HIGH ENERGY PHOSPHATE AND IMMEDIATE COMPOUNDS PRODUCED

DURING MUSCLE CONVERSION TO MEAT.

During conversion of muscle to meat a lot of compounds are produced including High energy
Phosphate and some immediate compounds. The muscle on the animal at slaughter is living
tissue with complex biochemical and physiological properties. Imposition of a series of
treatments, changing its temperature, tension and fluid and gaseous environment leads to
changing of the muscle to meat. It is agreed that the energy for muscle contraction comes
either directly or indirectly from the splitting of high energy phosphate bonds. Although there
may be other compounds that account for a small percentage of the total high energy
phosphate bonds of cardiac muscle, it is certain that 90% or more of such bonds occur in ATP
and creatine phosphate. A small amount of free ATP is available in the muscle for immediate
use. The energy for synthesis of ATP comes from the breakdown of foods and
phosphocreatine. Phosphocreatine is also known as creatine phosphate and like existing ATP,
it is stored inside muscle cells. Phosphocreatine provides phosphates to ADP molecules,
producing high energy ATP molecules. It is present in low levels in the muscle. Glycolysis
converts glucose to pyruvate, water and NADH, producing two molecules of ATP.

When the muscle starts to contract and needs energy, creatine phosphate transfers its
phosphate back to ADP to form ATP and creatine. This reaction is catalysed by the enzyme
creatine kinase and it occurs very quickly; thus, creatine phosphate-derived ATP powers the
first few seconds of muscle contraction. The source of energy that is used to power the
movement of contraction in working muscles is adenosine triphosphate (ATP), the body’s
biochemical way to store and transport energy. However, ATP is not stored to a great extent
in cells, so once muscle contraction starts, the making of more ATP must start quickly.
In living muscle, the complete oxidation of carbohydrate to carbon dioxide and water uses
aerobic respiration and it releases a lot of energy. Much of this energy is captured by adding a
phosphate group to another molecule that already has two phosphate groups. Thus, adenosine
triphosphate (ATP). The ATP molecule carries this energy within the muscle fibre, and it
may be released to another biochemical system by cleaving off the added phosphate (ATP
ADP + P). muscle contraction is a primary user of ATP in the living animal, but substantial
amounts of ATP are used by the membranes around and within the fibre for maintaining ionic
concentration gradients. One molecule of carbohydrate may be combined with oxygen to add
a phosphate group to each of 36 molecules of ATP. In addition to 36 molecules of ATP, this
produces carbon dioxide and water. However, if the muscle is without oxygen (anoxic)after
slaughter, the most it can normally gain by oxidizing each carbohydrate molecule is 2
molecules of A TP.

Glycogen is the primary storage carbohydrate in muscle fibres and appears in electron
micrographs as single granules or clumps of granules located in the sarcoplasm (cytoplasm)
between myofibrils (contractile fibrils) and under the cell membrane. New research using
scanning tunnelling microscopy, reveals that glycogen granules have a surface all plane
sections of which are circles with a laminar structure which suggests they grow from one
edge rather than a central point. In longitudinal sections of skeletal muscle, glycogen and its
associated enzymes are concentrated at the I bands, one of the transverse bands across the
muscle fibre when examined microscopically.

Glycogen is a polysaccharide formed by the linking together of large numbers of glucose

units. However, the glycogen from some animal tissues is a proteoglucan (glycoprotein) that
may contain other monosaccharides and phosphate ester group. Straight chains of glycogen
are formed by linkages between carbon atoms given numbers 1 and 4, while branch points are
formed by 1-6 linkages. There is a lot of interest in the possibility of post mortem glycogen
breakdown (glycogenolysis) by pathways other than the normal pathway mentioned. If
appreciable amounts of glycogen may be removed without lactic acid formation, this might
account for some of the considerable variability found in post mortem rates of meat
acidification or PH decline. About 5% of muscle glycogen may be contained in lysosomes
and post mortem glycogenolysis may be a combination of both hydrolysis and
phosphorolysis.

Glycogenolysis is the enzymatic degradation of glycogen, and is the first step in the release
of energy by the oxidation of glucose units (glycolysis). Phosphorylase erodes straight chains
(from their non-reducing ends at carbon 4) and attaches a phosphate group to the carbon atom
at position 1 as it removes a glucose unit. Phosphorylase erodes straight chains until it comes
to the fourth glucose unit preceding a branch point. The three glucose units before the fourth
one that carries the branch are removed together, and are added to an adjacent free straight
chain so that the 1-6 linkage thus exposed at the branch point may be severed. A second
enzyme, debranching enzyme, performs this task. Instead of being released as glucose-1-
phosphate, the glucose unit released from a branch point remains as free glucose. Thus, total
glycogenolysis liberates glucose-1-phosphate and glucose in a ratio indicating the ratio
between the mean length of straight chains and the number of branch points. While the
structure of glycogen and the mechanism of glycogenolysis are important in understanding
the conversion of muscles to meat, the remainder of the pathway by which glycogen is
anaerobically oxidized to lactate need only be covered in general principle. The most
important question to be answered is why lactate is produced under anaerobic conditions, yet
hardly at all under aerobic conditions. After a series of steps in the glycolytic pathway,
molecules with six carbon atoms derived from the glucose units of glycogen are split to
produce two molecules of pyruvate, each with three carbon atoms. All the glycolytic enzymes
(except for hexokinase) are concentrated in the I band. If aerobic conditions prevail, pyruvate
formed in the cytosol of the muscle fibre now enters a mitochondrion (the metabolic furnace
of the cell). After entering a mitochondrion, pyruvate is converted to Acetyl-CoA which
becomes fused to oxaloacetate to form citrate. The citrate then is oxidized in the well-known
Krebs' cycle, which is completed by the regeneration of oxaloacetate. Continuous activity of
the Krebs' cycle is fuelled by a range of carbohydrates, fatty acids and amino acids, and is the
primary system for the aerobic generation of energy. Large numbers of molecules of ATP are
produced from ADP by a series of reactions, oxidative phosphorylation, that occur in the
mitochondrial membrane. Under aerobic conditions, the production of two pyruvate
molecules from a glucose-1-phosphate molecule results in the reduction of 2NAD+. Thus,
somewhere else in the muscle fibre, NADH must be re-oxidized for glycolysis to continue.
Aerobically, this occurs as a consequence of mitochondrial Krebs' cycle activity, although
NADH and NAD+ do not actually cross the mitochondrial membrane. In anaerobic living
muscles and in meat, the Krebs' cycle is halted, and NADH is re-oxidized in the cytosol by
lactate dehydrogenase (LDH) during the conversion of pyruvate to lactate. Pyruvate is of no
immediate use anaerobically since mitochondrial oxidation has ceased, but its conversion to
lactate ensures a continued supply of NAD+ for the continuation of glycogenolysis and
anaerobic glycolysis in the cytosol. However, since these events form only the initial stages
of complete carbohydrate oxidation, they do not regenerate much ATP. The net gain of ATP
is reduced to only two molecules of ATP per molecule of glucose-1-phosphate. Molecules of
glucose released from glycogen branch points generate a total net gain of 3ATP. LDH adds
hydrogen to pyruvate to produce lactic acid and exists in a number of isoenzymes separable
electrophoretic ally by their net electrical charge. If LDH-1 is prevalent, it facilitates aerobic
metabolism, where possible, since it is inhibited by pyruvate and lactate. LDH-5 is not
inhibited by high levels of lactate and pyruvate, and it facilitates anaerobic metabolism.
LDH-1 is typical of cardiac muscle while LDH-5 is typical of skeletal muscles, particularly
those adapted for anaerobic conditions during contraction. In skeletal muscles, the ratio of
LDH-1 to LDH-5 corresponds to the dominant activity pattern of a muscle. For example,
muscles capable of sustained activity and which only use aerobic metabolism have high
LDH-1. LDH-5 is the dominant isoenzyme in skeletal muscles from slaughter-weight pigs.

The regulation of glycolysis in a muscle fibre of a live animal is integrated with the metabolic
state of the fibre and its immediate energy needs. The metabolic state of the fibre is
profoundly affected by hormones, particularly adrenaline, and by the extent of recent
contractile activity of the fibre. Phosphorylase is particularly important in the conversion of
muscle to meat since it may be a primary control site for post mortem glycolysis.

Phosphorylase in muscle is most active when it is, itself, phosphorylated (a). When
dephosphorylated, it is less active (b). In general terms, therefore, phosphorylase is switched
on and off by the addition or removal of its phosphate, with on and off states being relative
rather than absolute. The activity of phosphorylase b is dependent on the presence of AMP
(Adenosine monophosphate) but the activity of phosphorylase a is not. There are two
conflicting requirements that make the mechanism for the activation of phosphorylase rather
complex. Firstly, since phosphorylase initiates the release of considerable amounts of
chemical energy, there must be safeguards to prevent its uncontrolled activity. In stress-
susceptible pigs, for example, the uncontrolled activity of anaerobic glycolysis may lead to
excessive heat production and to a level of acidity that may soon prove fatal. The conflicting
requirement is that the vast amounts of phosphorylase spread through the muscle mass must
be rapidly activated by relatively small amounts of adrenaline. The adrenaline activation of
severely frightened animals often is called the "fight or flight" response: neither of these
responses is likely to be of much survival value if the anaerobic energy supply to body
muscles is delayed. The conflicting demands for fail-safe but rapid activation are satisfied by
two particular features of the activation system. Firstly, the conversion of phosphorylase b to
phosphorylase a is inhibited locally in each muscle fibre by high concentrations of ATP and
glucose-6-phosphate (an intermediate in the conversion of glycogen to lactate). Thus, if the
energy released by phosphorylase is not rapidly consumed, the energy release system shuts
down. If the energy is used, however, AMP and phosphate (from ATP ADP + P and from
ADP AMP + P) further enhance the activation of phosphorylase. Secondly, to enable the
rapid activation of phosphorylase throughout the musculature, the relatively small amounts of
adrenaline that arrive at the muscle initiate a series of biochemical changes functioning as an
amplifier. A small input leads to a large output. Adrenaline causes adenyl cyclase to increase
its formation, from ATP, of cyclic AMP. Then cyclic AMP activates protein kinase. With
ATP and magnesium ions present, protein kinase then phosphorylates another enzyme,
phosphorylase b kinase b. The active form, phosphorylase b kinase a, in the presence of
magnesium ions, finally activates phosphorylase b to phosphorylase a. As a final safety
factor, if the supply of inorganic phosphate is inadequate, even phosphorylase a will be
relatively inactive but the system will be primed for rapid energy production once muscle
contraction is initiated.

When animals require energy anaerobically during normal activity, phosphorylase b kinase
is activated by calcium ions released from the sarcoplasmic reticulum - normally the trigger
for muscle contraction in living muscle. Glycogen granules are closely related to the
sarcoplasmic reticulum and to glycogenolytic enzymes as part of a structural complex. The
activation system linking muscle contraction to glycogenolysis is short lived to avoid the
continuous use and depletion of glycogen reserves. Glycogen is a rapidly available energy
source for both brief muscle activity and the early stages of sustained activity. Phosphorylase
activity is reduced by phosphatase, which dephosphorylates phosphorylase a and
phosphorylase b kinase, when muscle activity ceases or an animal recovers from fright. Many
features of the system for activating phosphorylase are shared with the activation system for
glycogen synthesis, but the shared features are opposite in effect. Thus, the muscle fibre does
not attempt to synthesize new glycogen at the same time that it is breaking it down, and vice
Versa.

tt

The graph above shows how energy is used in the muscles

Conclusion

In conclusion, several immediate compounds are produced to drive effective conversion of

muscle to meat these compounds are lactic acid, ATP, ADP, Creatine-phosphate (high energy
phosphate).
REFERENCES

Sahoo, J.(2009). Meat science

Kerth, c. (2013). The science of meat quality

Warris, p. (2009). Meat science . Bristol: university

Samantha fowler, Rabacca Roush, James wise. 2018. concepts of Biology

Stephanie clark , Stephanie jung. 2004. Encyclopedia of meat sciences. Second

Edition . Wiley Blackwell.