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Food Sci. Biotechnol. Vol. 14, No. 1, pp.

152 ~ 163 (2005)

MINIREVIEW
+ The Ko r ean S oci ety of F o od S cien ce and Tech no lo gy

Mechanism of Lipid Peroxidation in Meat and Meat Products -A Review


B. Min and D. U. Ahn
Department of Animal Science, Iowa State University, Ames, IA 50011 Abstract Lipid peroxidation is a primary cause of quality deterioration in meat and meat products. Free radical chain reaction is the mechanism of lipid peroxidation and reactive oxygen species (ROS) such as hydroxyl radical and hydroperoxyl radical are the major initiators of the chain reaction. Lipid peroxyl radical and alkoxyl radical formed from the initial reactions are also capable of abstracting a hydrogen atom from lipid molecules to initiate the chain reaction and propagating the chain reaction. Much attention has been paid to the role of iron as a primary catalyst of lipid peroxidation. Especially, heme proteins such as myoglobin and hemoglobin and free iron have been regarded as major catalysts for initiation, and iron-oxygen complexes (ferryl and perferryl radical) are even considered as initiators of lipid peroxidation in meat and meat products. Yet, which iron type and how iron is involved in lipid peroxidation in meat are still debatable. This review is focused on the potential roles of ROS and iron as primary initiators and a major catalyst, respectively, on the development of lipid peroxidation in Keywords: Lipid peroxidation, mechanism, reactive oxygen species, catalyst, meat meat and meat products. Effects of various other factors such as meat species, muscle type, fat content, oxygen availability, cooking, storage temperature, the presence of salt that affect lipid peroxidation in meat and meat products are also discussed.

Introduction

lipid peroxidation in meat and meat products.

Consumer concerns on the quality of meat and meat Mechanism of lipid peroxidation products have greatly increased during past decades. Quality and healthfulness were reported to be one of Lipid peroxidation is a free radical chain reaction that is the most important factors for influencing consumers comprised of three primary steps: initiation, propagation, choice for foods (1). Three sensory quality characteristics and term ination. Initiation of lipid peroxidation takes place appearance/color, texture, and flavor are the main quality by attack of any species that has sufficient reactivity to attributes that affect consumer acceptance of meat, and abstract a labile hydrogen atom from a methylene group in lipid peroxidation is the primary cause of these quality lipid molecules (LH) to form lipid radicals (L1 ) (Equation deteriorations in meat primarily occurs through a free Lipid peroxidation and meat products (2). 1). radical chain reaction, and oxygen is the most important LH + Initiator1 +L1+ InitiatorH (reduced form) factor on the development of lipid peroxidation in meat (3, (Equation 1) 4). Theoretically, oxygen molecule and polyunsaturated fatty acid (PUFA) cannot interact with each other because Wagner et al. (9) reported that the amount of lipid radical of thermodynamic constraints. Ground state oxygen does generated increased with the total number of bis-allylic not have strong enough reactivity, but can be converted to carbons, and suggested that the number of bis-allylic reactive oxygen species (ROS) such as hydroxyl radical carbons in lipid molecules determines their susceptibility (1 OH), superoxide anion (O21 -), hydrogen peroxide to lipid peroxidation. More importantly, the rate of lipid (H2O21 ), hydroperoxyl radical (HO2 1 ), lipid peroxyl peroxidation exponentially increased with the number of radical (LOO1 ), alkoxyl radical (LO1 ), iron-oxygen bis-allylic carbons although lipid chain length had no complexes (ferryl- and perferryl radical) and singlet relationship with the rate of radical formation. The oxygen (1 O2), some of which are highly reactive to initiate differences in the initiation rate of lipid peroxidation are lipid peroxidation. In addition, numerous agents such as closely related to the dissociation energies of various enzymes and transition metals can directly or indirectly carbon-hydrogen (C-H) bonds in fatty acid chains. The catalyze these oxidative processes through enzymic and weakest C-H bond is at bis-allylic position, whose bond nonenzymic mechanisms. Especially, iron plays a critical energy is 75-80 kcal/mol, and those at allylic position and Many comprehensive reviews on the mechanism of lipid role in lipid peroxidation process as a major catalyst. alkyl C-H bond are 88 kcal/mol and 101 kcal/mol, peroxidation in muscle foods, includin g the major initiators respectively (10, 11). Consequently, the C-H bond at the and catalysts for the oxidative process (5-8), have been published. This review is focused on the potential roles of bis-allylic position is the most reactive site for hydrogen abstraction. The well-known species capable of abstracting reactive oxygen species (ROS) and iron as primary initiators and a major catalyst, respectively, on the development of hydrogen atom are ROS, especially 1 OH. Koppenol (10) estimated that the reduction potential of PUFA radical/ *Corresponding author: Tel: 515-294-6595; Fax: 515-294-9143 PUFA couple was +0.60 V at neutral pH, suggesting that E-mail: duahn@iastate.edu The could be of hydrogen atom (H1 from lipid V) as PUFAabstractionreadily oxidized by 1 )OH (+2.31chain well Received August 24, 2004; accepted October 12, 2004 as other ROS.
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Lipid Oxidation in Meat and Meat Products leaves unpaired electron on the carbon of the chain (L1 ) because H1 has only one electron. This carbon radical tends to be stabilized by a molecular rearrangement to form a conjugated diene. The conjugated diene formed can go through various reactions, depending on O2 concentration in biological system. Under aerobic conditions, the most likely fate of conjugated dienes is to react with oxygen molecules (O2) to form a LOO (Equation 2):

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destruction to form non-radical products. Although LOOH is stable at physiological temperature, it can be decomposed by heating at high temperature or by exposure to transitional metal ions (17). Numerous secondary derivatives of hydroperoxides can be decomposed via homolytic and heterolytic -scission catalyzed by transitional metal ions to generate a huge range of volatile and nonvolatile compounds such as carbonyls (e.g. ketones and aldehydes), alcohols, hydrocarbons (e.g. alkane, alkene), and furans (Equation 2) L1+ O2 LOO1 that contribute to the flavor deterioration in many foods On the other hand, under very low O2 conditions, a (18). Hexanal, 1-octen-3-ol, 2-nonenal, and 4-hydroxy-2conjugated diene can react to each other within the trans-nonenal (HNE) are reported to be originated from nmembranes or other membrane components such as 6 fatty acids and propanal, 4-heptenal, 2,4-heptadienal, 2protein and cholesterol (12). The formation of conjugated hexenal, 2,4,7-decatrienal, 1,5-octadien-3-ol, 2,5-octadiendienes is accompanied by the configuration changes of the 1-ol, 1,5-octadien-3-one, and 2,6-nonadienal are from n-3 double bond from cis to trans form, which may allow fatty acids (5, 19). Among these volatiles, aldehydes are unsaturated fatty acids to pack more tightly, leading to the one of most abundant, and are highly reactive and regarded creation of more rigid domains within bilayer of oxidized as second toxic messengers that disseminate and augment lipid (13). This abnormal conjugated diene can be one of initial free radical reactions (20). Aldehydes generated from the most important markers for lipid peroxidation in lipid peroxidation were reported to be capable of reacting In the propagation step various meat systems. (Equation 3), LOO1 formed is with protein to form adducts which may be related to the able to abstract H1 from another lipid molecule such as deterioration of protein stability and functionality (21). neighboring or surrounding fatty acids to form lipid Also, Lynch and Faustman (22) suggested that aldehydes hydroperoxide (LOOH): increase oxymyoglobin oxidation and prooxidant activity of metmyoglobin and decrease the enzymatic reduction of LOO1 + LH LOOH + L1 (Equation 3) metmyoglobin, which is directly related to the deterioration of meat color and flavor. The primary aldehydes Hydrogen abstraction from a bis-allylic position on the fatty acid chain by LOO1 is favorable with Gibbs free generated during lipid peroxidation in stored beef are energy of -9 kcal/mol (10). In addition, because LOO1 has propanal, pentenal, hexanal, and 4-hydroxynonenal (HNE) a higher standard reduction potential (+1.0V) than lipid molecule itself (+0.60 V) does, it can oxidize favorably an (21). Hexanal among aldehydes is the most prevailing adjacent PUFA. Newly formed L1 can form another LOO1 volatile generated from cooked meat. It has been suggested as an index of meat flavor deterioration (MFD) during by reacting with O2, so the free radical chain reaction can early storage stages of cooked meat because its continue. LOOH is a prominent non-radical intermediate concentration increased more quickly than any other of lipid peroxidation whose identification often provides aldehydes (23). In addition, HNE is known to have valuable information on the related mechanisms. Since Reactiveproperties for human and animals by binding to cytotoxic oxygen species (ROS) in lipid peroxidaLOOHs are more polar molecules than normal fatty acids, tion proteins to inhibit their functions (24). LOOHs can disrupt the integral structure and function of Although oxygen is essential for life, it can cause damages the m embrane, resulting in deleterious effect to cells and to various cells. The toxicity of oxygen is caused not by tissues. LOOHs may undergo various reactions, depending oxygen itself, but by the increased production of ROS. on environments in cell or tissue. Under low hydrogenROS can be produced under normal physiological donating conditions, however, LOOH tends to undergo conditions, but the amounts do not exceed the capacity of further reactions such as combination, intermolecular addi- natural defense systems in body. The reduction of oxygen tion, intramolecular rearrangement, and further reactions molecule by way of one-electron reduction processes with additional O2 molecule, resulting in the formation of produces short-lived but highly reactive oxygen products numerous secondary derivatives such as cyclic peroxides, such as hydroxyl radical (1 OH), superoxide anion (O21 -), prostaglandin-like bicycloendoperoxides, multi-hydroperxyl hydrogen peroxide (H2O2), hydroperoxyl radical (HO21 ), derivatives, etc., double bond isomerization, and formation and iron-oxygen complexes (ferryl and perferryl radical), of dimers and oligomers (14, 15). In addition, another all of which may directly or indirectly participate in lipid complexity of LOOH derivatives formed is caused by the peroxidation processes in meat and meat products. 1 fact that hydrogen abstraction from PUFA can take place Superoxide anion radical (O2 -) and hydroperoxyl 1 at different points on the fatty acid. Especially, hydroperoxyl radical (HO2 ) Superoxide anion radical (O2 1 -) is produced by one-electron reduction of oxygen, which acts cyclic peroxides and bicycloendoperoxides can be precursors of malonaldehyde, 2-thiobarbituric acid reactive substance as an intermediate in a number of biochemical reactions in body. Under physiological conditions, O21 - could be (TBARS). The formation of various LOOHs and their The last step of lipid peroxidation is termination process generated by numerous ways in muscle tissues. One of derivatives possibly produced from primary PUFA has in which the LOO1 s react with each other and/or selfmajor sources of O2 1- in muscle tissues are various been reviewed by others (5, 15, 16).

154
components of electron transport chain in mitochondria such as NADPH-dependent dehydrogenase and ubiquinone which may leak electrons onto O2 (25, 26). The autoxidation of heme proteins (27, 28) and enzymes associated with metabolism such as xanthine oxidase (29) are other major sources. Activation of several leukocytes present in the vasculature of muscle tissue by the internalization of bacteria causes production of O21 -

B. Min and D.U. Ahn


suggested that O21 - in vivo oxidizes the [4Fe-4S] clusters of dehydratases such as mammalian aconitase causing inactivation of enzyme and release of Fe(II) ion. Also, O21 - is suggested to decrease the activity of antioxidant defense enzymes such as catalase and glutathione peroxidase (39). Meanwhile, O21 - is indicated to serve not only as a reducing agent for Fe (III), but also as an oxidant for Fe(II) depending on the ligands or chelators of iron. Ahn et al. (4) and Ahn and Kim (40) in their mechanism study with O2 1 --generating systems associated with various iron sources indicated that O2

because O21 - is one of the major bactericides (30). Superoxide anion radical (O21 -) is a poorly reactive
radical in aqueous solution although it is highly reactive in hydrophobic environments. Hydroperoxyl radical (HO21 ), the protonated form of O21 -, is a more reactive than O21 -

- 1 is a strong oxidant

itself (Equation 4).


HO21 O21 - + H+
The pKa of this reaction is approximately pH 4.8 in aqueous solution. Therefore, less than 1% of O21 -

(Equation 4)

rather than a reducing agent and the antioxidant effect of O21 --generating systems, especially xanthine oxidase system, in oil emulsion is due to the oxidation of Fe(II) to Fe(III) by O2 1- and/or H2O2.

and relatively long half-life of O21 - in cytosol allows it to diffuse more effectively from its generation site to targets such as membrane lipid bilayers than HO21 or other reactive species. Furthermore, much of O2 1 - generated in in red blood cells is probably oxyhemoglobin autoxidation. cell may be produced near m embrane by membrane-boundChan et al. (42) suggested that H2 O2 generated during systems such as electron transport system of mitochondria oxymyoglobin oxidation plays an important role in lipid (25, 26) However, O21 - was suggested not to be able to peroxidation. Harel and Kanner (43) reported that turkey muscle tissues stored at 37oC for 30 minutes generated permeate deep into liposomal bilayer (32). Subsequently, almost 14.0 nmol H2O2 per gram of fresh weight and its some part of O2 1- present near membrane could exist as generation increased with storage at 4o C. HO21 . Uncharged conditions of HO21 , unlike O21 -, allow H2 O2 is not a radical because it has no unpaired it to permeate into membrane lipid bilayer, where it could electron, and has limited reactivity and permeability to initiate lipid peroxidation process by abstracting hydrogen biological membrane unlike the charged O21 - (44). The atom from bis-allylic position of PUFA in phospholipids poor reactivity and relatively long half-life of H2 O2 like (33, 34). Aikens and Dix (35, 36) indicated that the O21 - enables it to diffuse more effectively from its generainitiating effectiveness of HO21 is directly related to the tion site to targets such as membrane lipid bilayers. initial concentration of LOOH in lipids because LOO1 s However, H2O2 can perform most of its dam aging effects generated by either direct or indirect hydrogen atom by generation of more reactive species such as 1 OH by transfer between HO21 and LOOH can initiate lipid catalysis of Fe(II) (45). In addition, H2 O2 can denature peroxidation more efficiently than HO2 1 itself. However, heme proteins to release free irons and heme group or theA major toxicity of superoxide in lipid peroxidation is the evidence for the ability of HO21 to mediate directly convert heme protein to ferryl or perferryl radical, attributed to its radical reduce ionic has which are reinitiation of freeability tochain reactionironsnot been provendepending on its concentration (28) (1 OH) is the OH) Hydroxyl radical oxidized by H2O2 to produce 1 OH (Equations 5 and 6) - Hydroxyl radical (1 yet. most reactive oxygen radical with high positive reduction the most reactive oxygen species that can abstract (39). Usually, steady-state hydrogen atom from bis-allylic position of PUFA chains potentialeffectively zerothe vivo becauseconcentration of or 1 OH is in it would react at and initiates lipid peroxidation (37): close to its site of fo rmation with every molecule in living cell, such as DNA, protein, phospholipid, amino acid, Fe(III)-complex+O21 - Fe(II)-com plex+O2 sugar, etc. as soon as 1 OH is produced. Pryor (46) (Equation 5) Fe(II)-complex+H2 O2 Fe(III)-complex+OH-+1 OH hypothesized that the high reactivity of OH is due to a rare (Equation 6) combination of three characteristics: high electrophilicity, high thermochemical reactivity, and a mode of production In addition, Liochev and Fridovich (37) and Fridovich (38) that can occur near target molecules.

Hydrogen peroxide (H2O2) Low concentrations of hydrogen peroxide (H2O2) are present in aerobic cells as a metabolite under physiological conditions. An O21 -generating system would be expected to yield H2O2 by produced exists in this protonated form under physiological non-enzymatic or superoxide dismutase (SOD)-catalyzed conditions (pH 7.4). The negative charges of membrane dismutation. Hydrogen peroxide (H2O2) generation has surface due to phosphatidyl moiety of phospholipid may been easily detected in mitochondria, microsomes, peroxisomes, and phagocytic cells. Also, several enzymes, cause pH drop around the membrane, resulting in the including aldehyde oxidase, xanthine oxidase, urate increase of O21 - concentration at the membrane surface oxidase, glucose oxidase, glycolate oxidase, and D-amino acid oxidase, etc., can directly produce H2 O2 (7, 17). (31). The pH in muscle tissue after post-rigor also Giulivi et al. (41) reported that H2 O2 is generated at a rate of approximately 3.910-9M/h*g hemoglobin and the decreases from around 7 to 5.5-6.0, so the amount of of H2O2 in the HO21 could be 10-20% of total O21 -. The poor reactivityconcentration 10M, indicating steady-state red blood cells is around 210that the main source of H2O2

156 Lipid Oxidation in Meat and Meat Products

B. Min and D.U. 155 Ahn

in other tissues (73). Meanwhile, presented a direct of Bannister and Thornalley (47) the concentrations level of ~3 mg ascorbate equivalent/100 g of fresh weight, activation of metmyoglobin by electron spin resonance evidence for the generation pork,OH by adrianmycin in ferritin-bound iron in beef, of 1 and chicken thigh 80% of which would be ascorbic species. (ESR) techniques may be a ferrylacid (86). Many studies have tried to determine which form of intact red blood cells using the electron paramagnetic muscles were reported to be 1.2%, 4.6%, and 11.1% of resonanceconcentration in each species,from Most of (68). iron is responsible for the catalysis of the lipid peroxidatechnique of spin trapping. Fe(II)total iron (EPR)in vivo or in situ came respectively the Iron in lipid peroxidation 1 OH generated Ferritin has been suggested to be involved in oxidativeOH tion in meat and meat products. In the beginning, the catalyzed decomposition of H2O2 (45). In addition, 1 Iron is the most heme proteins as catalyzing in biological involvement of abundant transitional metal agents of lipid deterioration by releasing Fe(II) sources: sunlight can also be generated by various in the presence of (48), systems. Although iron has the possibility of various (7). peroxidation was first described by Robinson in 1924 reducing compound such ionizing and ascorbate (74, ultraviolet radiation (49), as O2 1- irradiation (50), the 75), oxidation states (from -II to +VI),heme pigments in meat Many studies have indicated that the forms of Fe(II) and heating, of hypochlorous acid (76, 77, - (51), and reaction or refrigerated storagewith O2170). Hemosiderin Fe(III)pivotal role in in biologicallipid peroxidation in the play a is dominated catalysis of systems. The ability of is an insoluble complex of iron, other sonolysis of water (ultrasound) (52). metals and proteins, iron with various oxidation state, reduction potential, and model systems with various meat species such as beef and and is thought of 1 OH ferritininhibited by 1 OHor polyThe reaction to be a can be decomposition electron spin configuration depending upon different scavengers such as mannitol, formate, thiourea, dimethyl- over fish (87- 90). Rhee and Ziprin (91) showed that the levels merization products (6). In pork and chicken muscles of lipid peroxidation were dependent on multifunctional thiourea, methanol, ethanol, was detected in insoluble fractionligand environments allows it to serve inanimal species a half of total iron (58%) 1-butanol, glucose, tris-buffer, roles as a proteinin raw meat, and beef was more and muscle type cofactor (65). Metal-binding proteins in or sorbitol (17). Although 1 OH scavengersnature of the (68). Although the amount and precise usually inhibit biological system are usually classified by the functional the reaction of 1 OHin muscle is unknown, some of them susceptible to lipid peroxidation than pork and chicken insoluble fraction with other molecules including lipid role of metal ion: structural, total pigment and myoglobin molecules, sometimes they doHemosiderin may There are not act effectively. release its muscle. They proposed that metal-ion storage and may be from hemosiderin. a couple of reasons that should be considered: 1) the transport, electron transport, dioxygen binding, and to bound iron in the presence of reducing agents, resulting in concentrations are well related(84,the differences in lipid Alternatively, (66). raw muscles in 93) suggested of 92, three potential reaction of 1 OH with a scavenger may generate scavenger catalytic proteinstored,However, the versatilespecies. that peroxidation of Kanner et al. the acceleration of 1 OH generation, but isin the lipid peroxidation in minced turkey muscle is primarily radicals that might react with other molecules far less effective iron allows it to catalyze the detrimental oxidation of than ferritin. Therefore, it reactivity of secondary radicals system. The production and was proposed that the conversionbiomolecules suchionic iron protein, lipid, etc. Therefore, affected by free as DNA, and this suggestion was of ferritin to hemosiderin in vivo is biologically favorable confirmed by the chelating ability of ceruloplasmin to low may sometimes be responsible for the unsuccessful proteciron metabolism in vivo should be tightly regulated by because it scavenger (53). 2) More attention to been tion by one reduces the availability of iron haspromote lipid molecular weigh iron. Hydrogen peroxide (H2O2 ) and An extremely small amount of hemosiderin in muscle iron-binding proteins in order to ensure the absence of free paid on the possibility of the metal-mediated site-specific peroxidation (78). The amount of nonprotein-bound iron is ascorbate presented in the cytosol of muscle cells can present has (45):been cytosol iron pool is often considered formsdistribution in tissue Iron is distributed in five Iron of iron existing. mechanism cells. 1 OHknown yet. vivo by the reaction of tissues in not This generated in release free iron from heme pigments and ferritin, H2O2 transit pool because it is related to ironin cells as the with metal ions bound to macromolecules in transit distinct pools, including transport, storage, oxygenrespectively, which can catalyze lipid peroxidation in meat can reactstransferrin and ferritinmolecules or the nearestlow carrying, functional, and low molecular weight irons, between with the metal-binding (71). Although very et al. (94) and Ahn molecules immediately after production before the causes the and meat products (43, 74). Also, Ahn hemoglobin/ myoglobin, solubility of iron under physiological conditions represented by transferrin, ferritin, and Kim (95) suggested that free ionic iron played an scavengers give accesswith anions suchet al. (54) demonto them. Auroma as hydroxyl ion precipitation of iron iron-dependent enzymes, and small transit pool of iron important role in the catalysis of lipid peroxidation, but strated the evidence for the formation of complex of Fe(II) (OH- ), various chelators can increase its solubility signi- chelates, respectively. About two-thirds of body iron is neither transferrin- and ferritin-bound irons nor heme ion and 2-deoxyrebose, suggesting that Fe(II) ion bound to ficantly (79). Thus,O2 to form 1 OH that immediately the intermediate pool of iron is found in hemoglobin, with smaller amounts of myoglobin, DNA reacts with H2 pigments had any catalytic effect in raw turkey muscle. composed of iron associated with low molecular weight various iron-containing enzymes, and transferrin. The rest damages DNA. Baysal et al. (55) suggested that Fe(III) ion They suggested that the status of ionic iron is more chelators such as organic phosphatefree radicals at the is stored protein, binds to membrane and then generates esters (e.g. NAD(P)H, not used for these amount ofin intracellular storage in important than the iron. Ahn and Kim (95) AMP, ADP,Although the inorganic phosphates,iron to acids, ferritin and hemosiderin. Intracellular concentration of free and ATP), specific binding site of amino binding site. their study with oil emulsion systems indicated that Fe(III) The concentrations of myoglobin and hemoglobin in and organic acids (e.g. they suggested is called as ionic iron seems to be extremely small. membrane was not found,citrate), which that carboxyllow catalyzed lipid peroxidation only in thespecies, muscle muscle tissue are dependent on animal presence of groups of sialic acids, sulfate17). The existence of low group of glycolipids and molecular weight iron (6, ascorbic acid while Fe(II) did it alone. In addition, studies glycoproteins, and sulfin poolsulfon group together with molecular weight iron and has been identified in various type, and anatomical location of muscle (67). Both myousing cooked meat model systems containing waterphosphate head group of the in mitochondria for heme globin and hemoglobin-bound iron accounted for 73.3, tissues (80-82) as well as phospholipids are considered extracted muscle of total iron concentration in beef,iron as the major binding sites ontissues, the content of low erythrocyte membrane. 47.0, and 28.5% fractions indicated that nonheme pork, synthesis (83). In muscle released from heme pigments and ferritin by heating is the Gutteridge (56) indicated that 1 OH scavengers inhibited molecular weight iron accounts for 2.4~3.9% of total iron, and chicken thigh meat, respectively (68). Myoglobin 1 OH generation effectively in the presence of EDTA principal catalyst rather than myoglobin (76, 77, 96). because EDTA may allow Fe(II) ions to be removed from depending on animal species and muscle types (68), and (70%) is the predominant iron compound in beef. these binding site. Therefore, the actual toxicity of O21 Therefore, these researches indicated that free ionic iron the concentration can be influenced by heating and in the Myoglobin accounts for most of heme iron in beef and released from heme pigments and ferritin may be presence may be dependent on H2O2 (69) and storage (84). pork, but the level of(97) suggested chicken breast and Kanner and the major catalyst for that ferryl species in Harel myoglobin in lipid peroxidation and H2O2of ascorbic acid and the availability and considered asis very low. Meanwhile, Schricker and Miller thigh muscle the interaction of H2O2 with metmyoglobin generated by distribution of metal ion catalysts to generateof intermediate Neither the size nor the chemical nature 1 OH in cells. raw and cooked meat. heating or addition of H2 O2 caused (69) suggested thatcan initiate lipid peroxidation in muscle Importance of iron as a catalyst for initiation of lipid or methemoglobin the pool of iron has been clearly identified. peroxidation the release of heme iron due to oxidative cleavage of Iron-oxygen complexes (ferryl and perferryl radical) The tissue. They showed that H2 O2 alone or metmyoglobin ferryl [Fe(IV)] and perferrylthe initiation mechanism of lipid Nonenzymic catalysis: [Fe(V)] radicals are porphyrin ring of heme. Han et al (70) reportedsarcosomal alone could not stimulate oxidation reaction in that the catalytically active in numerous biological processes, and is the most peroxidation is still an area of controversy. Iron iron content in water-soluble fractions of heated beef and fraction of turkey dark muscle whereas the membranal these ferryl/perferryl moiety, whether as components of probable catalyst complex, can be very powerful enzyme or simple ironfor the initiation of lipid peroxidation by chicken thigh muscle decreased due to the reduction of of lipid peroxidation was readily promoted in the presence catalyzing the generation hydrogen atom in lipid oxidants capable of abstracting of most 1 OH in vivo or in vitro heme iron content, but that in water insoluble fractions peroxidation (57). It has been indicated6) and oxidizing by reducing H2O2 and metmyoglobin. H2O2- or cumene hydroperoxidethat an is cycled via Fenton reaction (Equation increased metmyoglobin was shown iron transport and intermediate generated in Fe(II)-EDTA-H2O2 system does activated because ferritin are major to protein was also Transferrin and the denatured heme catalyze lipid agents such characteristic reactions of OH (37, 85). not undergo theas O21 - and ascorbic1acidbut shows In general,included in insoluble fraction. peroxidation in model systems containing PUFA (98, 99). storage proteins, which are capable of binding two and a pattern ofacid can serve as both an antioxidant and a ascorbic reaction more associated with ferryl complex Also, Fe(III) ion at a metmyoglobin was reported to be (58, 59). Also, itdepending on relative concentrations of ascorbate has been suggested that the reaction of ~2500H2O2- activatedtime, respectively. The structure, prooxidant, metmyoglobin and methemoglobin with low concentration able to oxidize a series role, and relationship phenols, function, physiological of compounds such asto oxidative and generates a short-lived ferryl species that concentration is H2O2iron present (6). Ascorbate at low contain one carotene, of them are well reviewed by Crichton and oxidizing equivalent on heme and another one on globin, muscle tissue processes methional, reducing agents, and uric acid (61, most likely to promote lipid peroxidation in and is not affected by all efficient 1 OH scavengers (60-63). 100). The ratio of H2O2 to metmyoglobin seemed al be Charloteaux-Wauters (71), Reif (72), and Welch et to (65). by the (64) reported that free radicals generated by H2O2 Xu et al. reduction of iron, whereas at high concentration it important the role of transferrin as ferryl species. Rhee However, for the generation of the a catalyst for lipid et tends to reduce some of LOO1 directly to LOOH, al. (101) demonstrated that the catalytic activity of resulting in breaking the free radical chain reactions and peroxidation has not been yet demonstrated in muscle metmyoglobin-H2O2 treatment was the highest at the also regenerates a-tocopherol in biological membrane. In tissues although released irons from transferrin were molar ratio of ~1:0.25 in raw microsomal system of beef turkey muscle, reducing compounds were observed at the suggested to be participated in lipid peroxidation process and at the molar ratio of 1:1.5 or 1:2 in the cooked system