Intense Degradation of Myosin Light Chain Isoforms in Spanish Dry-Cured Ham

Mora, Leticia; Sentandreu, Miguel Ángel

doi:10.1021/jf104070q

Cited by 45 publications

(19 citation statements)

References 37 publications

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“…For that, the obtained MS/MS spectra are matched with theoretical peptide sequences contained in databases in order to elucidate the specific sequences. So, numerous peptides derived from myofibrillar proteins such as actin, myosin light chain, troponin T, titin, LIM domain‐binding protein 3, and myozenin, as well as peptides from sarcoplasmic proteins such as creatine kinase, glycolytic enzymes, myoglobin, and ubiquitin have been identified in Spanish dry‐cured ham using mainly MALDI‐TOF MS and ESI‐LC‐Q/TOF MS. Table reports the number of peptides and their proteins of origin identified in Spanish dry‐cured ham. Several small peptides were also identified in Chinese dry‐cured Jinhua ham using MS in tandem, but their proteins of origin were not elucidated .…”

Section: Peptidomics In the Characterization Of Dry‐cured Hammentioning

confidence: 99%

Perspectives in the Use of Peptidomics in Ham

Gallego

Mora

2018

Proteomics

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The use of proteomics in food science has permitted both a better characterization of the food products and the control of their final quality despite the fact that food systems are under continuous changes during processing and consumption. Ham is a very popular meat product frequently consumed in Mediterranean countries after a dry-curing processing that results in the generation of large amounts of peptides that contribute to its texture, flavor, and final quality. Proteolysis is the main biochemical mechanism occurring throughout the dry-cured ham processing and a better knowledge of this phenomenon is essential to give an extra value to the product and produce regular batches. In this regard, peptidomics has become an important tool for the characterization of dry-cured hams in order to identify and quantify bioactive peptides and potential biomarkers, study their stability under processing conditions or gastrointestinal digestion, and search for post-translational modifications that could affect the quality of dry-cured hams. This manuscript is reviewing from the first uses of comparative proteomics in dry-cured ham approaches to the most modern peptidomic studies and their contribution to the advance in meat science.

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Section: Peptidomics In the Characterization Of Dry‐cured Hammentioning

confidence: 99%

Perspectives in the Use of Peptidomics in Ham

Gallego

Mora

2018

Proteomics

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“…On the other hand, Discriminant component 2 is responsible for 12.6% of the variance within the dataset for these two discriminant components, which allows to differentiate between raw hams and hams at the beginning of the process (post-salting and first period of ripening) as well as between hams along the ripening-drying period and the final product (9 months of ripening). In addition, the loading plot ( Figure 1B Numerous studies have reported the intense proteolysis of myosin protein during drycured ham processing by using electrophoretic techniques [31,32] and MS techniques [31,33,34]. Focusing on MYL1, Mora et al [34] identified 137 peptides resulting from this protein in dry-cured hams at 9 months of processing by using tandem mass spectrometry.…”

Section: Resultsmentioning

confidence: 99%

Peptidomics as a tool for quality control in dry-cured ham processing

Gallego

Mora

Toldrá

2016

Journal of Proteomics

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Spanish dry-cured ham is a high quality product whose economic value is mainly given by its curing time. An intense proteolysis takes place throughout the dry-cured processing, which results in the generation of a high amount of peptides and free amino acids responsible for the final quality of dry-cured hams. In this work, a peptidomics approach has been used to study the evolution of peptides throughout the ham dry-curing process, identifying and quantifying the generated peptides in order to define potential quality biomarkers. For this purpose, dry-cured ham extracts at different processing times (0, 2, 3.5, 5, 6.5 and 9months) were fractionated by size-exclusion chromatography and analysed by nanoliquid chromatography coupled to tandem mass spectrometry. Differences obtained in the relative quantification of peptides by using a label-free methodology were useful to establish differences between processing times, being peptides generated by the degradation of myosin light chain 1 protein mainly responsible for the observed differences during the last stages of curing. In particular, APAPAPAPPKEEKI and PAPAPAPAPAPAPAPPKE, exclusively identified at 9months of curing, would be potential markers to control the time of curing and thus the final quality of dry-cured hams. Biological significance A peptidomics approach has been used to study the evolution of peptides throughout the ham dry-curing process, identifying peptides APAPAPAPPKEEKI and PAPAPAPAPAPAPAPPKE, which were only detected at 9months of process. So, they would constitute good potential markers to control the time of processing and thus the final quality of dry-cured hams.

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“…Meat protein proteolysis creates small peptides, free amino acids, and degradation products that determine the texture, flavor, and odor of the final product (Toldrá et al, 2000;Sforza et al, 2001;Sentandreu et al, 2003). Recently, a number of peptides generated from actin (Sentandreu et al, 2007), troponin T (Mora et al, 2010), and MLC-1 and MLC-2 (Mora et al, 2011) during the dry curing of Spanish hams have been isolated and identified by 2D-LC coupled to MS/MS. However, the microflora also plays a relevant role in the ripening process (Talon et al, 2007), as do endogenous proteases.…”

Section: Postmortem Changes In Meat Proteinsmentioning

confidence: 99%