The effects of HNE on ovine oxymyoglobin redox stability in a microsome model

The effect of 4-hydroxy-2-nonenal (HNE), a secondary lipid oxidation product, on ovine myoglobin (Mb) redox stability was investigated. HNE increased oxymyoglobin (OxyMb) oxidation under all pH/temperature conditions studied. Mono-, di- and tri-HNE adducts were detected by ESI-Q-TOF MS analysis. Sit...

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Veröffentlicht in:	Meat science 2013-10, Vol.95 (2), p.224-228
Hauptverfasser:	Yin, Shuang, Faustman, Cameron, Tatiyaborworntham, Nantawat, Ramanathan, Ranjith, Sun, Qun
Format:	Artikel
Sprache:	eng
Schlagworte:	4-Hydroxy-2-nonenal Aldehydes - adverse effects alpha-Tocopherol - pharmacology Animals Chromatography, Liquid Histidine - metabolism Hydrogen-Ion Concentration Lipid Metabolism - drug effects Lipid oxidation Meat color Microsome Microsomes - drug effects Microsomes - metabolism Myoglobin Myoglobin - chemistry Ovine Oxidation-Reduction - drug effects Sheep, Domestic Tandem Mass Spectrometry Temperature
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Zusammenfassung:	The effect of 4-hydroxy-2-nonenal (HNE), a secondary lipid oxidation product, on ovine myoglobin (Mb) redox stability was investigated. HNE increased oxymyoglobin (OxyMb) oxidation under all pH/temperature conditions studied. Mono-, di- and tri-HNE adducts were detected by ESI-Q-TOF MS analysis. Sites of adduction, His 120, His 25 and His 65, were determined by ESI–CID–MS/MS analysis. The relationship between ovine Mb (with/without HNE) and lipid oxidation was also studied in a microsome model in the presence of α-tocopherol. Surprisingly, preincubation of Mb with HNE did not affect subsequent Mb redox stability in the microsome model (P
ISSN:	0309-1740 1873-4138
DOI:	10.1016/j.meatsci.2013.04.055