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Meat Sci. 2002 Oct;62(2):157-63.

Role of deoxyhemoglobin in lipid oxidation of washed cod muscle mediated by trout, poultry and beef hemoglobins.

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1
University of Wisconsin-Madison, Muscle Biology and Meat Science Laboratory, 1805 Linden Dr. West, Madison, WI 53706, USA.

Abstract

Deoxyhemoglobin content was measured in hemoglobins from trout, chicken and bovine sources between pH 5.5 and 7.5. With decreasing pH, deoxyhemoglobin content of trout was highest, low to intermediate in chicken, and lowest in beef hemoglobin. Each type of hemoglobin was added to washed cod muscle and lipid oxidation assessed during 2 °C storage. The lipid oxidation rate was trout >> chicken > beef based on thiobarbituric reactive substances (TBARS) and lipid hydroperoxide formation. There was no significant difference in pro-oxidative activity of chicken compared to turkey hemoglobin. Hemoglobins from trout appeared to oxidize more rapidly compared to chicken hemoglobin in the washed cod muscle model system, as measured by a decrease in redness (a-value) during storage. Loss of red color was slowest in beef samples. These studies suggest that deoxyhemoglobin may be a major catalyst of lipid oxidation at post mortem pH values found in muscle foods, especially in fish and poultry compared to beef.

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