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Attributes of lipid oxidation due to bovine myoglobin, hemoglobin and hemolysate

Jie Yin1, Wenjing Zhang1, Mark P Richards1

  • 1Meat Science and Muscle Biology Laboratory, Department of Animal Sciences, University of Wisconsin-Madison, Madison, WI 53706, USA.

Food Chemistry
|May 29, 2017
PubMed

Bovine hemolysate was purified by size exclusion chromatography, and one high molecular weight protein was detected relative to the hemoglobin (Hb) fraction. Purified Hb promoted lipid oxidation in washed muscle slightly but significantly better than hemolysate, which may have been due to the absence of catalase and peroxiredoxin in the purified Hb. Purified Hb auto-oxidized to metHb more rapidly than Hb in the hemolysate (P<0.05). OxyHb promoted lipid oxidation in washed muscle more effectively compared to oxyMb (P<0.05). This was ascribed to hemin, released from metHb, promoting lipid oxidation more readily than oxidative forms of Mb that retain their protoporphyrin moiety. A 3:1 ratio of Mb:Hb promoted lipid oxidation similarly compared to adding a 1:1 ratio of Mb:Hb to washed muscle. Lipid oxidation products due to Hb-mediated lipid oxidation were elevated 60-fold at pH 6.3 compared to pH 6.7.

Keywords:
BeefHemolysateLipid oxidationSEC-purificationoxyHboxyMb

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