Proteomic Identification of Small (<2000 Da) Myoglobin Peptides Generated in Dry-Cured Ham

Leticia Mora and Fidel Toldrá*

Instituto de Agroquímica y Tecnología de Alimentos (CSIC), Avenue Agustín Escardino 7, ES-46980 Paterna, Valencia, Spain

Article history:
Received January 30, 2012
Accepted May 9, 2012

Key words:
myoglobin, proteolysis, dry-cured ham, peptides, MS/MS ion search, protein identification

Summary:
Myoglobin is a very important sarcoplasmic protein responsible for the colour of meat and meat products. This protein is degraded during post-mortem period (ageing) as well as during longer processes such as dry curing. In the present study, a total of eleven naturally generated fragments of myoglobin detected at the end of the processing of dry-cured ham have been identified for the first time and the intense proteolysis of myoglobin during dry curing has been confirmed. This study was carried out using one-dimensional reversed- phase liquid chromatography combined with nano liquid chromatography and an electrospray ionization source coupled to a quadrupole time-of-flight mass spectrometer. Paragon and Mascot search engines with the databases NCBInr and Swiss-Prot were used for the identification based on raw MS/MS data from one or more peptides, and the possible enzymes involved in myoglobin hydrolysis have also been discussed.

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