Acknowledgement
This study was supported by National Natural Science Foundation of China (31972137), China Agriculture Research System (CARS-41), Primary Research & Development Plan of Jiangsu Province (BE2017392), the Priority Academic Program Development of Jiangsu Higher Education Institutions, Overseas Expertise Introduction Center for Discipline Innovation (111 Center) On Quality & Safety Control and Nutrition of Muscle Food (B14023).
References
- Ordway GA, Garry DJ. Myoglobin: an essential hemoprotein in striated muscle. J Exp Biol 2004;207:3441-6. https://doi.org/10.1242/jeb.01172
- Giaretta N, Giuseppe AMAD, Lippert M, Parente A, Maro AD. Myoglobin as marker in meat adulteration: a UPLC method for determining the presence of pork meat in raw beef burger. Food Chem 2013;141:1814-20. https://doi.org/10.1016/j.foodchem.2013.04.124
- Suman SP, Joseph P. Myoglobin chemistry and meat color. Annu Rev Food Sci Technol 2013;4:79-99. https://doi.org/10.1146/annurev-food-030212-182623
- Carlsen CU, Moller JKS, Skibsted LH. Heme-iron in lipid oxidation. Coord Chem Rev 2005;249:485-98. https://doi.org/10.1016/j.ccr.2004.08.028
- Maitra D, Byun J, Andreana PR, et al. Reaction of hemoglobin with HOCl: mechanism of heme destruction and free iron release. Free Radic Biol Med 2011;51:374-86. https://doi.org/10.1016/j.freeradbiomed.2011.04.011
- Min B, Cordray JC, Ahn DU. Effect of NaCl, myoglobin, Fe (II), and Fe (III) on lipid oxidation of raw and cooked chicken breast and beef loin. J Agric Food Chem 2010;58:600-5. https://doi.org/10.1021/jf9029404
- Grunwald EW, Richards MP. Studies with myoglobin variants indicate that released hemin is the primary promoter of lipid oxidation in washed fish muscle. J Agric Food Chem 2006; 54:4452-60. https://doi.org/10.1021/jf0603228
- Mokrani A, Krisa S, Cluzet S, et al. Phenolic contents and bioactive potential of peach fruit extracts. Food Chem 2016; 202:212-20. https://doi.org/10.1016/j.foodchem.2015.12.026
- Sorensen G, Jorgensen SS. A critical examination of some experimental variables in the 2-thiobarbituric acid (TBA) test for lipid oxidation in meat products. Z Lebensm Unters Forsch 1996;202:205-10. https://doi.org/10.1007/BF01263541
- Meullenet JF, Jonville E, Grezes D, Owens CM. Prediction of the texture of cooked poultry pectoralis major muscles by near-infrared reflectance analysis of raw meat. J Texture Stud 2004;35:573-85. https://doi.org/10.1111/j.1538-7836.2004.01165.x-i1
- Bertram HC, Oksbjerg N, Young JF. NMR-based metabonomics reveals relationship between pre-slaughter exercise stress, the plasma metabolite profile at time of slaughter, and waterholding capacity in pigs. Meat Sci 2010;84:108-13. https://doi.org/10.1016/j.meatsci.2009.08.031
- Lan X, Zhang X, Zhou G, Wu C, Li C, Xu X. Electro-acupuncture reduces apoptotic index and inhibits p38 mitogen-activated protein kinase signaling pathway in the hippocampus of rats with cerebral ischemia/reperfusion injury. Neural Regen Res 2017;12:409-16. https://doi.org/10.4103/1673-5374.202944
- Gueraud F, Atalay M, Bresgen N, et al. Chemistry and biochemistry of lipid peroxidation products. Free Radic Res 2010; 44:1098-124. https://doi.org/10.3109/10715762.2010.498477
- Yu Y, Mukherjee A, Nilges MJ, Hosseinzadeh P, Miner KD, Lu Y. Direct EPR observation of a tyrosyl radical in a functional oxidase model in myoglobin during both H2O2 and O2 reactions. J Am Chem Soc 2014;136:1174-7. https://doi.org/10.1021/ja4091885
- Rhee KS, Ziprin YA. Lipid oxidation in retail beef, pork and chicken muscles as affected by concentrations of heme pigments and nonheme iron and microsomal enzymic lipid peroxidation activity. J Food Biochem 1987;11:1-15. https://doi.org/10.1111/j.1745-4514.1987.tb00109.x
- Roginsky V, Zheltukhina GA, Nebolsin VE. Efficacy of metmyoglobin and hemin as a catalyst of lipid peroxidation determined by using a new testing system. J Agric Food Chem 2007;55:6798-806. https://doi.org/10.1021/jf0714362
- Vernier G, Chenal A, Vitrac H, Barumandzadhe R, Montagner C, Forge V. Interactions of apomyoglobin with membranes: mechanisms and effects on heme uptake. Protein Sci 2007;16: 391-400. https://doi.org/10.1110/ps.062531207
- Baron CP, Andersen HJ. Myoglobin-induced lipid oxidation. A review. J Agric Food Chem 2002;50:3887-97. https://doi.org/10.1021/jf011394w
- Mozuraityte R, Rustad T, Storro I. The role of iron in peroxidation of polyunsaturated fatty acids in liposomes. J Agric Food Chem 2008;56:537-43. https://doi.org/10.1021/jf0716073
- Cheng Z, Li Y. What is responsible for the initiating chemistry of iron-mediated lipid peroxidation: an update. Chem Rev 2007;107:748-66. https://doi.org/10.1021/cr040077w
- Giri RP, Mukhopadhyay MK, Basak UK, et al. Continuous uptake or saturation- investigation of concentration and surface-packing-specific hemin interaction with lipid membranes. J Phys Chem B 2018;122:7547-54. https://doi.org/10.1021/acs.jpcb.8b03327
- Faustman C, Sun Q, Mancini R, Suman SP. Myoglobin and lipid oxidation interactions: mechanistic bases and control. Meat Sci 2010;86:86-94. https://doi.org/10.1016/j.meatsci.2010.04.025
- Zhou C, Tan S, Li J, Chu X, Cai K. A novel method to stabilize meat colour: ligand coordinating with hemin. J Food Sci Technol 2014;51:1213-7. https://doi.org/10.1007/s13197-012-0625-z
- Zhang W, Xiao S, Ahn DU. Protein oxidation: basic principles and implications for meat quality. Crit Rev Food Sci Nutr 2013;53:1191-201. https://doi.org/10.1080/10408398.2011.577540
- Lund MN, Luxford C, Skibsted LH, Davies MJ. Oxidation of myosin by haem proteins generates myosin radicals and protein cross-links. Biochem J 2008;410:565-74. https://doi.org/10.1042/BJ20071107
- Malheiros JM, Braga CP, Grove RA, et al. Influence of oxidative damage to proteins on meat tenderness using a proteomics approach. Meat Sci 2019;148:64-71. https://doi.org/10.1016/j.meatsci.2018.08.016
- Shao JH, Deng YM, Jia N, et al. Low-field NMR determination of water distribution in meat batters with NaCl and polyphosphate addition. Food Chem 2016;200:308-14. https://doi.org/10.1016/j.foodchem.2016.01.013
- Huff-Lonergan E, Lonergan SM. Mechanisms of water-holding capacity of meat: the role of postmortem biochemical and structural changes. Meat Sci 2005;71:194-204. https://doi.org/10.1016/j.meatsci.2005.04.022
- Barbut S, Zhang L, Marcone M. Effects of pale, normal, and dark chicken breast meat on microstructure, extractable proteins, and cooking of marinated fillets. Poult Sci 2005; 84:797-802. https://doi.org/10.1093/ps/84.5.797
- Zhang WG, Lonergan SM, Gardner MA, Huff-Lonergan E. Contribution of postmortem changes of integrin, desmin and μ-calpain to variation in water holding capacity of pork. Meat Sci 2006;74:578-85. https://doi.org/10.1016/j.meatsci.2006.05.008
- Wang Z, He Z, Emara AM, Gan X, Li H. Effects of malondialdehyde as a byproduct of lipid oxidation on protein oxidation in rabbit meat. Food Chem 2019;288:405-12. https://doi.org/10.1016/j.foodchem.2019.02.126
- Lai JF, Dobbs J, Dunn MA. Evaluation of clams as a food source of iron: total iron, heme iron, aluminum, and in vitro iron bioavailability in live and processed clams. J Food Compost Anal 2012;25:47-55. https://doi.org/10.1016/j.jfca.2011.07.004