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Protein modifications in cooked pork products investigated by a proteomic approach
- Source :
- Food chemistry. 172
- Publication Year :
- 2014
-
Abstract
- To evaluate process-induced protein modifications in cooked ham and emulsion sausages, the proteomes of whole-cut (Parma and “Praga” cooked hams) and comminuted pork (mortadella and wurstel) products were compared to raw pork using two-dimensional gel electrophoresis (2-DE) coupled to image analysis and mass spectrometry (MS). Other than heat-induced breakdown of part of the myosin heavy chains, the 2-DE pattern of cooked ham was substantially similar to that of raw pork. However, the MS-based analysis showed minor modifications, including the extensive oxidation of methionines. In contrast, likely due to emulsification, comminuted sausages were characterized by an abundant insoluble protein fraction (IPF). Interestingly, tropomyosin and myosin light chains in comminuted sausages were exclusively found in the IPF. Our results indicate that the protein aggregation systems of cooked hams and emulsion sausages reflect the processing conditions and are definitely different, the former being characterized mainly by disulphide bridges and the latter by additional covalent inter-protein links.
- Subjects :
- Proteomics
Myosin light-chain kinase
Proteome
Swine
Tropomyosin
Protein aggregation
Myosins
Analytical Chemistry
Myosin
Animals
Electrophoresis, Gel, Two-Dimensional
Food science
Cooking
Gel electrophoresis
Chromatography
Chemistry
technology, industry, and agriculture
food and beverages
General Medicine
Hydrogen-Ion Concentration
Meat Products
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Emulsion
Insoluble protein
Electrophoresis, Polyacrylamide Gel
Dietary Proteins
Food Science
Subjects
Details
- ISSN :
- 18737072
- Volume :
- 172
- Database :
- OpenAIRE
- Journal :
- Food chemistry
- Accession number :
- edsair.doi.dedup.....8b6359b5d9ba8ce8f2a7d39cabfd29d6