Meat is defined by FDA as Meat is the properly dressed flesh derived from cattle, swine, sheep or goats sufficiently

mature and in good health at the time of slaughter. There are a wide variety of meat products that are attractive to consumers because of their characteristic color, flavor, and texture. Although scientific literature on biochemical changes during meat conditioning (ageing) and in some meat products were abundantly reported during the 1970s and 1980s, little information was available on the origin of the biochemical changes in other products such as cooked, dry-fermented, and dry-cured meats. The need to improve the processing and quality of these meat products promoted research in the last decades on endogenous enzyme systems that play important roles in these processes, as has been later demonstrated (Flores and Toldr 1993).

1. Muscle 2. Connective tissue

Collagen
Elastin

Adipose tissue
Cartilage Bone

 There are 3 types of muscles in animals. Striated/voluntary muscle which constitutes meat. Smooth/involuntary muscle which is discarded when the animal is dressed. And heart muscle. Striated muscle is composed of long cylindrical cells, called the muscle fibers, which lie parallel to one another and lengthwise of the muscle. Each cell contains a number of nuclei lying close to the outer edge near the membrane or sarcolemma. Muscle also contains lipid-phospholipid and cholesterol. However determining how much lipid is in the muscle cell and how much in the connective tissue is difficult. Striated muscle is believed to contain about 3% lipid. The proteins of muscle cell are numerous and comprise those important in contraction, in the functions of the nucleus, and in the enzymatic reactions of the cell. The salts in the muscle cells are the same as those in the most cells of the body and are at the same concentration.

 Potassium is the most common cation, with magnesium and sodium following. The anions are acid phosphate, bicarbonate, and sulfate in the order of their concentration. The organic compounds that can be separated from muscle by treatment with water and that are not lipid or protein are called extractives. These substances appear in the water when meat is stewed, fricasseed, or in any way treated with moist heat and in the pan juice when meat is roasted or fried. Striated muscle has approximately 1% organic extractives and 1% salts.

Glycogen is the most abundant extractive in resting muscle, but, as pointed out above, the amount decreases after slaughter.
Several other compounds, also present in small amounts, are anserine, carnosine, and carnitine whose structures are shown below.

 This tissue is composed of a few rather large cells scattered through a matrix composed of fibers and amorphous ground substance. There are many types of connective tissue; but they all have this common structure of few cells and numerous fibers in ground substance. The Collagen molecule is a polypeptide chain with a very high percentage of glycine residues.

Beef collagen, which has been studied most extensively contains 19.9% glycine.
It contains a very high percentage of amino acid residues which have nonpolar side chains(glycine, proline, alanine, leucine). Polar side chains are those containing hydroxyl groups(hydroxyproline, threonine,serine and tyrosine). The collagen molecule is coiled and the protofibril is made of parallel molecules coiled or twisted together to form a helix.

 Elastin is the protein that forms the yellow elastic fibers. Unlike collagen, it is not hydrolyzed on boiling with water and consequently a tissue that contains a considerable number of yellow elastic fibers shows little softening or dissolving upon cooking. Adipose tissue is a specialized type of connective tissue in which the cells rather than the intercellular material are most abundant. Fat cells are found scattered in groups in loose connective tissue. Adipose tissue varies in color from very light cream to dark yellow. In general, the outer layers of adipose tissue contain fat with higher iodine numbers and lower melting points than the inner layers. Cartilage is also a specialised type of connective tissue, like all other connective tissue cartilage is composed of cells, fibers, and ground substance. The ground substance is a gel composed of chondroitin sulfate, chondromucoid, and albumoid in water.

Bone is a specialized connective tissue like cartilage, it is composed of cells located in lacunae, fibers, and ground substance in which tiny crystals of salts are deposited. The ground substance is composed of the proteins ossomucoid and ossoalbuminoid surrounding small crystals of salts.
Food gelatin is manufactured from fresh bones by boiling them in water, a process converting collagen to gelatins.

 When an animal dies, the skeletal muscles stiffen in rigor mortis and remain in this condition for a period after which they soften and become flexible again.
The stiffness that develops when muscles pass into the rigor is the result of changes in the proteins. Living muscle fibers contain protein in a soft, pliable gel. During rigor this gel stiffens, but when rigor passes, the muscle again becomes soft and pliable. Finally during cooking, another change called rigor caloris occurs and the proteins stiffen again. In a living muscle changes occur in the proteins actin and myosin when a muscle contracts. The energy for contraction and its accompanying heat production comes principally from these high energy phosphate bonds.

Resynthesis of ATP in the living cell is at the expense of glycogen which passes through a long oxidized by way of the citric acid cycle to CO2 and small bursts of energy are released as each carbon and hydrogen are oxidized.
2(C6H11O5)n + 5[0]
Glycogen

4n CH3COCOOH + H2O
Pyruvic acid

 The series of chemical reactions occuring after slaughter produces enough heat to cause a rise in the temperature of the meat. The average body temperature is 99.7 F in cattle, but shortly after death, the internal temperature of a round beef may rise to 103 F. The fresh meat cools very slowly even in a refrigerator because of the continuing production of heat. Meat that develops a relatively high pH is difficult to cure properly because the pickling salts do not penetrate the meat in a normal rate. Ripening or Aging: After passing of rigor mortis, meat becomes progressively more tender, juicier, and more flavorful.

The speed with which this ripening or aging occurs depends on the time the carcass is kept and the temperature.
Changes occur quite rapidly at room temperature but more slowly at refrigerator temperatures.

 A recent study shows that aging beef at elevated temperatures with high humidity, with air velocity 5 to 20 lineal ft/min and with ultraviolet radiation to control microbes for 2 or 3 days produces beef equal in quality to that aged in a refrigerator 12 to 14 days. Aging caused an increase in the free amino acid nitrogen. The nitrogen in drippings of freshly slaughtered meat was present mostly as non protein nitrogen with a large proportion of it as amino nitrogen. After the beef had aged for two weeks, drippings showed an increase in the amount of NPN. The amino acids histidine, leucine, tyrosine, glutamic acid, and lysine were present in a bound form. Histidine accounted for as much as 26% of the NPN in the extracts. It was concluded that part of the bound histidine is present as carnosine.

The principal pigment present in muscle cells is myoglobin, a red conjugated protein closely related to hemoglobin of the red blood.

Probable Reactions of Myoglobin*

Oxymyoglobin Prot. Fe++ Porph. O2 Bright red

Nitric oxide Denat. Globin Pink

Heat Denat.

O2
Myoglobin Fe++ Porph. H2O Purple Red
denaturation

Nitric Oxide Myoglobin Prot. Fe++ Porph. NO Pink

Prot.

oxidation

reduction

Metmyoglobin Prot. Fe+++ Porph. Brown

Heme Prot. + Fe++ Porph.

oxidation

Hemin Fe+++ Porph. Brown

The chemical and physical changes occur on cooking are numerous and although some studies have been made on this problem the reactions are not all known or understood. They are: 1) 2) 3) 4) 5) Denaturation of the protein, Hydrolysis of collagen to gelatin, Color change, Formation of grid, Development of brown flavor,

6)
7)

Rupture of fat cells and dispersion of fat through the meat, and
Decrease in vitamins and possibly decrease in the nutritive value of the protein.

 Heat denaturation of protein is a familiar experience in food cookery, but it is not always accompained by a toughening of the protein.

Denaturation of a protein molecule is believed to be a series of reactions in

which the protein molecule is altered by splitting of some of the links, particularly some of the hydrogen bonds and sulfur-sulfur links which help maintain the three-dimensional shape of the molecule. The molecular weight of the molecule may not be very much changed in the first steps of the reactions. In heat denaturation, as in other types of denaturation, it is believed that these changes in molecule account for alteration in such properties as solubility and density.

 Griswold studied a number of factors in beef rounds, commercial and prime grades, cooked by various methods.

Collagen was significantly higher in the raw meat for the commercial grade over the prime but not for the top round over bottom round.
The loss of collagen on cooking occurred with all the methods and increased in the internal temperature to which the round was cooked. When pressure cooking was compared, it was found that meat cooked at 10 lbs pressure showed greater losses of collagen than that cooked at 5 lbs pressure. It was higher in meat roasted at 250 F than in that roasted at 300 F or braised.

 When meat is cooked, oxyhemoglobin and oxymyoglobin(red) and hemoglobin (purplish red) are denatured. The ferrous iron in the free porphyrin formed is rapidly oxidised to ferric iron of hemin (brown). Some transformation of oxyhemoglobin, oxymyoglobin, and myoglobin to met hemoglobin and metmyoglobin (brown) can occur.

 This accounts for some of the change in weight that occurs in a piece of meat during cooking. The drip is composed of water carrying a number of soluble compounds as well as come coagulable protein and fat. As cooking proceeds the coagulable protein is denatured by the heat and forms a curd in the pan gravy. The cut of meat and the amount of fattiness, the method of cooking, the extent to which the piece is cooked all obviously affect the amount of fat in the drip. There may also be fat degradation products in the drip. Griswold found that the amount of soluble nitrogen compounds increased in the drippings during cooking but did not find that free amino nitrogen showed an increase.

 The change in the flavor that occurs with cooking is one of the most apparent changes to the man at the table. Cooked meat likewise has this slightly salty, slightly sweet taste but it also possess an aroma that adds greatly to the flavor. The aroma is composed of low molecular weight, volatile compounds such as amines, ammonia, hydrogen sulfide, and organic acids.

These compounds probably arise from the cracking of amino acids during heating.
The reactions may be decarboxylation, deamination, or desulfuring in which either the free amino acid or polypeptides react.

The compounds formed vary according to the species, so that the flavor of lamb is recognizable and different from the flavor of beef.

 Fat cells rupture and fat disperses through the meat on

cooking. The proteins in fat cells of the adipose tissues undergo denaturation on cooking just as all other proteins in the meat.

There is a change in the permeability of the cell walls and

fat flows out.

 The B complex vitamins are all more or less sensitive to heating and thiamin and pantothenic acid are particularly labile. If cooking is prolonged and if the temperature is high, the destruction of the vitamins may be appreciable. There is always some loss. Niacin and riboflavin are more stable to heat do not disappear as rapidly during the cooking of meat. However, the folic acid group is very sensitive to heat, and as much as 90% may disappear.

Ascorbic acid begins to decrease as soon as an animal is slaughtered, during cooking any that is still present will suffer further diminution.
Cooked meat cannot be counted on to supply more than very small amounts of ascorbic acid to our diet.

 The reddening does not make the meat harmful or unpalatable. A red color is produced whenever the meat comes in contact with nitrites, nitrates, carbon monoxide, or sulfites during preparation so that hemoglobin react. This occasionally occurs when nitrites are present in water supplies in very small amounts.

 This causes an excessive loss of drip and a toughening of the meat. The meat becomes stringy as the amount of connective tissue falls and the fat drips out. Not only are the tenderness and juiciness of the meat diminished tribute to the flavor are driven off during the excessive cooking period, and the meat becomes less and less flavorful. A decrease in the nutritive value of the protein may also occur. Overcooking can be the result either of too long a time or too high a temperature.

 The effect of phosphates on the ability of meat to bind water has been investigated in recent years. Some results appear to indicate that the effect is specific for phosphate, others that it depends on the increased pH which occurs. Hamm and Grau found that the addition of 1% phosphate to the sodium chloride that is put in meat has a definite effect on the amount of bound water and decreases the loss of drip. Commercially, phosphate is now added to canned meat as well as to shrimp.

The increased binding of water decreases the shrinkage during processing and improves tenderness.

 Alexander, J. C. and Elvehjem, C. A., Isolation and

Identification of Nitrogenous Compounds of meat, J. Agr. Food Chem., 4, 708-711(1956). Book of Food Chemistry edited by LILLIAN HOAGLAND MEYER., Professor and Head Dept. of Chemistry.

Book of Food Biochemistry and Food Processing., Editor., Y.

H. Hui.