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Biochemical changes in myofibrillar protein isolates exposed to three oxidizing systems
Donkeun Park1, Youling L Xiong, Amy L Alderton
1Department of Animal and Food Sciences, University of Kentucky, Lexington, Kentucky 40546, USA.
Abstract:
The objective of the study was to compare three different oxidizing systems commonly present in muscle foods for their influence on the biochemical properties of muscle proteins. Myofibrillar protein isolate (MPI) prepared from pork serratus ventralis muscle was suspended (30 mg protein/mL) in 15 mM piperazine-N,N-bis(2-ethane sulfonic acid) buffer (pH 6.0). Oxidation was induced by incubating the protein suspension at 4 degrees C for 24 h with (i) a hydroxyl radical-generating system (HRGS: 10 microM FeCl3, 0.1 mM ascorbic acid, and 0.05-5.0 mM H2O2), (ii) a lipid-oxidizing system (LOS: 0.05-5.0 mM linoleic acid and 3750 units of lipoxidase/mL), or (iii) a metmyoglobin-oxidizing system (MOS: 0.05-0.5 mM metmyoglobin). Changes in oxidized MPI were measured as Ca- and K-ATPase activities, formation of protein carbonyls and 2-thiobarbituric acid-reactive substances (TBARS), loss of protein thermal stability, and protein aggregation. The three oxidizing matrixes induced complex MPI changes; for example, the Ca- and K-ATPase activities were altered mainly by low-concentration oxidants, but the changes were unique for each oxidizing system. The carbonyl content in MOS-treated MPI was the highest, while the TBARS production, changes in thermal properties, and loss of the myosin heavy chain were the greatest in HRGS-treated MPIs. Overall, the hydroxyl radical-producing medium appeared to be the most oxidative to myofibrillar proteins under the experimental conditions employed in the study.
Insights
This study compared how three muscle food oxidants affect myofibrillar proteins. Hydroxyl radical-generating systems caused the most damage to proteins, impacting their structure and function.
Area of Science:
- Food science
- Protein chemistry
- Biochemistry
Background:
- Muscle foods are susceptible to oxidation, affecting protein quality.
- Understanding the impact of different oxidants is crucial for food preservation.
Purpose of the Study:
- To compare the effects of hydroxyl radical-generating systems (HRGS), lipid-oxidizing systems (LOS), and metmyoglobin-oxidizing systems (MOS) on myofibrillar protein isolate (MPI) biochemical properties.
Main Methods:
- MPI from pork was incubated with HRGS, LOS, or MOS at 4°C for 24 hours.
- Assessed changes in Ca- and K-ATPase activities, protein carbonyls, TBARS, thermal stability, and protein aggregation.
Main Results:
- All three systems induced complex changes in MPI.
- HRGS treatment resulted in the highest TBARS production, greatest loss of thermal stability, and most significant degradation of the myosin heavy chain.
- MOS treatment led to the highest protein carbonyl content.
Conclusions:
- The hydroxyl radical-generating system was the most potent oxidant among the tested systems under the experimental conditions.
- Different oxidizing systems exert unique effects on muscle protein structure and function.
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