What Is a Cell Organelle? Chicken on a Beef

Inquiry Article

Role of Mitochondria in Beef Color: A Review

Authors: Ranjith Ramanathan (Oklahoma State Academy) , Richard A. Mancini (University of Connecticut)

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  Research Article

  Role of Mitochondria in Beef Color: A Review

  Authors: Ranjith Ramanathan (Oklahoma Land University) , Richard A. Mancini (University of Connecticut)

Abstract

In postmortem muscle, mitochondria remain active and can influence beefiness color by oxygen consumption and metmyoglobin reduction. Enzymes involved in glycolysis and the tricarboxylic acid cycle can generate reducing equivalents such as succinate or NADH. Mitochondrial action is disquisitional to maintain steaks that are vivid cherry-red and meliorate color stability. This review seeks to narrate the role of mitochondria in beef colour; more specifically to empathise the effects of mitochondrial function on myoglobin redox stability.

Keywords: beef color, myoglobin, MRA, mitochondria, oxygen consumption

How to Cite:

Ramanathan, R. & Mancini, R. A., (2018) "Role of Mitochondria in Beef Color: A Review", Meat and Muscle Biology 2(1). doi: https://doi.org/10.22175/mmb2018.05.0013

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Introduction

Visual perception plays an important office in the acceptability of food products. This is particularly relevant to beef purchasing decisions considering consumers associate bright-red lean with freshness and wholesomeness. Discoloration of meat has resulted in an annual loss of $1 billion to the U.S. meat manufacture (Smith et al., 2000). Although discoloration is inevitable, understanding the biochemical pathways that influence myoglobin redox chemical science can aid processors to develop strategies that improve colour stability. Several reviews (Giddings, 1977; Faustman and Cassens, 1990; Cornforth, 1994; Bekhit and Faustman, 2005; Mancini and Hunt, 2005) have discussed in detail the factors affecting discoloration, yet, no published reviews take focused specifically on the function of mitochondria in meat color. Hence, the objective of this review was to provide an overview of the interrelationship amongst mitochondria, myoglobin, and beef color.

Myoglobin chemistry

Myoglobin is the water-soluble sarcoplasmic protein responsible for meat color. The globular structure of myoglobin contains 153 amino acids equanimous of 8 α-helices and a heme prosthetic group in the protein's eye. The apo-poly peptide portion of myoglobin is colorless and therefore, the heme prosthetic grouping imparts colour (Giddings, 1977). The heme moiety is located inside myoglobin's hydrophobic pocket and contains a central iron cantlet that can grade 6 bonds. Four of these bonds are coordinated with pyrrole nitrogens, the 5th coordinates with the proximal histidine of myoglobin, and the 6th position is bachelor to bind ligands. Both the proximal and the distal histidine play a significant role in stabilizing the heme and the ligand bound to myoglobin. More specifically, the proximal histidine coordinates the heme ring and the distal histidine stabilizes the heme-oxygen circuitous (American Meat Science Clan, 2012).

The valence state and the ligand present at the sixth position determine meat color. In fresh beef, myoglobin tin can exist in three forms: deoxymyoglobin, oxymyoglobin, and metmyoglobin. Deoxymyoglobin is formed when no ligand occupies the sixth position and fe is in the ferrous land. This results in purplish color and occurs mainly in vacuum-packaged meat. An oxygen tension of less than 1.4 mm Hg is required to maintain deoxymyoglobin (Ledward, 1970). Oxymyoglobin produces a bright cherry-reddish color and is formed when oxygen binds to the 6th position of myoglobin'due south centrally located iron. Oxidation of oxymyoglobin results in brown metmyoglobin, which has ferric atomic number 26 and water occupies the 6th position. Aggregating of metmyoglobin results in surface discoloration.

The introduction of case-ready packaging has immune beef purveyors to modify the gas compositions within packages. This has generated interest in the use of carbon monoxide at a level of 0.four% in depression-oxygen packaging (FDA, 2004). Carboxymyoglobin can form a stable red color due to stiff binding of carbon monoxide to the 6th position of iron. More specifically, binding of oxygen to iron results in a bent configuration with the distal histidine while carbon monoxide forms a stable linear configuration with atomic number 26 and the distal histidine (Makinen et al., 1979).

The processes that regulate the interconversion among myoglobin redox states determine beefiness color. Oxygen consumption and metmyoglobin reducing activity (MRA) are 2 important biochemical properties that influence myoglobin redox state and are influenced past mitochondrial function (Figure one).

Effigy 1.

Effects of oxygen consumption and metmyoglobin reducing activity on redox grade of myoglobin in fresh beef. OC = oxygen consumption; MRA = metmyoglobin reduction activity.

Mitochondria and postmortem oxygen consumption

Mitochondria are double membrane-bound organelles ranging from one to x micrometers and are responsible for cellular respiration (Stevens, 1981). The outer membrane is a phospholipid bilayer completely surrounding the organelle and is readily permeable to ions and pocket-sized molecules. The electron transport complex, ATP synthase complex, and transport proteins are present in the inner membrane. Between the inner and outer membranes is the inter-membrane space. The inner membrane is highly convoluted, permeable to oxygen and water, and folded to form cristae that increase surface expanse (Frey and Mannellab, 2000). The mitochondrial matrix contains enzymes for the tricarboxylic acid bike and contains about 2/3 of the total protein present in mitochondria.

The inner membrane contains complexes and proteins involved in the electron transport chain, including various fat-soluble electron carrier proteins such as ubiquinone, cytochromes, and atomic number 26-sulfur proteins. At that place are iv enzyme complexes within the electron transport chain, each of which transfer electrons from reducing equivalents such every bit NADH and FADH₂ to NADH-Coenzyme Q reductase (complex I), succinate dehydrogenase (complex 2), and to cytochrome bc ₁ (complex Iii) and cytochrome c oxidase (complex IV; Scheffler, 2007). Oxygen is consumed at complex IV to form water.

Mitochondria go along to metabolize oxygen in postmortem muscle, although oxygen consumption past meat tends to decrease as fourth dimension increases. For example, mitochondria isolated from ox muscle retained normal configuration subsequently 5 days of postmortem storage at 4 °C (Cheah and Cheah, 1971). In the presence of succinate, mitochondria isolated from bovine cardiac muscle after 60 days of postmortem storage in vacuum parcel at four °C can consume 75.4 and 22.four nanomoles of oxygen per min per mg of mitochondria at pH 7.iv and five.vi, respectively, (Tang et al., 2005a). These authors also demonstrated that mitochondrial morphology changes with storage fourth dimension, indicating swelling and membrane breakdown.

Other researchers take investigated the effects of glycolytic- and tricarboxylic substrates on postmortem bovine mitochondrial part. For example, the add-on of lactate, pyruvate, malate, and lactate-LDH-NAD to isolated beef heart mitochondria increased oxygen consumption (Ramanathan et al., 2009). Pyruvate tin enter mitochondria via pyruvate translocase and is converted to acetyl-CoA (Alam et al., 2015), which can take part in the tricarboxylic acid cycle and ultimately produce NADH. Similarly, NADH is produced when lactate is converted to pyruvate past lactate dehydrogenase activeness. Mohan et al. (2010) reported that malate-NAD-malate dehydrogenase increased NADH germination in beef. In support, pyruvate and malate increased mitochondrial oxygen consumption in vitro (Ramanathan and Mancini, 2010). Thus, metabolites that can generate either NADH or succinate have the potential to increase mitochondrial oxygen consumption.

The United states of america beef industry has started retailing individual muscles. Hence, it is important to sympathize muscle-specific differences in color stability. Mckenna et al. (2005) classified beef muscles based on colour stability into 3 groups, including color labile, intermediate, and color stable. Mitochondria is one of several factors that can influence this classification. Mitochondrial concentration in muscle depends on muscle fiber type. For example, red fibers take more mitochondria and myoglobin than white fibers. The psoas major has more cerise fibers than the longissimus (Chase and Hedrick, 1977). This suggests that mitochondrial content and metabolite utilization within these two muscle types may be different because the psoas is a color labile muscle whereas the longissimus is a colour stable muscle. A greater mitochondrial content tin can pb to more oxidative stress; hence, more discoloration in the psoas than the longissimus. Differences in color stability between the psoas and the longissimus likewise tin can be attributed to variation in antioxidant enzymes and MRA (Mohan et al., 2010; Ke et al., 2017).

Lanari and Cassens (1991) reported that the oxygen consumption rate of mitochondria isolated from Holstein longissimus and gluteus muscles decrease during storage. Cheah and Cheah (1971) concluded that increased storage time resulted in a significant loss of cytochrome c activity and a decline in country III respiration. O'Keeffe and Hood (1982) reported that the oxygen consumption rate (micromole of oxygen consumed/g fresh tissue) of longissimus and psoas muscles decreased from 221.7 (d 0) to 32.seven (d 10) and 249.7 (d 0) to (d 10) 52.nine, respectively, as measured using a Warburg constant volume respirometer. The oxygen penetration depth beneath the surface of steaks was deeper for the longissimus muscle compared with the psoas musculus (Joseph et al., 2012). More specifically, the depth of oxygen penetration and thickness of the oxymyoglobin layer depend on the rate of oxygen diffusion and oxygen consumed by mitochondria (O'Keeffe and Hood, 1982).

Several other factors that influence mitochondrial part are summarized in Tabular array 1. A better agreement of the parameters involved in mitochondrial function can offer insights related to mitochondria-mediated effects on colour.

Tabular array 1.

Factors affecting mitochondrial oxygen consumption

	Factor	Upshot	System	OCR methodology	Reference
one	pH	Increased pH enhances mitochondria activity, while decreased pH limits activity	Isolated beef mitochondria	Clark oxygen electrode	Ashmore et al. 1972
			Isolated beef mitochondria	Clark oxygen electrode	Tang et al. 2005a
			Permeabilized pork tissue	High-resolution respirometer	Phung et al., 2011
			Intact pork	Measured as a change in %OxyMb using reflectance measurement	Zhu and Brewer, 1998
			Intact beefiness	Measured as a change in %OxyMb using reflectance measurement	English et al.,2016b
2	Temperature	Increased temperature enhances mitochondria activity, while cold temperature subtract activity	Isolated beef mitochondria	Clark oxygen electrode	Tang et al. 2005a
			Intact and minced	Manometrically in a Warburg apparatus	Bendall and Taylor, 1972
			Permeabilized pork tissue	High-resolution respirometer	Phung et al., 2011
three	Species	Lamb > pork > beefiness	Minced tissue	Manometrically in a Warburg apparatus	Atkinson and Folett, 1973
4	Breed	Cross bred > Holstein	Isolated beef mitochondria	Clark oxygen electrode	Lanari and Cassens, 1991
v	Muscle effect	Diaphragm > PM > Tensor fasciae late	Ground tissue	Clark oxygen electrode	Renerre and Labas, 1987
		PM = LD = SM (twenty-four hour period 0) PM = LD > SM (day 5)	Intact muscle	As a change in carbondioxide level	Mckenna et al., 2005
		PM > LL	Intact musculus	Changes in oxymyoglobin level	Seyfert et al., 2007; Abraham et al., 2017
		PM > LL	Isolated mitochondria	Clark oxygen electrode	Ke et al., 2017
6	Muscle location	Inside semimembranosus has greater oxygen consumption than outside semimembranosus	Intact beefiness	Measured alter in oxygen concentration in flask using Oxygen analyzer	Sammel et al., 2002
		Outside semimembranosus has greater oxygen consumption than inside semimembranosus	Isolated mitochondria (day 0)	Clark oxygen electrode	Nair et al., 2017
7	Postmortem age	Increased storage time decreased oxygen consumption	Intact beefiness	Measured as a modify in % OxyMb using reflectance measurement	Madhavi and Carpenter, 1993; King et al., 2011
		Increased storage fourth dimension decreased mitochondrial activity and electron-send mediated MRA	Isolated mitochondria	Clark oxygen electrode	Mancini and Ramanathan, 2014
8	Substrates	Succinate, lactate, pyruvate increased oxygen consumption	Isolated beef mitochondria	Clark oxygen electrode	Tang et al. 2005a; Ramanathan et al., 2009.
		NADH increased oxygen consumption	Minced lamb	Manometrically in a Warburg apparatus	Atkinson et al., 1969
nine	Packaging	PVC > High oxygen	Intact beef	Measured change in % OxyMb using reflectance measurement	Seyfert et al., 2007
10	Lipid oxidation	a) Decreased oxygen consumption	Intact beef	Measured alter in % OxyMb using reflectance measurement	Seyfert et al., 2007
		b) Decreased oxygen consumption	Isolated beefiness mitochondria	Clark oxygen electrode	Ramanathan et al., 2012
10	Processing	a) Fabrication type: basis > saw > pocketknife	Intact beef	Measured equally a change in % OxyMb using reflectance measurement	Madhavi and Carpenter, 1993
			Minced and intact beef	Manometrically in a Warburg apparatus	Bendall and Taylor, 1972
		b) Ground v/south intact: mincing increase oxygen consumption	Isolated beefiness mitochondria	Clark oxygen electrode	Tang et al., 2006
		c) Sonication decrease mitochondrial activity	Isolated beef mitochondria	Clark oxygen electrode	Tang et al., 2006
		d) Freezing thaw cycle increase oxygen consumption, only decrease functional integrity	Isolated beef mitochondria	Clark oxygen electrode	Tang et al., 2006

Oxidative stress and mitochondrial degeneration

Immediately after slaughter, a lack of continuous oxygen and blood supply shifts energy production from aerobic to anaerobic metabolism. Although postmortem muscle attempts to maintain homeostasis, antioxidant defense mechanisms get less efficient and mitochondrial degeneration occurs (Crimi and Esposti, 2011). Every bit a effect, mitochondria are the first organelle affected by tissue anoxia (Ouali et al., 2013). More specifically, mitochondrial cardiolipin and Bcl-ii protein can interact with the outer membrane and increase mitochondrial outer membrane permeabilization. In addition, the shut proximity of mitochondrial membranes to free radicals increases susceptibility to oxidative damage.

Increased mitochondrial damage can take a detrimental effect on color. The presence of cytochrome c (electron carrier between complex Iii and Iv within electron-transport concatenation) in the cytosol is used equally an indicator of mitochondrial degeneration. Recent studies have reported that the decreased color stability of psoas musculus can be attributed to greater mitochondrial damage (Ke et al., 2017; Mancini et al., 2018). In back up, cytochrome c content was greater in psoas sarcoplasm than longissimus sarcoplasm during a 6 d brandish. Other research indicates that incubation of oxymyoglobin with mitochondrial lipids promoted myoglobin oxidation (Tang et al., 2005c). Conversely, supplementing lamb diets with α-tocopherol (vitamin E) decreased oxymyoglobin oxidation and increased mitochondrial function due to the aggregating of α-tocopherol in the mitochondrial membrane (Tang et al., 2005c).

Interrelation betwixt mitochondria and myoglobin function

Lipid and protein oxidation, microorganisms, mitochondria, and myoglobin compete for oxygen in postmortem musculus (Faustman and Cassens, 1990). Myoglobin serves as an oxygen reservoir and oxygen transporter for mitochondria. Approximately fourscore% of oxygen in the cell is used by mitochondria (Wittenberg, 1970). Therefore, competition for oxygen between mitochondria and myoglobin is the limiting factor responsible for the evolution of bright cherry-blood-red surface color. More specifically, mitochondria tin can affect myoglobin redox state by (i) decreasing oxygen partial pressure via respiration, and (2) reducing metmyoglobin (Tang et al., 2005a, 2005b). Thus, mitochondria can influence both colour development (oxygenation/flower) and color stability (oxidation).

Oxygen consumption and muscle darkening

A characteristic brilliant-red color is required for consumer credence (Smith et al., 2000). Although bloomed steaks from both nighttime-cutting beef and lactate-enhanced meat will have a dark reddish color, the mechanism(s) responsible for this darkening is different. In dark-cutting beef, a greater than normal pH will prevent the decrease in mitochondrial activity that typically occurs as muscle pH declines postmortem. Equally a result, an increment in mitochondrial activity promotes oxygen consumption and darkens muscle due to decreased oxygen partial pressure. This encourages the maintenance of myoglobin in a deoxygenated state (Ashmore et al., 1972; Cornforth and Egbert, 1985; Egbert and Cornforth, 1986; Renerre and Labas, 1987). In this situation, meat fails to bloom (oxygenate) and does not form the characteristic brilliant cherry-red-ruddy color associated with fresh beef. This is supported by decreased myoglobin oxygenation of bloomed night-cutting beef compared with normal-pH beef (English et al., 2016a).

The mechanism(due south) of lactate-induced darkening in beef suggests that the addition of lactate results in NADH formation by lactate dehydrogenase activity (Kim et al., 2006). This NADH tin can be used as a complex I substrate, resulting in increased mitochondrial oxygen consumption and musculus concealment. This was supported in vitro by the add-on of lactate, NAD, and LDH to bovine longissimus mitochondria and oxymyoglobin (Ramanathan et al., 2013). Incubating mitochondria-oxymyoglobin mixture with substrates increased deoxymyoglobin by 6 h of incubation, and maintained deoxymyoglobin for 24 h. A greater corporeality of deoxymyoglobin results in a darker beef color. Previous research demonstrated lactate-enhanced steaks had less myoglobin oxygenation than command steaks (Ramanathan et al., 2012). The office of mitochondria in lactate-mediated darkening besides has been supported by research utilizing the addition of mitochondrial inhibitor (rotenone; complex I inhibitor) to lactate-cardiac muscle homogenates, which reversed lactate-induced darkening. Both in dark-cutting and lactate-enhanced beef, physical mechanism(s) besides contribute to muscle concealment. More specifically, a greater pH in dark-cut beef tin increase the power of muscle fibers to hold more h2o (Swatland, 2008). However, in lactate-enhanced beefiness, presence of lactate tin influence refractive index of sarcoplasm (Ramanathan et al., 2010). Both weather can subtract light reflectance properties, resulting in darker meat color.

The upshot of mitochondrial oxygen consumption on myoglobin redox state has been demonstrated in vitro. Mitochondrial respiration will event in the conversion of oxy- to deoxymyoglobin post-obit the improver of mitochondrial substrate such every bit succinate (Tang et al., 2005a). This conversion is promoted by greater mitochondrial density and pH. Farther, anaerobic weather favor a decrease in oxygen partial pressure and deoxymyoglobin formation from oxymyoglobin. Cornforth and Egbert (1985) reported that inhibition of pre-rigor mitochondrial respiration by rotenone volition result in a brilliant-red colour.

Mitochondrial oxygen consumption and metmyoglobin reduction

In addition to the role of mitochondria in oxygen consumption (color evolution), mitochondrial activity also can affect myoglobin redox stability (color stability). Metmyoglobin reducing activeness is an important intrinsic holding that prolongs the color stability of meat during storage (Ledward, 1985). More specifically, MRA relies on the production of either NADH (by dehydrogenase enzymes) or electrons (by mitochondria), both of which can be used to reduce metmyoglobin (Giddings, 1977; Faustman et al., 1988; Bekhit and Faustman, 2005). Mitochondria-mediated MRA can occur via four different pathways:

• 1. Electron-send mediated MRA: Cytochrome c is an electron carrier that transports bachelor electrons from the electron ship chain to metmyoglobin (from the inner membrane to outer membrane). Addition of succinate to metmyoglobin-mitochondria mixtures increased ferrous myoglobin by promoting the transfer of bachelor electrons within the electron transport chain to metmyoglobin between complexes 3 and IV via cytochrome c (Tang et al., 2005b). Other studies take reported that the add-on of pyruvate and lactate increased electron-transport mediated reduction (Ramanathan and Mancini, 2010; Ramanathan et al., 2010). This is probable due to the formation of NADH or succinate via utilization of pyruvate or lactate by the tricarboxylic acid cycle. On the other hand, pre-incubation of mitochondria with 4-hydroxy-two-nonenal (HNE; a secondary lipid oxidation product) decreased electron-ship mediated metmyoglobin reduction at both pH 5.half-dozen and 7.4. The improver of antimycin A (complex III inhibitor) with succinate inhibited electron-transported mediated metmyoglobin reduction. Electron-transport mediated reduction depends on pH, temperature, mitochondrial-, and substrate-concentration.

• 2. Anaerobic weather: Mitochondrial oxygen consumption is critical for creating anaerobic conditions that favor metmyoglobin reduction (Watts et al., 1966). The conversion of oxymyoglobin to deoxymyoglobin is a two-step procedure, where oxymyoglobin is outset converted to metmyoglobin and then to deoxymyoglobin. Therefore, limited mitochondrial activity will produce conditions that are not ideal for reducing activity. Furthermore, when mitochondria cannot eat sufficient oxygen and the oxygen fractional pressure reaches 3 to seven mm Hg, myoglobin is prone to oxidation. Lanier et al. (1978) reported that metmyoglobin reduction occurs more efficiently in anaerobic conditions than in aerobic atmospheres.

• 3. NADH-dependent reductase activeness: Like to NADH-dependent hemoglobin reductase, muscle has NADH-dependent myoglobin reductase to convert metmyoglobin to deoxy-/oxymyoglobin. NADH-dependent metmyoglobin reductase and diaphorase are present in the outer mitochondria membrane and promote metmyoglobin reduction (Giddings, 1977; Arihara et al., 1995). These enzymes tin convert metmyoglobin to ferrous myoglobin in the presence of NADH. This conversion is physiologically important because the ferric form of myoglobin cannot conduct oxygen. There are muscle-dependent differences in NADH-dependent enzyme activeness (Lanari and Cassens, 1991). For case, chiliadluteus medius had greater enzyme activity than the longissimus dorsi muscle both in Holstein and crossbred cattle. The add-on of lactate-LDH-NAD to metmyoglobin-mitochondria mixtures increased metmyoglobin reduction via NADH-dependent reductase activity (Ramanathan et al., 2010). Withal, lipid oxidation products can limit mitochondria-mediated NADH-dependent reductase activeness. Pre-incubation of mitochondria with HNE decreased enzymatic metmyoglobin reduction resulting from the mitochondrial fraction.

• four. Non-enzymatic MRA: In non-enzymatic metmyoglobin reduction, compounds such equally quinone, cytochrome c, or methylene blue can transfer electrons from NADH to metmyoglobin (Elroy et al., 2015). Recently, Belskie et al. (2015) reported that the addition of NAD and succinate to isolated beef mitochondria increased NADH formation and metmyoglobin reduction by reverse electron transfer. More specifically, reverse electron flow occurs when substrates are available and forrard electron menstruation is inhibited or when oxygen is absent. The NADH formed as a event tin be used for either enzymatic or non-enzymatic MRA. The role of mitochondria in non-enzymatic metmyoglobin may be express due to other MRA pathways present in mitochondria. Notwithstanding, NADH formed can be used by multiple metmyoglobin reduction pathways.

Effects of crumbling on mitochondria part

Wet aging is commonly used to increment beef palatability. Yet, aging time likewise can influence beef colour. For example, initial color development (oxymyoglobin formation) of longissimus thoracis steaks increased with fourth dimension postmortem due to a decrease in oxygen consumption (Lee et al., 2008). Although decreased oxygen consumption might be responsible for increased in initial cerise color intensity, MRA is also required to maintain bloom or carmine color intensity. Therefore, increased aging time can decrease color stability of steaks during display (Lindahl, 2011; English et al., 2016b); in part, due to decreased mitochondrial function. Increased aging fourth dimension decreased oxygen consumption and electron send-mediated metmyoglobin reduction with the improver of succinate and lactate-LDH-NAD (Mancini and Ramanathan, 2014). Wet aging of beefiness beyond 14 d is detrimental to beef longissimus color. For example, Seyfert et al. (2007) reported a 3 unit decrease in beef longissimus steak redness (a* values) when aged for eleven d and during vii d display in PVC packaging. Withal, equally crumbling fourth dimension increased to 21 d, changes in redness (a* values) during 6 d brandish was xvi.i units (English et al., 2016b). In add-on to the office of mitochondria in decreased color stability, increased aging period also can subtract metabolites required to regenerate of NADH. The effects of crumbling on beef color is summarized in Figure 2.

Figure 2.

Effects of aging on beef colour.

Mitochondria and myoglobin interaction

Myoglobin serves as an oxygen carrier and reservoir by reversibly bounden oxygen. For case, in diving mammals and birds, oxygen stored in myoglobin provides the basis for aerobic cellular activity during extended periods of apnea. Myoglobin content is 10-30 times greater in muscles of diving animals compared with animals not experiencing extended periods of apnea (Noren and Williams, 2000). Furthermore, myoglobin concentration is correlated positively with dive duration (Kooyman and Ponganis, 1998).

Studies have shown that a direct interaction between mitochondria and myoglobin exists and their functions are interrelated (Wittenberg and Wittenberg, 1987; Tang et al., 2005a; Postnikova et al., 2009). Myoglobin provides oxygen to mitochondria via interaction between oxymyoglobin and the outer membrane (Wittenberg and Wittenberg, 1987). Charged residues within the C-D inter-helical region of myoglobin (C and D represents the names of alpha helix) can demark transiently to proteins present on the surface of mitochondria during oxygen delivery (Romero-Herrera et al., 1978). Oxygen can be transported from oxymyoglobin to mitochondria by facilitated diffusion (Wittenberg and Wittenberg, 2007). Postnikova et al. (2009) noted that facilitated diffusion is effective just when the oxygen partial pressure is two to 5 mm Hg and oxymyoglobin concentration is greater.

A subtract in oxymyoglobin and oxygen partial pressure were reported when rat mitochondria and sperm whale oxymyoglobin were incubated with succinate (Postnikova et al., 2009). More specifically, when actively respiring mitochondria were separated by a semipermeable membrane, no deoxygenation of myoglobin was observed. Therefore, these authors concluded that a mechanism other than facilitated diffusion might be present in tissue to provide constructive oxygen transfer to mitochondria. More than specifically, direct interaction between myoglobin and mitochondria may exist necessary for oxygen transfer. However, limited enquiry has assessed the interaction betwixt myoglobin and mitochondria in postmortem muscle.

Mitochondria and substrates

In general, enzymes involved in glycolysis and the tricarboxylic acrid cycle remain agile in postmortem muscle, however, the substrates are depleted. Among the substrates and cofactors involved in color stability, NADH is a key component required for both enzymatic and not-enzymatic metmyoglobin reduction (Renerre and Labas, 1987; Echevarne et al., 1990). Although processes capable of producing NADH are continually depleted postmortem, NADH can be regenerated past dehydrogenase enzymes present in postmortem muscle, either cytoplasmic or mitochondrial (Stewart et al., 1965; Watts et al., 1966; Giddings, 1977). For example, lactate enhancement increased NADH concentration in beef longissimus by lactate dehydrogenase activity and this NADH was used for not-enzymatic metmyoglobin reduction (Kim et al., 2006). Addition of glycolytic and tricarboxylic acid (TCA) bicycle intermediates to ground beef increased metmyoglobin reduction (Saleh and Watts, 1968). These authors suggested that NADH in conjunction with sarcoplasmic diaphorase enzymes facilitates metmyoglobin reduction. Atkinson et al. (1969) demonstrated a significant increment in oxygen uptake later on add-on of NADH to lamb semimembranosus musculus. They noted that oxygen uptake was increased 3-fold with the addition of 1 to 4 micromoles NADH/ml of Ringers solution in a Warburg flask in 2 h at 15 °C. Conversely, inhibition of postmortem glycolysis decreased color stability by limiting NADH content (Jerez et al., 2003).

Enhancing beef with succinate and pyruvate increased color stability in PVC and HiOx-MAP packaging (Ramanathan et al., 2011), whereas the addition of pyruvate to steaks packaged in vacuum package increased discoloration. This suggests that the role of substrates in beef color is packaging-dependent. Enhancing beef with succinate and lactate increased MRA due to the regeneration of reducing equivalents such equally NADH for MRA. Although the mechanism of pyruvate-mediated discoloration is not clear, the authors speculated that pyruvate oxidized NADH in sarcoplam via conversion of pyruvate to lactate with lactate dehydrogenase. Bjelanovic et al. (2016) also reported that pyruvate increased metmyoglobin germination in ground beefiness packaged in vacuum.

Mohan et al. (2010) reported muscle-specific effects of metabolites in a model system. In semitendinosus muscle, ii% lactate was effective in limiting discoloration, while malate was effective in longissimus and psoas muscles. Other researchers have reported that incorporating TCA substrates either individually or in combination can bear upon myoglobin redox stability of beef packaged in aerobic and anaerobic packaging. For instance, a combination of glutamate-malate-citrate retained oxymyoglobin content in MAP packaging (70% oxygen and 30% carbon dioxide) when stored for 6 d (Bjelanovic et al. 2016). Hence, characterizing the role of metabolites will improve our understanding of beef colour (Abraham et al., 2017).

Mitochondria and lipid oxidation

Polyunsaturated fatty acids, such as linoleic acid, linolenic acid, and arachidonic acrid are abundant in phospholipids of prison cell membranes to maintain fluidity. Approximately l% of the fatty acids present in mitochondria are unsaturated (Lass and Sohal, 1998). These fatty acids comprise double bonds that are prone to oxidation. Equally a result, lipid oxidation within the mitochondria tin grade various aldehydes, alkenals, and hydroxyalkenals, all of which are highly reactive and cytotoxic to nucleic acids and proteins (Esterbauer et al., 1991). For case, oxidation of ω-vi polyunsaturated fatty acids produces HNE, which can inactivate enzymes and modify poly peptide structure by alkylating histidine, cysteine, and lysine residues. In addition, HNE tin bind covalently to histidine residues of equine (Faustman et al., 1999), bovine (Alderton et al., 2003), porcine (Suman et al., 2007), yellowfin tuna (Lee et al., 2003), craven and turkey (Naveena et al., 2010), and ovine (Yin et al., 2011) myoglobins. The HNE can decrease color stability by covalent binding of histidine residues. The HNE also can decrease color stability by limiting functionality of enzymes involved in NADH production. For example, incubation of bovine heart LDH with HNE decreased NADH formation (Ramanathan et al., 2014). Mass spectrometric investigation indicated that HNE tin covalently bind to cysteine and histidine residues, limiting LDH functionality (Ramanathan et al., 2014). Other studies have shown that HNE can bind covalently to enzymes, including glucose-6-phosphate dehydrogenase (Szweda et al., 1993), pyruvate dehydrogenase (Patel and Korotchkina, 2002), glutathione reductase (Jagt et al., 1997), and glutathione transferase (Drake et al., 2004.

In addition to the furnishings of HNE on myoglobin and enzymes in color stability, studies have shown that HNE can limit mitochondrial role. The HNE tin demark to cytochrome c, which transports electrons between ubiquinol cytochrome c oxidoreductase (Complex Three) and cytochrome c oxidase (Circuitous Four; Villani and Attardi, 2000; Isom et al., 2004). Further, HNE tin can covalently bind to cytochrome c oxidase, an enzyme that catalyzes electron transfer from cytochrome c to oxygen (Chen et al., 2001).

Incubation of bovine heart mitochondria with HNE decreased country III and state Iv oxygen consumption with the improver of circuitous I and II substrates at pH 5.6 and 7.4 (Ramanathan et al., 2012). Enquiry utilizing mitochondria from laboratory animals also noted inhibitory furnishings of HNE on mitochondrial function. Pre-incubation of isolated rat heart mitochondria with HNE inhibited complex I of the electron ship chain (Humphries et al., 1998). Similarly, Picklo et al. (1999) reported that the addition of HNE to mitochondria isolated from rat brain decreased oxygen consumption past complexes 1 and iii.

Electron microscopy revealed that HNE-treated mitochondria had a pH-dependent effect on morphology. Mitochondria were bloated and had increased membrane permeability at pH 7.4. Conversely, mitochondria incubated with HNE at pH 5.6 had decreased book and permeability (Ramanathan et al., 2012). The HNE can induce swelling via stimulation of permeability transition pores present in the mitochondrial membrane (Kristal et al., 1996). Fluorescence studies indicated that HNE binds to the membrane of mitochondria isolated from bovine cardiac muscle. The interaction betwixt HNE and rat hepatic mitochondria results in restricted membrane mobility and fluidity, which can influence both mitochondrial morphology and function (Humphries et al., 1998). Chen and Yu (1994) reported that HNE binds to rat mitochondrial membranes, oxidizes phospholipids and poly peptide thiols, and alters membrane fluidity.

Conclusions

Postmortem mitochondrial function, specifically oxygen consumption and metmyoglobin reduction are essential in beef color development and stability. Greater oxygen consumption and MRA tin can result in improved color stability. This is probable due to mitochondrial product of NADH and other reducing equivalents involved in maintaining myoglobin in ferrous form. Therefore, characterizing the factors that influence the interrelation betwixt mitochondria and myoglobin will increase our fundamental noesis related to beef colour chemistry.

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