Effects of aldehyde products of lipid oxidation on the color stability and metmyoglobin reducing ability of bovine Longissimus muscle. (20th February 2018)

• Record Type: Journal Article
• Authors: Chen, Cheng; Yu, Qunli; Han, Ling; Zhang, Jiaying; Guo, Zhaobin
• Is Part Of: Animal science journal. Volume 89:Number 5(2018)
• Page Start: 810
• Page End: 816
• Publication Date: 2018-02-20
• Subjects: bovine Longissimus muscle -- color -- metmyoglobin -- oxymyoglobin -- stability; Animal culture -- Periodicals; Livestock -- Periodicals; 636
• DOI: 10.1111/asj.12993
• Languages: English
• ISSNs: 1344-3941

Abstract

Abstract: Lipid oxidation and metmyoglobin (MMb) 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, MMb reduction ability, electron transport chain‐mediated MMb reduction, and nicotinamide adenine dinucleotide reduced form (NADH)‐dependent MMb 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 MMb reduction. However, HNE and hexenal were found to exert no effect on the activity of NADH‐dependent MMb reductase. Thus, the aldehyde products of lipid oxidation could damage the microstructure of mitochondria and inhibit mitochondria‐mediated MMb reduction, which is disadvantageous in terms of the color stability of fresh bovine Longissimus muscle.