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Myoglobin in meat

Myoglobin in meat


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When looking at the reason why some meat is white and the rest is red, I found out it is down to the levels of myoglobin as higher levels of myoglobin are found in "slow twitch" muscles.

I have also seen that myoglobin is not the same as haemoglobin, so what is the source of myoglobin? Does it come from the blood?


Myoglobin is a protein made in muscle cells. It is similar to hemoglobin, a protein made by blood cells. The answer you linked helps explain the difference, which it sounds like you understand. The source is simply the ribosomes in the respective cells that express that protein. The color in both blood and uncooked or rare meat is due to the heme group in hemoglobin and myoglobin respectively.


Myoglobin

Myoglobin (symbol Mb or MB) is an iron- and oxygen-binding protein found in the skeletal muscle tissue of vertebrates in general and in almost all mammals. [5] [6] [7] [8] [9] Myoglobin is distantly related to hemoglobin. Compared to hemoglobin, myoglobin has a higher affinity for oxygen and does not have cooperative-binding with oxygen like hemoglobin does. [8] [10] But at the core, it is an oxygen-binding protein in red blood cells. In humans, myoglobin is only found in the bloodstream after muscle injury. [11] [12] [13]

High concentrations of myoglobin in muscle cells allow organisms to hold their breath for a longer period of time. Diving mammals such as whales and seals have muscles with particularly high abundance of myoglobin. [13] Myoglobin is found in Type I muscle, Type II A, and Type II B, but most texts consider myoglobin not to be found in smooth muscle. [ citation needed ]

Myoglobin was the first protein to have its three-dimensional structure revealed by X-ray crystallography. [14] This achievement was reported in 1958 by John Kendrew and associates. [15] For this discovery, Kendrew shared the 1962 Nobel Prize in chemistry with Max Perutz. [16] Despite being one of the most studied proteins in biology, its physiological function is not yet conclusively established: mice genetically engineered to lack myoglobin can be viable and fertile, but show many cellular and physiological adaptations to overcome the loss. Through observing these changes in myoglobin-depleted mice, it is hypothesised that myoglobin function relates to increased oxygen transport to muscle, and to oxygen storage as well, it serves as a scavenger of reactive oxygen species. [17]

In humans, myoglobin is encoded by the MB gene. [18]

Myoglobin can take the forms oxymyoglobin (MbO2), carboxymyoglobin (MbCO), and metmyoglobin (met-Mb), analogously to hemoglobin taking the forms oxyhemoglobin (HbO2), carboxyhemoglobin (HbCO), and methemoglobin (met-Hb). [19]


Variations in meat colour due to factors other than myoglobin chemistry a synthesis of recent findings (invited review)

This review focuses on the mechanisms responsible for some the achromatic aspects of meat colour (paleness or darkness) due to light scatter from structures within the tissue. Recent investigations have highlighted the role of three key mechanisms contributing to variations in the lightness of meat: (1) Variations in the myofilament lattice spacing, and the resultant changes in myofibril diameter and muscle fibre diameter. A 20% increase in lightness (L* value) between muscles with ultimate pH of 6.1 versus 5.4 is accompanied by a 17% change in muscle fibre diameter. (2) Variations in sarcomere length, if these are associated with changes in myofilament and myofiber diameter, (3) Variations in sarcoplasmic protein distribution, including whether these are bound or precipitated onto the myofilaments, as demonstrated by an increase of 1.24 in the ratio of X-ray diffraction intensities from mass centered on the thin filaments versus thick filaments in dark (pH 6.15) versus light (pH 5.47) muscles. For clarity, the discussion of these mechanisms is principally in relation to pH and temperature at rigor (5 °C-35 °C), although the possibility of contributions from numerous other factors is acknowledged.

Keywords: Achromicity Colour Meat Microstructure Muscle Myofibrils Rigor temperature Sarcoplasmic proteins pH.


Scientists enhance color and texture of cultured meat

Bovine skeletal muscle cells grown in the presence of myoglobin (center) or hemoglobin (right) Credit: Robin Simsa & David Kaplan, Tufts University

A team of Tufts University-led researchers exploring the development of cultured meat found that the addition of the iron-carrying protein myoglobin improves the growth, texture and color of bovine muscle grown from cells in culture. This development is a step toward the ultimate goal of growing meat from livestock animal cells for human consumption.

The researchers found that myoglobin increased the proliferation and metabolic activity of bovine muscle satellite cells. Addition of either myoglobin or hemoglobin also led to a change of color more comparable to beef. The results, published today in FOODS, indicate potential benefits of adding heme proteins to cell media to improve the color and texture of cell-grown meat.

"Taste, color, and texture will be critical to consumer acceptance of cultured meat," said David Kaplan, Stern Family Professor of Engineering at the Tufts University School of Engineering and corresponding author of the study. "If our goal is to make something similar to a steak, we need to find the right conditions for cells to grow that replicate the formation of natural muscle. The addition of myoglobin looks to be one more important addition to the recipe that brings us closer to that goal," added Kaplan, chair of the Department of Biomedical Engineering and a program faculty member at the Sackler School of Graduate Biomedical Sciences at Tufts.

The rationale for developing cultured meat (also referred to as 'lab-grown meat', 'cellular agriculture' or 'cell-based meat') is the potential to reduce the amount of resources required in meat production, as well as significantly shrink its environmental footprint relative to animal farming. Animal farming has been associated with greenhouse gas emissions, antibiotic resistance problems, animal welfare concerns, and land use issues, such as the clearing of the Amazon rainforests. The ability to grow cultured meat in a bioreactor, as in tissue engineering, could potentially alleviate these issues. However, much remains to be done to grow the cells in a way that replicates the texture, color and flavor of naturally derived meat.

Plant-based meat substitutes like the Impossible Burger have incorporated heme proteins from soy, which make the product more meat-like in appearance and taste. The Tufts-led research team hypothesized that adding heme proteins to meat cell culture could not only have a similar effect but also could improve the growth of muscle cells which require the heme proteins to thrive.

Myoglobin is a natural component of muscle, and hemoglobin is found in blood. As heme proteins, both carry iron atoms that are responsible for the natural bloody, slightly 'metallic' taste of beef. The researchers found that adding hemoglobin or myoglobin changes the color of the bioartificial muscle to a reddish-brown meat-like hue. Myoglobin, however, was much better for promoting cell proliferation and differentiation of the BSCs to mature muscle cells, and better at helping the cells form fibers and adding a rich meat-like color.


Total Pigments and Myoglobin Concentration In Four Bovine Muscles

Journal Series Paper No. 1294 approved by the Director of the Oklahoma Agricultural Experiment Station.

SUMMARY

—This research was to determine whether quantitative differences in total pigment and myoglobin concentration could be detected, chemically, in muscles which differed in visual color. For this purpose, a portion of the longissimus dorsi, psoas major, biceps femoris, and semitendinosus muscles was removed at specific locations, from choice-grade steer carcasses, for use as experimental material. Each muscle was subjected to total pigment, myoglobin, fat, and moisture analysis. Hemoglobin content was determined by the difference between total pigment and myoglobin concentrations, Correction of total pigment and myoglobin concentration for fat and/or moisture was used to determine its influence upon the variation in the quantity of muscle pigmentation.

Precise results were obtained with the total pigment and myoglobin procedures. Total pigment concentration was greatest in the biceps femoris and least in the semitendinosus. Little difference was obtained between the longissimus dorsi and psoas major. Myoglobin concentration, in decreasing order of magnitude, for the muscles studied was biceps femoris, longissimus dorsi, psoas major, and semitendinosus. The difference between myoglobin and total pigment concentration in the psoas major muscle was a result of hemoglobin constituting a greater portion of the total pigmentation. Results also indicated that hemoglobin contributed more to total pigment concentration and probably to muscle color than previously reported. The significance of the results obtained was not altered by correcting the data for fat and/or moisture.


Myoglobin in meat - Biology

Today I found out the red juice in raw red meat is not blood. Nearly all blood is removed from meat during slaughter, which is also why you don’t see blood in raw “white meat” only an extremely small amount of blood remains within the muscle tissue when you get it from the store.

So what is that red liquid you are seeing in red meat? Red meats, such as beef, are composed of quite a bit of water. This water, mixed with a protein called myoglobin, ends up comprising most of that red liquid.

In fact, red meat is distinguished from white meat primarily based on the levels of myoglobin in the meat. The more myoglobin, the redder the meat. Thus most animals, such as mammals, with a high amount of myoglobin, are considered “red meat”, while animals with low levels of myoglobin, like most poultry, or no myoglobin, like some sea-life, are considered “white meat”.

Myoglobin is a protein that stores oxygen in muscle cells, very similar to its cousin, hemoglobin, that stores oxygen in red blood cells. This is necessary for muscles which need immediate oxygen for energy during frequent, continual usage. Myoglobin is highly pigmented, specifically red so the more myoglobin, the redder the meat will look and the darker it will get when you cook it.

This darkening effect of the meat when you cook it is also due to the myoglobin or more specifically, the charge of the iron atom in myoglobin. When the meat is cooked, the iron atom moves from a +2 oxidation state to a +3 oxidation state, having lost an electron. The technical details aren’t important here, though if you want them, read the “bonus factoids” section, but the bottom line is that this ends up causing the meat to turn from pinkish-red to brown.

Pro-tip: when searching for non-copyrighted pictures for an article, don’t search for “white meat” or really any variation of that on Google Image Search.

If you liked this article and the Bonus Facts below, you might also enjoy:

  • It is possible for meat to remain pinkish-red all through the cooking if it has been exposed to nitrites. It is even possible for packagers, through artificial means, to keep the meat looking pink, even after it has spoiled, by binding a molecule of carbon monoxide to produce metmyoglobin. Consumers associate pink meat with “fresh”, so this increases sales, even though the pink color has little to do with the freshness of meat.
  • Pigs are often considered “white meat”, even though their muscles contain a lot more myoglobin than most other white meat animals. This however, is a much lower concentrate of myoglobin than other “red meat”, such as cows, due to the fact that pigs are lazy and mostly just lay around all day. So depending on who you talk to, pigs can be considered white meat or red meat they more or less sit in between the two classifications.
  • Chickens and Turkeys are generally considered white meat, however due to the fact that both use their legs extensively, their leg muscles contain a significant amount of myoglobin which causes their meat to turn dark when cooked so in some sense they contain both red and white meat. Wild poultry, which tend to fly a lot more, tend to only contain “dark” meat, which contains a higher amount of myoglobin due to the muscles needing more oxygen from frequent, continual usage.
  • White meat is made up of “fast fibers” that are used for quick bursts of activity. These muscles get energy from glyocogen which, like myoglobin, is stored in the muscles.
  • Fish are primarily white meat due to the fact that they don’t ever need their muscles to support themselves and thus need much less myoglobin or sometimes none at all in a few cases they float, so their muscle usage is much less than say a 1000 pound cow who walks around a lot and must deal with gravity. Typically, the only red meat you’ll find on a fish is around their fins and tail, which are used almost constantly.
  • Some fish, such as sharks and tuna, have red meat because they are fast swimmers and are migratory and thus almost always moving they use their muscles extensively and so they contain a lot more myoglobin than most other sea-life.
  • For contrast, the white meat from chickens is made up of about .05% myoglobin with their thighs having about .2% myoglobin pork and veal contain about .2% myoglobin non-veal beef contains about 1%-2% of myoglobin, depending on age and muscle use.
  • The USDA considers all meats obtained from livestock to be “red” because they contain more myoglobin than chicken or fish.
  • Beef meat that is vacuum sealed, thus not exposed to oxygen, tends to be more of a purple shade. Once the meat is exposed to oxygen, it will gradually turn red over a span of 10-20 minutes as the myoglobin absorbs the oxygen.
  • Beef stored in the refrigerator for more than 5 days will start to turn brown due to chemical changes in the myoglobin. This doesn’t necessarily mean it has gone bad, though with this length of unfrozen storage, it may have. Best to use your nose to tell for sure, not your eyes.
  • Before you cook the red meat, the iron atom’s oxidation level is +2 and is bound to a dioxygen molecule (O2) with a red color as you cook it, this iron loses an electron and goes to a +3 oxidation level, and now coordinates with a water molecule (H2O). This process ends up turning the meat brown.

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So, next time I’m barbecuing and my friend says, “The bloodier the better!” I’m going to correct him and say, “No. The more myoglobin, the better!”

On second thought, I may get punched!

Nitrite soaking of meat is one of the oldest myoglobin fixes. The procedure was discussed at length in several German chemistry journals as early as the 19th century. The structure of MbNO2 was one of the first bioinorganic structures solved and continues to this day to be a system of great interest. Nitrites and nitrosyls are important biological signaling molecules. While nitrite soaking of meat may improve their sale value, high concentrations of nitrites should be avoided. Foods like packaged pepperoni (while delicious) do contain very high amounts of nitrite. When proteins are exposed to heat, thermal degradation occurs and the free nitrite groups will attach, forming nitrosamines. Nitrosamines have been implicated in pancreatic cancer (among other types). Strangely, nitrite should theoretically kill any organism whose respiration is dependent on Mb/Hb systems, since nitrite is favorable to oxygen. This means that nitrite displaces oxygen from myoglobin and hemoglobin at a very fast rate. The reversal of this process, believed to be mediated by cd1 nitrite reductase is the subject of a great deal of study in biochemistry (on experimental, analytical and theoretical fronts).

Yi, J. Heinecke, H. Tan, H. Ford, P. Richter-Addo, G. The Distal Pocket Histidine Residue in Horse Heart Myoglobin Directs the O-Binding Mode of Nitrite to the Heme Iron. J. Am. Chem. Soc. 2009, 131, 18119-18128.
Visser, S. Density functional theory (DFT) and combined quantum mechanical/molecular mechanics (QM/MM) studies on the oxygen activation step in nitric oxide synthase enzymes. Biochem. Soc. Trans. 2009, 37, 373-377.
Chen, H. Hirao, H. Derat, E. Schlichting, I. Shaik, S. Quantum Mechanical/Molecular Mechanical Study on the Mechanisms of Compound I Formation in the Catalytic Cycle of Chloroperoxidase: An Overview on Heme Enzymes. J. Phys. Chem. B 2008, 112, 9490-9500.
Cho, K. Hirao, H. Chen, H. Carvajal, M. Cohen, S. Derat, E. Thiel, W. Shaik, S. Compound I in Heme Thiolate Enzymes: A Comparative QM/MM Study. J. Phys. Chem. A 2008, 112, 13128-13138.
Marti, M. Crespo, A. Bari, S. Doctorovich, F. Estrin, D. QM-MM Study of Nitrite Reduction by Nitrite Reductase of Pseudomonas aeruginosa. J. Phys. Chem. B 2004, 108, 18073-18080.
Copeland, D. Soares, A. West, A. Richter-Addo, G. Crystal structures of the nitrite and nitric oxide complexes of horse heart myoglobin. J. Inorg. Biochem. 2006, 100, 1413-1425.
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Why is pork different from other red meats?

In other words why is that cow, dogs, cats, horses, even humans have bright red meat *(not a cannibal), But pork is totally different. Same question for birds too. I know ones a mammal and the other is a bird, duh. But why are they different.

Red/dark meat is muscle high in myoglobin, used for sustained effort. White meat is better for short bursts (higher output but low endurance, since no oxygen storage).
Turkey & chicken have dark meat legs and white meat flight muscles, since they are ground birds that walk a lot but fly rarely. Geese & ducks fly long distances, so they are all dark meat. Many small animals are mostly white meat, since they need to run fast to escape predators.
From the meat color, it would be a good guess that the porcine ancestry involves more panic running, and less long-distance travel.


Scientists enhance color and texture of cultured meat

A team of Tufts University-led researchers exploring the development of cultured meat found that the addition of the iron-carrying protein myoglobin improves the growth, texture and color of bovine muscle grown from cells in culture. This development is a step toward the ultimate goal of growing meat from livestock animal cells for human consumption.

The researchers found that myoglobin increased the proliferation and metabolic activity of bovine muscle satellite cells. Addition of either myoglobin or hemoglobin also led to a change of color more comparable to beef. The results, published today in FOODS, indicate potential benefits of adding heme proteins to cell media to improve the color and texture of cell-grown meat.

"Taste, color, and texture will be critical to consumer acceptance of cultured meat," said David Kaplan, Stern Family Professor of Engineering at the Tufts University School of Engineering and corresponding author of the study. "If our goal is to make something similar to a steak, we need to find the right conditions for cells to grow that replicate the formation of natural muscle. The addition of myoglobin looks to be one more important addition to the recipe that brings us closer to that goal," added Kaplan, chair of the Department of Biomedical Engineering and a program faculty member at the Sackler School of Graduate Biomedical Sciences at Tufts.

The rationale for developing cultured meat (also referred to as 'lab-grown meat', 'cellular agriculture' or 'cell-based meat') is the potential to reduce the amount of resources required in meat production, as well as significantly shrink its environmental footprint relative to animal farming. Animal farming has been associated with greenhouse gas emissions, antibiotic resistance problems, animal welfare concerns, and land use issues, such as the clearing of the Amazon rainforests. The ability to grow cultured meat in a bioreactor, as in tissue engineering, could potentially alleviate these issues. However, much remains to be done to grow the cells in a way that replicates the texture, color and flavor of naturally derived meat.

Plant-based meat substitutes like the Impossible Burger have incorporated heme proteins from soy, which make the product more meat-like in appearance and taste. The Tufts-led research team hypothesized that adding heme proteins to meat cell culture could not only have a similar effect but also could improve the growth of muscle cells which require the heme proteins to thrive.

Myoglobin is a natural component of muscle, and hemoglobin is found in blood. As heme proteins, both carry iron atoms that are responsible for the natural bloody, slightly 'metallic' taste of beef. The researchers found that adding hemoglobin or myoglobin changes the color of the bioartificial muscle to a reddish-brown meat-like hue. Myoglobin, however, was much better for promoting cell proliferation and differentiation of the BSCs to mature muscle cells, and better at helping the cells form fibers and adding a rich meat-like color.


Myoglobin in meat - Biology

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U.S. DEPARTMENT OF AGRICULTURE

Livestock Bio-Systems: Clay Center, NE

ARS-wide

At this Location

Title: Genome-wide association of myoglobin concentrations in pork loins

Interpretive Summary: Pork quality is a concern for producers, packers, retailers, and consumers. Lean meat color is a major focus for consumers as they often associate color with freshness. Myoglobin is the primary pigment resulting in the red color of pork. In order to increase redness of pork, increasing myoglobin concentration is important. Therefore, we must understand genetic factors that affect myoglobin concentration to enable improving pork color. The objective of this study was to identify genetic markers associated with myoglobin concentration in pork loin muscle. Ultimate pH and myoglobin concentrations were measured in 599 loin samples of pigs from two different commercial finishing swine facilities. An association analysis identified regions within seven chromosomes that explained over half of the genetic variance in myoglobin concentration. Chromosome 7 had one significant region which accounted for over one third of the genetic variance, while chromosome 14 had three significant regions. Within the region identified we found genes involved in regulating iron or calcium concentrations in muscle. Improving pork color may be possible by monitoring these genes or by using the genetic markers associated with myoglobin in selection decisions

Technical Abstract: Lean color is a major focus for identifying pork loins for export markets, and myoglobin is the primary pigment driving pork color. Thus, increasing myoglobin concentration should increase redness of pork products and the number of loins acceptable for exportation. Therefore, understanding genetic variation and parameters affecting myoglobin concentration is critical for improving pork color. The objective of this study was to identify genetic markers associated with myoglobin concentration in pork loin muscle. Ultimate pH and myoglobin concentrations were measured in longissimus thoracis et lumborum samples of pigs (n = 599) from two different commercial finishing swine facilities. A Bayes-C model implemented in GenSel identified regions within 7 chromosomes that explained greater than 63% of the genetic variance in myoglobin concentration. Chromosome 7 had 1 significant region which accounted for 37% of the genetic variance, while chromosome 14 had 4 significant regions accounting for 9.8% of the genetic variance. Candidate genes in the region on chromosome 7 were involved in iron homeostasis, and genes in the significant regions on chromosome 14 were involved in calcium regulation. Genes identified in this study represent potential biomarkers that could be used to select for higher myoglobin concentrations in pork, which may improve lean meat color.


Spoilage of Different Kind of Meat | Microbiology

In this article we will discuss about the spoilage of different kind of meat.

Pork is the only meat which spoils more readily than other meats because of its high content of Vitamin B. Lactic acid bacteria chiefly Lactobacillus, Leuconostoc, Streptococcus, and Pediococcus are present in either meats and can grow even at refrigerated temperature. Lactic acid bacteria cause slime production especially in the presence of sucrose give green colouration and souring.

Fresh beef undergoes the changes in the haemoglobin and myoglobin, the red pigment in the blood muscles, respectively, so as to cause loss of bloom and the production of reddish brown methaemoglobin and met-myoglobin (Fig. 21.3) and the green grey brown oxidation pigments by action of oxygen and microorganisms action. Pseudomonas and Micrococcus grow in beef, held at 10°C or lower.

It usually putrefies at room temperature. Among the genera reported are Bacillus, Clostridium, Escherichia, Enterobacter, Proteus, Pseudomonas, Alcaligenes, Lactobacil­lus, Leuconostoc, Streptococcus, Micrococcus and Sarcina. Penicillium and Mucor grow on hamburger.

4. Fresh Pork Sausage:

It is made up of ground fresh pork to which salt and spices have been added. It must be kept in refrigerators. Alternaria has been found to cause small dark spots refrigerated links. Souring, the most common type of spoilage at 0°C to 11°C has been attributed to growth and acid production by Lactobacillus and Leuconostoc.

Curing salts make meats more favourable to growth of Gram-positive bacteria, yeasts and molds than to Gram-negative bacteria which usually spoil meats. The load of microorganisms on the piece of meat to be cured may influence the deterioration and will affect the curing operation.

6. Dried Beef or Beef Hams:

Beef hams are made spongy by species of Bacillus, sour by a variety of bacteria, red by Halobacterium salinarium or due to Bacillus species. Gas in jars of chipped dried beef has been attributed to a denitrifying aerobic organism that resembles Pseudomonas fluorescens. The gases are oxides of nitrogen. Bacillus species produce CO2.

In the presence of enough moisture, micrococci and yeasts can form a slimy layer. With less moisture, molds may produce fuzziness and discolouration. Various bacteria are responsible for the greening due to the production of peroxides. Surface slimyness often accompanies the greening. Bacon and Ham are the other meats which become putrefied by various bacteria.


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