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Elucidating Aldehyde-induced Redox Instability in Carboxymyoglobin
Department of Animal and Food Sciences
The ferrous forms of myoglobin - oxymyoglobin (OxyMb) and carboxymyoglobin (COMb) provide desirable cherry-red color critical for consumer acceptance of fresh red meat. This proposal is designed to understand the influence of lipid oxidation on meat discoloration, in carbon monoxide containing modified atmosphere packaging.
2009 Project Description
In 2009, we completed part of objective #2. Tandem mass spectrometry was utilized to determine the sites of adduction of 4-hydroxy-2-nonenal (HNE), a reactive lipid oxidation product, in carboxymyoglobin at pH 7.4, 37°C, in comparison with oxymyoglobin. Equine carboxymyoglobin and oxymyoglobin (0.15 mM) were incubated with HNE (1.0 mM) at pH 7.4 and 37°C for 6 hours (physiological condition). The samples were passed through desalting column to remove excess HNE and were subjected to tryptic digestion. The tryptic peptides were analyzed using tandem mass spectrometry. Analyses of tandem mass spectra revealed that HNE formed adducts only with histidines in carboxymyoglobin and oxymyoglobin. Histidine residues at positions 24, 36, 48, 81, and 93 were adducted in both carboxymyoglobin as well as oxymyoglobin.
Lipid oxidation compromises flavor and color of meat. Reactive secondary products of lipid oxidation induce redox instability in myoglobin, which leads to meat discoloration. Although previous studies reported lipid oxidation-induced discoloration in carboxymyoglobin, the molecular basis for interactions between carboxymyoglobin and reactive lipid oxidation product (HNE) is not completely understood. Determination of amino acid residues susceptible to HNE adduction in carboxymyoglobin is necessary to elucidate the molecular basis of lipid oxidation-induced discoloration in red meats stored in carbon monoxide modified atmosphere packaging.
Joseph, P.; Suman, S.P.; Mancini, R.A; Beach, C.M. 2009. Mass spectrometric evidence for aldehyde adduction in carboxymyoglobin. Meat Science 83: 339-344.
Suman, S.P.; Joseph, P.; Li, S.; Steinke, L.; Fontaine, M. 2009. Primary structure of goat myoglobin. Meat Science 82: 456-460.
Suman, S.P.; Mancini, R.A.; Ramanathan, R.; Konda, M.R. 2009. Effect of lactate-enhancement, modified atmosphere packaging, and muscle source on the internal cooked color of beef steaks. Meat Science 81: 664-670.
Joseph, P.; Suman, S.P.; Li, S.; Xiong, Y.L.; Webster, C.D.; Thompson, K.R.; Metts, L.S. 2009. Fishmeal-based diet decreases red color of sunshine bass (Morone chrysops x Morone saxatilis) fillets. LWT-Food Science and Technology 42: 730-734.
Suman, S.P.; Mancini, R.A.; Konda, M.R.; Ramanathan, R.; Joseph, P. Effects of packaging and lactate on ground beef cooked color. In proceedings of 55th International Congress of Meat Science and Technology, August 2009, Copenhagen, Denmark. Paper # 137.
Joseph, P.; Suman, S. P.; Mancini, R. A.; Beach, C. M. Mass spectrometric investigations on lipid oxidation-induced carboxymyoglobin oxidation. American Meat Science Association Annual Reciprocal Meat Conference, June 2009, Rogers, AR. Abstract # 3.
Joseph, P.; Suman, S. P.; Li, S.; Steinke, L.; Fontaine, M.; Claus, J. R. Partial amino acid sequence of turkey myoglobin. American Meat Science Association Annual Reciprocal Meat Conference, June 2009, Rogers, AR. Abstract # 92.
Joseph, P.; Suman, S. P.; Li, S.; Beach, C. M.; Steinke, L.; Fontaine, M. Primary structure and oxidative stability of bison myoglobin. American Meat Science Association Annual Reciprocal Meat Conference, June 2009, Rogers, AR. Abstract # 93.
Joseph, P.; Suman, S.P.; Li, S.; Xiong, Y.L.; Webster, C.D.; Thompson, K.R.; Metts, L.S. Influence of fishmeal-based diet on quality attributes of hybrid striped bass fillets during frozen storage. Institute of Food Technologists Annual Meeting, June 2009, Anaheim, CA. Abstract # 027-05.