry; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2016.11.023
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Actin-derived peptides were identified in dry fermented sausages. Actin was highly proteolysed, especially in nine regions of the sequence. A more acid pH profile generated more unique peptides. 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-MS E ). 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.