Professional Documents
Culture Documents
(YFS20203)
ASSIGNMENT 2
DATE OF
SUBMISSION:
12 APRIL 2023
PREPARED FOR:
PREPARED BY:
NO SUBTOPICS PAGE NO
5. INSTRUMET
8. CONCLUSION
9. REFERENCES
INTRODUCTION OF RIGOR MORTIS
The most important change that occurs in postmortem muscle is the development of rigor
mortis, which means stiffness of the muscle. The primary cause of onset of rigor is post
mortem decline in the level of ATP. The process takes from 7-24 hrs depending on the
species; however it is linked with the rate of depletion of ATP in muscle. The entire process
Pre-rigor stage
During early stages of postmortem or pre-rigor stage, the concentration of ATP more or less
remains constant as the muscle tries to maintain ATP levels by an active creatine kinase.
However it will lead to liberation of creatine from muscle. Thus, in this state creatine
phosphate levels fall more rapidly than that of ATPs. ATPs provides a cushioning effect for
the filaments of two proteins i.e. actin and myosin. This results in a meat which is soft and
pliable. In the pre-rigor stage, myosin dissociates from actin and can be extracted in solution
of high ionic strength. Water holding capacity of the muscle proteins remains high during
this stage.
Rigor mortis
This period is very important as meat becomes rigid and stiff. Onset of rigor mortis may be
8-10 hours postmortem and it may last in 15-20 hours in meat. Onset of rigor is
demonstrated by fall in ATP, loss of extensibility of muscles and contraction of tissues. Time
difference between the death of an animal and the onset of rigor is termed the delay phase.
This period depends upon a number of factors such as age, health, size of carcass, the
amount of fat cover, nutritional status of animal, pH and glycogen level, temperature as well.
ATP plays a very important role in this stage. As ATP level falls two muscle proteins
for contraction. This is the necessary criterion for development of rigor mortis. The extent of
contraction of the muscles is determined by estimation of length of the sacromere within the
myofibril. Meat which is cooked in this state is very tough in texture. The water holding
capacity of the muscle protein remains minimum during this stage due to drop in pH as it
comes closer to their iso-electric point i.e. pH 5.3-5.5. If the ultimate pH (5.60) falls too
quickly, carcass would still be warm adversely affecting water holding capacity and prevailing
partial denaturation of protein resulting into pale, soft and exudative (PSE) muscle ultimately
leading to lower yield of the meat. This is often encountered in pigs having sufficient
reserves of glycogen. On the other hand if inadequately feed or fasting animal having
minimum reserve of glycogen is subjected for slaughtering; dark, firm and dry (DFD) meat
conditions. DFD meat is having pH not below 6.0 and is darker in colour and susceptible for
microbial growth.
During the post rigor stage meat tenderizes and organoleptically acceptable when it is kept
cold for sometime after rigor mortis. The muscle again becomes soft and pliable with
improved flavour and juiciness. The post rigor meat provides lesser problems in toughness,
when cooked compared to that cooked in rigor. Meat gradually reaches to an optimum
tenderness period after an ageing period of 10-18 days stored following the dissolution of
rigor. However, prolonged storage of meat in some species may result in some problems viz.
recommended to consume meat before it gets spoiled. The ageing which is also called as
e.g. holding meat for 3 days period in UV to control the microbial growth at surface. While in
the case of pork, ageing is not recommended rather to eat fresh as it develops rapid onset of
fat rancidity even at low temperature. On the other hand beef is generally aged and lamb &
for this desirable changes are still been researchable issue, however it is now a fact that in
post- rigor state actomyosin complex does not dissociate but other subtle changes occur
like, increase in the water holding capacity due to increase osmotic pressure in the muscle
fibre due to net inside movement of cations and breakdown of proteins by liberated
proteolytic enzymes, the cathepsins may lead to tenderness. While cooking of meat
tenderizing agents such as enzyme calpain etc are added which breaks down the stiff
1. Thawing rigor
2. Cold shortening
3. Heat Ring
4. Blood splash
1. Thawing rigor:
Muscle is frozen before rigor mortis occurs because, ATP hasn’t been used in rigor mortis
events and is high when the muscle is frozen and When thawing occurs, calcium is released
from the Sarcoplasmic Reticulum, causing a massive contraction because of the high ATP
2. Cold shortening:
Similar events occur when cold muscle shortens except it isn’t frozen (chilled below 15ºC –
16ºC onset of rigor mortis occurs). Because of too quick chilling, the SR is unable to hold the
calcium. Muscle contraction occurs while ATP still is available. Electrical stimulation helps
3. Heat Ring:
It is found in carcasses with a thin rind i.e. lean carcass which are not chilled properly. Outer
ring of muscle gets cold too quickly because of slower glycolytic rate and slower pH decline,
this Result is an undesirable ring around the muscle that is darker in color, coarser in texture.
4. Blood splash:
Blood splash is caused by rupture of capillaries, usually between stunning and sticking
times. This occurs due to blood pressure increases after stunning and results in small blood
spots in muscles. This problem mostly occurs in hogs and poultry. An excessive stun:stick
Intrinsic factors
• Species of animal.
• Type of muscle
• Amount of glycogen
phosphate
Extrinsic factors
• Atmospheric temperature
Main pigment of muscle is myoglobin, a red colored conjugated protein, which is not
completely bled during exsanguinations.Most of the blood cells remain in numerous blood
vessels and traverse the muscle tissue, which contains haemoglobin. Other things, like
some coloured enzymes like heme pigments also occur in muscle. They are cytochromes
and peroxidase. The molecular weight of myoglobin is one fourth of haemoglobin, likewise
Loss of immunity:
During post mortem period, body defense mechanism stops operating and membrane
proteins alter the properties of meat membrane, which leads to the invasion of
microorganisms. However, low pH cause some defense against the invading microorganism.
Handling and precautions during meat slaughtering can resist Invasion of organisms to some
extent.
Enzymes like cathepsin which remain inactive in living tissue become active as muscle pH
drops.These initiates the degradation of muscle protein and thus loose the structure integrity.
inhibit the action of calpains (Brahman cattle contain higher levels). Thus, if an animal has a
higher calpastatin level, the calpains are less active, and cooler aging has less affect on
muscle tenderness. Brahman cattle are naturally tougher because of higher contents of
calpastatin.
TYPE OF MEAT
Slow-twitch muscle fibres are what make up the muscles in red or dark meat. These muscles
require a constant energy source because they are used for prolonged durations of activity,
including standing or walking. Muscle cells utilise oxygen, which is stored in the protein
myoglobin, to generate the energy required for continuous activity. Myoglobin is a protein
with a lot of pigment. The meat will be redder or darker the more myoglobin there is in the
cells.
Muscles with fast-twitch fibres are what make up white flesh. When running away from
danger, fast-twitch muscles are required for short bursts of action. Glycogen, which is
likewise stored in the muscles, provides energy to these muscles.
When white flesh is raw, it has a translucent, "glassy" appearance. When meat is cooked,
the proteins coagulate and denature, making the meat opaque and white.
Although pig is frequently referred to as "the other white meat," both cows and pigs are
sources of dark meat. Myoglobin is present in pig muscles, but it is not as concentrated as it
is in beef. Fish primarily contain white flesh, while chickens have a mixture of dark and white
meat.
STRUCTURE
Muscle is made of a number of fibre bundles (1.0 mm thick), composed of a group of fibers,
(0.1 mm thick) held together by a structure of connective tissues or perimysium (figure 22.1).
Connective tissues which provide edible texture, structure and flexibility to the muscles,
composed of fibrous protein collagen, reticulin, and elastin. Muscle fiber, a unit of muscle
sarcolemma and consists of myofibrils of 1-2 micron size. Myofibrils are separated by
sarcoplasmic reticulum, a fine network of tubules. Each fibre is filled with sarcoplasm
containing mitochondria, enzymes, glycogen, ATP, creatine, and myoglobin. The myofibrils
are cross striated to give rise to understanding of physical structure of muscles (dark or A
and light or I/Z bands). The unit of fibril is sacromere which lies between adjacent two Z-
bands. Fibrils consist of two sets of filaments i.e. myosin and F-actin. Contraction and
relaxation of striated muscles takes place due to interaction between actin, myosin and ATP.
In the presence of magnesium and calcium ions, myosin liberates ATP which results in
muscle contraction.
The composition of muscle is highly variable depending upon specie, type of muscle, animal
maturity and the treatments given to the animal before its slaughtering. Variation in the
composition ultimately affects the nutritional and functional profile muscle tissues.
The lipid components of muscle tissue vary more widely than do the amino acid in fish
muscle, the differences have been made in the concept of lean or white fish and fatty fish. In
lean fish, storage fat is carried in the liver. Muscle of lean fish contains <1% lipid, mostly
phospholipids, located in the membrane. In fatty fish, depot fat apparently occurs as
INSTRUMENT
A rigorometer is a device for measuring the loss of extensibility as rigor mortis develops. The
first rigorometer was developed in the late 1930s by one of the pioneer meat scientists
In the diagram above, the muscle strip (M) is loaded with a weight (W) as the platform (P)
drops. Whether or not the muscle extends when loaded is detected by the transducer
SEQUENCES OF EVENT IN RIGOR MORTIS
The most easily observed structural change during the development of rigor is the change
from soft pliable tissue to rigid inextensible tissue. This rigidity is brought about by a series of
biochemical events that take place within muscle following death of the animal. Ultimately
these events lead to a fall in ATP concentration and the gradual accumulation of actomyosin
cross-bridges resulting in the loss of muscle extensibility. The development of rigor can be
measured by the degree of stretching while alternatively loading and unloading the muscle,
and in most cases a carcase will have reached rigor mortis (or completely lost muscle
extensibility) when the pH of the muscle has fallen to about pH. Changes in muscle
extensively over the pre-rigor time for post-mortem psoas muscle from a rabbit. In this
instance the muscle was extracted from an anaesthetist rabbit and was held at 17oC. As can
be seen when the muscle becomes rigid rigor set in after about 10 hours post-mortem.
For example,rigor mortis in beef completely occurs within 12 hours. But the process will take
During the delay phase, ATP is still being synthesised. During the fast phase, each myofibre
runs out of ATP, and during the last post-rigor phase, enough myofibres have developed
rigour mortis to limit further extensibility. Sometimes, as a muscle enters rigidity, it will
contract slowly and weakly. The health of the animal at the time of slaughter has a significant
impact on both the behaviour of muscle strips in a rigorometer and the behaviour of
At body temperature but not at room temperature, a calm animal gives a long latency, a
sluggish fast phase, and a reduction in unloaded length. At body temperature, but not at
room temperature, an animal resisting during the slaughter causes a brief delay, a brief fast
phase, and a reduction in unloaded length. At both body and room temperature, a fatigued
animal has a very short or nonexistent delay period, a very brief fast phase, and a shorter
unloaded length. At body temperature but not at room temperature, a starving animal
exhibits a short latency period, a relatively long fast phase, and a decrease in unloaded
duration.
Depending on the state of the animal at the moment of slaughter and the temperature of the
muscle, some muscles may attempt to shorten when they enter rigour mortis (superficial
muscles will cool faster if not extensively insulated by fat). Because they are already
stretched from the weight of the hanging corpse, some of these muscles won't be able to
shorten at all, but unfettered muscles, like the muscles in the posterior hindlimb, are free to
contract. The forelimb may be elevated against gravity if the rigour contraction is more
As a conclusion, rigour is important as the length of the sarcomeres, and hence the muscle's
length and maybe the meat's texture, are fixed by rigour, which is crucial. Tough meat is
typically produced by muscles severely constricted during rigour; tender meat is typically
produced by relaxed or extended muscles.rigour mortis has an impact on meat quality. The
stiffening and acidity brought on by glycogenolysis during the rigour mortis setting in are the
key alterations in muscle tissue affecting eventual meat quality. The kinetics of acidification,
in short, has a significant impact on colour and water-holding capacity.After 36 hours, rigour
mortis typically vanishes, and secondary flaccidity then sets in. The body tissue begins to
decompose in the late post-mortem phase, which can be best described by decomposition
of rigour mortis during this time in the hot box is a crucial factor (stiffness of death). Live
animals have fluid, free-moving muscle that enables movement. Rigour mortis eventually
develops as a result of the muscles tightening up after an animal passes away because of
https://www.beefresearch.org/grading/LMDisplay.html?chp=2&sc=7&A=undefined&B
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