Surface Characterization of Oxidized Myofibrils Using X-ray Photoelectron Spectroscopy and Scanning Electron Microscopy

摘要

The functional properties of myofibrils depend largely on their surface characteristics. Changes in surface characteristics of myofibrils after chemical oxidation were elucidated using X-ray photoelectron spectroscopy (XPS) and scanning electron microscopy. Myofibrils were oxidized by a hydroxyl radical generating system. Lipid oxidation and phospholipid distribution were altered during the oxidative processing. Results from particle size analysis, sodium dodecyl sulfate— polyacrylamide gel electrophoresis, and salt solubility indicated that protein cross-linking and fragmentation occurred during the oxidation of myofibrils. XPS analysis of C1s, N 1s, and O 1s spectra suggested that surface chemical function concentrations changed significantly because of the modification of amino acid side chains that rendered protein cross-links and fragmentation and phospholipid alteration. Analysis of the correlation between the surface chemical composition and parameters of particle size distributions confirmed that protein carbonylation and phospholipid alteration were involved in protein surface modification. Results of the microstructure analysis were in agreement with those of particle size and XPS analysis.