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Published on: December 14, 2011
Small peptides released from muscle glycolytic enzymes during dry-cured ham processing
L Mora1, M L Valero, M M Sánchez Del Pino
1Instituto de Agroquímica y Tecnología de Alimentos (CSIC), Avenida Agustín Escardino, Paterna, Valencia, Spain.
Journal of Proteomics
|January 18, 2011
Summary
Researchers identified 45 novel enzyme fragments in dry-cured ham, revealing significant protein breakdown during processing. This study aids in identifying naturally generated peptides in meat products.
Area of Science:
- Food Science
- Biochemistry
- Proteomics
Background:
- Glycolytic enzymes are crucial for carbohydrate energy extraction in muscle sarcoplasm.
- The glycolytic pathway involves 10 enzyme-catalyzed steps, with specific enzymes playing key roles in energy metabolism and protein degradation.
- Dry-cured ham processing involves complex biochemical changes, including proteolysis, affecting its final characteristics.
Purpose of the Study:
- To identify and characterize specific enzyme fragments resulting from proteolysis in dry-cured ham sarcoplasmic fraction.
- To provide a comprehensive list of novel enzyme-derived peptides generated during dry-cured ham processing.
- To evaluate and compare the efficacy of different search engines and databases for identifying naturally generated peptides.
Main Methods:
- Proteomic analysis of dry-cured ham sarcoplasmic fraction using mass spectrometry (1100-2600 Da range).
- Identification of enzyme fragments using Paragon and Mascot search engines.
- Cross-validation of identified peptides against UniProt and NCBInr databases.
Main Results:
- Identification of 45 specific enzyme fragments for the first time, including glycogen phosphorylase, enzymes catalyzing steps 6-10 of glycolysis (glyceraldehyde 3-phosphate dehydrogenase, phosphoglycerate kinase, phosphoglycerate mutase, enolase, pyruvate kinase), and lactate dehydrogenase.
- Evidence of intense proteolysis within the sarcoplasmic fraction of dry-cured ham.
- Comparative analysis of search engine performance in identifying naturally generated peptides.
Conclusions:
- The study successfully identified numerous novel enzyme fragments, confirming significant proteolysis in dry-cured ham.
- The findings contribute to understanding meat biochemistry and the generation of bioactive peptides during meat curing.
- This research facilitates the selection of optimal bioinformatic tools for identifying naturally occurring peptides in processed meat products.

