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Characterization of the Myofibrillar Proteome as a Way to Better Understand Differences in Bovine Meats Having Different Ultimate pH Values
Author(s) -
FuenteGarcia Claudia,
Sentandreu Enrique,
Aldai Noelia,
Oliván Mamen,
Sentandreu Miguel Ángel
Publication year - 2020
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.202000012
Subject(s) - fractionation , myofibril , proteome , chromatography , myosin , chemistry , desmin , gel electrophoresis , polyacrylamide gel electrophoresis , biochemistry , biology , enzyme , vimentin , immunohistochemistry , immunology
Influence of ultimate pH (pHu) on the occurrence of defective meats known as dark, firm, and dry (DFD) meats has been studied through a proteomic approach at early post‐mortem times. The myofibrillar sub‐proteome of longissimus thoracis et lumborum muscle from twelve loin samples from Asturiana de los Valles x Friesian yearling bulls, previously classified into two groups of six samples according to their pH values (normal, pHu < 6.0 and high, pHu ≥ 6.0), is analyzed at 24 h post‐mortem. Fractionation/enrichment of muscle samples is carried out by combining OFFGEL fractionation in the pH range 4–7 followed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS‐PAGE) of the retrieved liquid fractions. Four protein bands satisfactorily discriminate between meat samples with normal and high pHu. These bands are quantified by image analysis, and further identified by liquid chromatography‐mass spectrometry as desmin, pyruvate kinase, myosin light chain, and myosin heavy chain‐1 and ‐2. Coupling OFFGEL and SDS‐PAGE separation with MS provides detailed and reproducible myofibrillar protein profiles enabling comparison among the sample groups assayed. This makes feasible to identify biomarkers capable to better understand pre‐slaughter stress condition susceptible to give DFD meats with high pHu values.