Role of peroxidation and heme catalysis in coloration of raw meat

Abstract

Lipid peroxidation (LPO) alongside with other processes of post mortem metabolism is decisive for quality formation of meat products. Phenomena encountered in meat raw materials as a result of LPO can be summarized under three headings: 1 -those affecting safety (formation of malonic dialdehyde, fatty acids peroxides, oxidized cholesterol etc); 2 -those affecting biological value (lowering the content of non-replaceable fatty acids and vitamins, oxidative amino-acid decomposition, decrease of protein digestibility); 3 -those affecting technological quality parameters (decrease of protein solubility, colour and fl avour changes, as well as appearance of a typical odour). MEAT COLOUR AND ITS NATUREAmong the meat quality parameters affecting its salability, colour plays a special role. The colour of meat depends on the content and physical and chemical changes of hemoglobin and myoglobin (Mb) -complex proteins of hemoprotein group contained ROLE OF PEROXIDATION AND HEME CATALYSIS IN COLORATION OF RAW MEAT ABSTRACTIt is known, that lipid peroxidation is one of the main factors limiting the quality and acceptability of meat and other animal tissues. The current data concerning connection of heme and peroxidation were summarized and analysed here. The muscle food compounds that are most infl uenced by oxidative processes include unsaturated fatty acids of lipids, amino acids of proteins and heme groups of pigments. Heme proteins and particularly myoglobin are abundant in muscle tissues. Meat colour is primarily infl uenced by the concentration and chemical state of heme pigments, myoglobin and hemoglobin. Oxygenated myoglobin oxidized to the brown metmyoglobin form and its accumulation is highly correlated with progress of lipid peroxidation. Heme proteins such as hemoglobin or myoglobin accelerate the decomposition of hydroperoxides to free radicals. Metmyoglobin possesses «pseudoperoxidase» activity and catalyzes the oxidation of various compounds following the reaction with hydrogen peroxide. The reaction between hydrogen peroxide and metmyoglobin results in the formation of two active hypervalent myoglobin species, perferrylmyoglobin (•MbFe lV =O) and ferrylmyoglobin (MbFe lV =O), which participate in lipid oxidation catalysis. Both MbFe lV =O and •MbFe lV =O are deactivated in the presence of reducing agents, whose nature determines the overall effect of the pseudoperoxidase cycle. Hypothesis can be put forward that loss of cellular antioxidants might precede the rise of peroxidase-like activity, thus being a sign of incipient discoloration of meats and muscle components of foods.

Chemical characteristics and volatile compounds profiles in different muscle part of the farmed hybrid catfish (Clarias macrocephalus × Clarias gariepinus)

“…Haem protein has the ability to speed up the decomposition of peroxides, resulting in the formation of secondary aldehydic lipid oxidation products. When haem proteins like haemoglobin or myoglobin interact with lipid hydroperoxides, they cause the hydroperoxide to decompose into free radicals or reactive aldehyde compounds (Maestre et al., 2009; Shleikin and Medvedev, 2014; Chaijan and Panpipat, 2017). Although the PV of dorsal muscle was lower than that of ventral muscle ( P < 0.05), their TBARS content was comparable ( P > 0.05) (Table 1).…”

Mechanisms of Oxidative Processes in Meat and Toxicity Induced by Postprandial Degradation Products: A Review

“…The high tendency of unsaturated fatty acids, especially polyunsaturated fatty acids, to rapidly oxidize is important in further biochemical changes that have undesirable effects, such as rancidity and color deterioration (Wood and others ). The unsaturated fatty acyl group of phospholipids from muscle fiber membranes (sarcolemma, mitochondria, and sarcoplasmic reticulum) is the 1st to be oxidized (Morrissey and others ; Shleikin and Medvedev ). Turkki and Campbell () have studied the distribution of phospholipids in 2 beef muscles and suggested that in both muscles lecithin accounted for about 62%, cephalins for 30%, and sphingomyelins for less than 10%.…”

“…More studies were undertaken to determine in which form iron is responsible for the catalysis of the lipid peroxidation in meat and meat products. In experimental models with various meat species, such as beef and fish, many researchers have indicated that iron from meat heme proteins plays a crucial role in catalysis of lipid peroxidation (Rhee and Ziprin ; Min and Ahn ; Min and others ; Gheisari and others ; Shleikin and Medvedev ). Rhee and Ziprin () studied lipid peroxidation, myoglobin concentration, and total pigment in pork, beef, and chicken raw muscles during 2 to 6 d of storage and they concluded that the lipid peroxidation intensity was dependent on animal species and muscle type.…”

Muskox myoglobin: purification, characterization and kinetics studies compared with cattle and water buffalo myoglobins

“…Mb oxidized to the brown MetMb form and its accumulation is highly correlated with the progression of lipid peroxidation (LPO), another process of post mortem metabolism that is decisive for meat quality. Indeed, the pseudoperoxidase activity of MetMb that catalyses the oxidation of various compounds in the presence of H 2 O 2 is highly correlated with LPO progression, which is one of the main factors limiting the quality and acceptability of meat …”

“…Indeed, the pseudoperoxidase activity of MetMb that catalyses the oxidation of various compounds in the presence of H 2 O 2 15,16 is highly correlated with LPO progression, which is one of the main factors limiting the quality and acceptability of meat. 11,17…”