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Does oxidation affect the water functionality of myofibrillar proteins?
J Agric Food Chem. 2007 Mar 21; 55(6):2342-8.JA

Abstract

Water-binding properties of myofibrils extracted from porcine muscle, and added hemoglobin with and without exposure to H2O2, were characterized using low-field proton NMR T2 relaxometry. The effects of pH and ionic strength in the samples were investigated as pH was adjusted to 5.4, 6.2, and 7.0 and ionic strength was adjusted to 0.29, 0.46, and 0.71 M, respectively. The formation of dityrosine as a measure of oxidative protein cross-linking revealed a significant increase in dityrosine concentrations upon H2O2 activation. The formation of dityrosine was strongly pH-dependent and increased with decreasing pH. In addition, increased levels of thiobarbituric acid reactive substances were observed upon addition of H2O2, implying that lipid oxidation was enhanced, however, with a different oxidation pattern as compared to the myofibrillar proteins. Low-field NMR relaxation measurements revealed reduced T2 relaxation times upon H2O2 activation, which corresponds to reduced water-holding capacity upon oxidation. However, a direct relationship between degree of oxidation and T2 relaxation time was not observed with various pH values and ionic strengths, and further studies are needed for a complete understanding of the effect of oxidation on myofibrillar functionality.

Authors+Show Affiliations

Research Center Foulum, Department of Food Science, Faculty of Agricultural Sciences, University of Aarhus, P.O. Box 50, DK-8830 Tjele, Denmark. HanneC.Bertram@agrsci.dkNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17316016

Citation

Bertram, Hanne Christine, et al. "Does Oxidation Affect the Water Functionality of Myofibrillar Proteins?" Journal of Agricultural and Food Chemistry, vol. 55, no. 6, 2007, pp. 2342-8.
Bertram HC, Kristensen M, Østdal H, et al. Does oxidation affect the water functionality of myofibrillar proteins? J Agric Food Chem. 2007;55(6):2342-8.
Bertram, H. C., Kristensen, M., Østdal, H., Baron, C. P., Young, J. F., & Andersen, H. J. (2007). Does oxidation affect the water functionality of myofibrillar proteins? Journal of Agricultural and Food Chemistry, 55(6), 2342-8.
Bertram HC, et al. Does Oxidation Affect the Water Functionality of Myofibrillar Proteins. J Agric Food Chem. 2007 Mar 21;55(6):2342-8. PubMed PMID: 17316016.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Does oxidation affect the water functionality of myofibrillar proteins? AU - Bertram,Hanne Christine, AU - Kristensen,Mette, AU - Østdal,Henrik, AU - Baron,Caroline P, AU - Young,Jette F, AU - Andersen,Henrik Jørgen, Y1 - 2007/02/23/ PY - 2007/2/24/pubmed PY - 2007/7/7/medline PY - 2007/2/24/entrez SP - 2342 EP - 8 JF - Journal of agricultural and food chemistry JO - J Agric Food Chem VL - 55 IS - 6 N2 - Water-binding properties of myofibrils extracted from porcine muscle, and added hemoglobin with and without exposure to H2O2, were characterized using low-field proton NMR T2 relaxometry. The effects of pH and ionic strength in the samples were investigated as pH was adjusted to 5.4, 6.2, and 7.0 and ionic strength was adjusted to 0.29, 0.46, and 0.71 M, respectively. The formation of dityrosine as a measure of oxidative protein cross-linking revealed a significant increase in dityrosine concentrations upon H2O2 activation. The formation of dityrosine was strongly pH-dependent and increased with decreasing pH. In addition, increased levels of thiobarbituric acid reactive substances were observed upon addition of H2O2, implying that lipid oxidation was enhanced, however, with a different oxidation pattern as compared to the myofibrillar proteins. Low-field NMR relaxation measurements revealed reduced T2 relaxation times upon H2O2 activation, which corresponds to reduced water-holding capacity upon oxidation. However, a direct relationship between degree of oxidation and T2 relaxation time was not observed with various pH values and ionic strengths, and further studies are needed for a complete understanding of the effect of oxidation on myofibrillar functionality. SN - 0021-8561 UR - https://www.unboundmedicine.com/medline/citation/17316016/Does_oxidation_affect_the_water_functionality_of_myofibrillar_proteins L2 - https://doi.org/10.1021/jf0625353 DB - PRIME DP - Unbound Medicine ER -