4.7 Article

Factors Affecting Lipid Oxidation Due to Pig and Turkey Hemolysate

Journal

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 65, Issue 36, Pages 8011-8017

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.7b02764

Keywords

oxidative rancidity; protein crystallography; poultry; swine; myoglobin

Funding

  1. National Institute of Food and Agriculture, U.S. Department of Agriculture [2014-67017-21648]
  2. China Scholarship Council (CSC)
  3. Nanjing Agricultural University

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Turkey hemolysate promoted lipid oxidation in washed muscle more effectively than pig hemolysate, which was partly attributed to the greater ability of H2O2 that formed during auto-oxidation to oxidize the avian hemoglobin (Hb). Turkey and pig hemcilysate (2.5 mu M Hb) exposed to 10 mu M H2O2 oxidized to 48% and 4% metHb, respectively. Catalase activity, which converts H2O2, to water, was elevated in the pig hemolysate. The larger difference in Hb oxidation when comparing turkey and pig hemolysate in washed muscle (relative to their auto-oxidation rates) suggested that lipid oxidation products facilitated formation of metHb. Turkey metHb released hemin more readily than pig metHb, which coincided with turkey metHb promoting lipid oxidation more effectively than pig metHb. Ferryl Hb was not detected during storage of turkey or pig hemolysate in washed muscle, which suggested a minor role for hypervalent forms of Hb in the oxidation of the lipids.

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