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Effects of aldehyde products of lipid oxidation on the color stability and metmyoglobin reducing ability of bovine Longissimus muscle
Author(s) -
Chen Cheng,
Yu Qunli,
Han Ling,
Zhang Jiaying,
Guo Zhaobin
Publication year - 2018
Publication title -
animal science journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.606
H-Index - 38
eISSN - 1740-0929
pISSN - 1344-3941
DOI - 10.1111/asj.12993
Subject(s) - metmyoglobin , lipid oxidation , chemistry , biochemistry , electron transport chain , mitochondrion , aldehyde , myoglobin , biophysics , biology , antioxidant , catalysis
Lipid oxidation and metmyoglobin ( MM b) reduction are popular issues in meat color research. This study evaluated the effects of aldehyde products, particularly 4‐hydroxy‐2‐nonenal ( HNE ) and hexenal, of lipid oxidation on the oxymyoglobin stability, mitochondrial membrane permeability, MM b reduction ability, electron transport chain‐mediated MM b reduction, and nicotinamide adenine dinucleotide reduced form ( NADH) ‐dependent MM b reductase activity of bovine Longissimus muscle. The results indicated that HNE and hexenal accelerate the oxidation rate of oxymyoglobin, significantly increase the permeability of the mitochondrial membrane, and inhibit electron transport chain‐mediated MM b reduction. However, HNE and hexenal were found to exert no effect on the activity of NADH ‐dependent MM b reductase. Thus, the aldehyde products of lipid oxidation could damage the microstructure of mitochondria and inhibit mitochondria‐mediated MM b reduction, which is disadvantageous in terms of the color stability of fresh bovine Longissimus muscle.