| Literature DB >> 24295685 |
Marta Gallego1, Leticia Mora, Paul D Fraser, María-Concepción Aristoy, Fidel Toldrá.
Abstract
Extensive proteolysis takes place during the processing of dry-cured ham due to the action of muscle peptidases. The aim of this work was to study the degradation of LIM domain binding protein 3 (LDB3), which is located at the Z-lines of the sarcomere, at different times during the Spanish dry-cured ham processing (2, 3.5, 5, 6.5, and 9 months). A total of 107 peptides have been identified by mass spectrometry, most of them generated from the first region of the protein sequence (position 1-90) providing evidence for the complexity and variability of proteolytic reactions throughout the whole process of dry-curing. Methionine oxidation has been observed in several peptides by the end of the process. The potential of some of the identified peptides to be used as biomarkers of dry-cured ham processing has also been considered.Entities:
Keywords: BLAST; BSA; Biomarker; Dry-cured ham; ETD; FA; HCl; HPLC; LDB3; LIM domain binding protein 3; LIM domain-binding protein 3; MS; Mass spectrometry; NCBInr; National center for biotechnology information non-redundant; Peptide oxidation; Peptides; Proteolysis; RSLC; SDS–PAGE; Uniprot; Z-band alternatively spliced PDZ-motif protein; ZASP; basic local alignment search tool; bovine serum albumin; electron transfer dissociation; formic acid; high performance liquid chromatography; hydrochloric acid; mass spectrometry; nLC; nanoliquid chromatography; rapid separation liquid chromatography; sodium dodecyl sulphate polyacrylamide gel electrophoresis; universal protein resource
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Year: 2013 PMID： 24295685 DOI： 10.1016/j.foodchem.2013.10.076
Source DB: PubMed Journal: Food Chem ISSN： 0308-8146 Impact factor: 7.514