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Does oxidation affect the water functionality of myofibrillar proteins?

Hanne Christine Bertram¹, Mette Kristensen, Henrik Østdal

¹Research Center Foulum, Department of Food Science, Faculty of Agricultural Sciences, University of Aarhus, P.O. Box 50, DK-8830 Tjele, Denmark. HanneC.Bertram@agrsci.dk

Journal of Agricultural and Food Chemistry

|February 24, 2007

Summary

Oxidation significantly reduces water-holding capacity in porcine myofibrils, impacting protein functionality. This study used NMR T2 relaxometry to investigate oxidation effects on muscle proteins and lipids under varying pH and ionic strength conditions.

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Area of Science:

Food Science
Biochemistry
Analytical Chemistry

Background:

Myofibrils are key proteins in muscle structure and water-holding capacity.
Oxidative stress can alter protein structure and function, affecting meat quality.
Hemoglobin can act as a pro-oxidant in muscle systems.

Purpose of the Study:

To characterize the water-binding properties of porcine myofibrils.
To investigate the impact of hydrogen peroxide (H2O2)-induced oxidation on myofibrils and lipids.
To determine the influence of pH and ionic strength on oxidative changes.

Main Methods:

Low-field proton NMR T2 relaxometry was used to assess water-binding.
Dityrosine formation was measured as an indicator of protein cross-linking.
Thiobarbituric acid reactive substances (TBARS) assay was used to detect lipid oxidation.
Experiments were conducted at varying pH (5.4, 6.2, 7.0) and ionic strengths (0.29, 0.46, 0.71 M).

Main Results:

H2O2 activation significantly increased dityrosine formation, indicating protein oxidation, which was pH-dependent (higher at lower pH).
Lipid oxidation, measured by TBARS, was also enhanced by H2O2 but followed a different pattern than protein oxidation.
NMR T2 relaxation times decreased upon H2O2 activation, suggesting reduced water-holding capacity.
A direct correlation between the degree of oxidation and T2 relaxation time was not consistently observed across different pH and ionic strengths.

Conclusions:

Oxidation, particularly induced by H2O2, negatively impacts the water-holding capacity of porcine myofibrils.
The extent of protein oxidation is influenced by pH, while lipid oxidation shows a distinct pattern.
Further research is needed to fully elucidate the complex relationship between oxidation, environmental factors, and myofibrillar functionality.