Comparative proteomic profiling of myofibrillar proteins in dry-cured ham with different proteolysis indices and
M López-Pedrouso1, C Pérez-Santaescolástica2, D Franco2
1Department of Zoology, Genetics and Physical Anthropology, University of Santiago de Compostela, Santiago de Compostela 15872, Spain.
Abstract:
Excessive proteolysis during dry-cured ham processing may lead to high adhesiveness and consumer dissatisfaction. The aim of this research is to identify biomarkers for proteolysis and adhesiveness. Two hundred biceps femoris porcine muscle samples from Spanish dry-cured ham were firstly evaluated for various physicochemical parameters, including their proteolysis indices and instrumental adhesiveness. Proteins of samples with extreme proteolysis indices were separated by two-dimensional electrophoresis and identified by tandem mass spectrometry (MALDI-TOF/TOF). We found that hams of higher proteolysis index had statistically significant increased adhesiveness. Proteomic analysis revealed statistically significant qualitative and quantitative differences between sample groups. Thus, protein fragments increased remarkably in samples with higher proteolysis index scores. In addition, higher proteolysis index hams showed increased degradation for a total of five non-redundant myofibrillar and sarcoplasmic proteins. However, myosin-1, α-actin and myosin-4 proteins were the biomarkers that underwent the most intense response to proteolysis and adhesiveness.
More Related Videos
10:51Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting
Published on: April 10, 2014
09:26Species Determination and Quantitation in Mixtures Using MRM Mass Spectrometry of Peptides Applied to Meat Authentication
Published on: September 20, 2016
