This study aimed to investigate the relative reaction rate of protein and lipid oxidation in different biphasic model systems (linoleic acid; liposome; emulsion) containing myofibrillar protein (MFP at 1, 8 and 20 mg/mL) under hydroxyl radical stress. Protein oxidation markers exhibited significant changes in 2 h: reduced tryptophan fluorescence intensity, carbonyl formation, and extensive polymerization of myosin. In contrast, no detectable changes (P >.05) in lipid peroxide occurred within 2 h except for samples with 1 mg/mL MFP which showed an early TBARS formation. Of the three biphasic systems, the oxidative stability of lipids followed the order of emulsion > linoleic acid > liposome, indicating the steric role of proteins. In general, MFP was more susceptible to radicals than lipids, and a higher protein:lipid ratio was associated with a slower TBARS production and more rapid protein oxidation, suggesting a sacrificing role of MFP to protect lipids.
|Number of pages||8|
|State||Published - Mar 15 2018|
Bibliographical noteFunding Information:
This study was supported by the USDA National Institute of Food and Agriculture (Hatch project 1005724) and an Oversea Study Fellowship from the China Scholarship Council (to J.Y.). Approved for publication as journal article number 17-07-060 by the Director of the Kentucky Agricultural Experiment Station.
- Linoleic acid
- Lipid oxidation
- Protein oxidation
ASJC Scopus subject areas
- Analytical Chemistry
- Food Science