MEAT COLOR

Dr. R. EMILIN RENITTA

AP/FPT
• The appearance of meat is important to retail
shoppers.
• Appearance includes size; shape; the relative
quantities and distribution of lean tissue, fat and
bone; and color.
• Each of these factors is evaluated, either
consciously or unconsciously, as buyers examine
meat on retail display.
• Consumers consider that the color of lean tissue is
a particularly important indicator of meat quality.
• Red meat tends to turn brown with time when
exposed to air.
• Meat also tends to spoil with time due to
microbiological activity, so the browning of
meat with time is a rough indicator of spoilage.
• Important to realize that the two events—
browning and spoilage—are largely
independent, and with modern hygiene control,
meat exposed to air will become brown long
before spoilage develops.
• Unlike many fish species, the meat of land
mammals—particularly if undomesticated—is
characteristically red.
Fresh Meat Colour:
• Fresh meat colour is due to myoglobin and
haemoglobin.
• Myoglobin is a conjugate protein, consists of a
typical amino acid protein chain and a non-protein
haeme molecule.
• The colour of fresh meat does not influence its
palatability and nutritive value, yet it is regarded
as a reflection on the quality by the consumers.
• The conjugate protein myoglobin provides the red
colour of the muscle and serves as a storage site
for oxygen in muscle.
Myoglobin
• Myoglobin (and its various chemical forms) is not
the only pigments in muscle but is generally in
large enough quantity to colour the tissue.
• Other pigments of important to living tissues
(contribute little to the total colour) are
hemoglobin cytochromes, cyanocobalamin (B12 ),
flavins etc.
• Cytochrome is an enzyme involved in oxidative
phosphorylation, contain iron but contribute very
little to meat colour.
• Differences in Mb – due to variations in species,
breed, age, sex, type of muscle and training
exercise etc.
Chemistry of Myoglobin
• Meat pigments mainly have two proteins i.e.
Hemoglobin(Hb) – pigment of blood and Myoglobin(Mb) –
pigment of muscles.
• In well bled tissues Mb constitutes 80-90 per cent of total
pigments.
• The two pigments are similar in structure, except that Mb
molecule is one fourth as large as Hb.
• Mb molecule consists of a haematin nucleus attached to a
protein component of globulin type called globin.
• The mol. wt. is about 17000. The haematin portion
comprises of a ring of four pyrrole nuclei linked together by
methene bridge (-CH=) and coordinated with a central iron
atom.
• The haem moity of Mb (Porphyrin ring with iron atom in
ferrous state)
Myoglobin Haemoglobin
• Myoglobin is chemically very similar to the blood
protein hemoglobin, which also contains iron
bound in porphyrin.
• Muscle contains some hemoglobin, but its
hemoglobin content is much lower than that of
myoglobin.
• This hemoglobin is restricted to the fine vascular
supply that permeates the muscle.
• The drip that leaks from raw steaks and other meat
cuts is not blood as is commonly believed, but
mainly myoglobin dissolved in the muscle cell
exudate.
• Because myoglobin is the dominant pigment in
muscle, measurements of iron concentration,
myoglobin concentration, and color are all strongly
correlated.
• If one muscle appears redder than another, it very
likely contains more myoglobin and, thus, more
iron.
• The porphyrin ring structure held in the confines
of the myoglobin protein accounts for four of the
six coordination sites available on the iron atom.
• These four sites are the nitrogen atoms of the
porphyrin’s pyrrole groups.
• A fifth coordination site is a strategically
placed histidine molecule resident in the
globular protein.
• The sixth coordination site is available for
binding oxygen or other small molecule that
qualifies.
• Binding at the sixth site is largely responsible
for the various colors of meat, mainly red, but
also purple, brown, and other colors.
• Within an animal, different muscles often have
different concentrations of myoglobin, generally
reflecting their role in the animal.
• Muscles involved in sustained repetitive action,
like breathing (diaphragma), contain higher
concentrations of myoglobin than muscles used
less often.
• The lateral line muscle of fish, which is used for
sustained, low-power movement, is very much
redder than the muscle groups used for short bursts
of high-power movement.
• The pectoralis muscle of chicken, used for power
takeoffs, is paler than leg muscles.
• Muscles low in myoglobin are generally tailored to
glycolysis as a means of generating ATP, whereas
muscles rich in myoglobin generate ATP through
oxidative metabolism.
• It therefore follows that redder muscles are also
richer in mitochondria and, as part of the oxidative
machinery, richer in cytochromes.
• cytochromes are colored, again due to iron bound
in porphyrin.
• However, cytochromes are present in much lower
concentrations than myoglobin. Thus, the color of
meat is dominated by the color reactions of
myoglobin.
THE CHEMISTRY OF MYOGLOBIN COLOR
• A. Reactions of Myoglobin with Oxygen
• In its role as an oxygen store, the sixth
coordination site on the iron in myoglobin’s
porphyrin ring reversibly binds molecular
oxygen (Fig. 1).
• When bound, the color of myoglobin changes
from a purple-red to a bright red (Reaction 1).
Myoglobin O2 → Oxymyoglobin (Reaction 1)
(Purple-red) (Bright red)
•
• Myoglobin in the ferric state—called
metmyoglobin—cannot bind oxygen but binds a
molecule of water instead.
• Metmyoglobin’s inability to bind oxygen is
crucially important because metmyoglobin slowly
forms from oxymyoglobin, both in live muscle and
in meat.
• In the case of the live animal, metmyoglobin
formation must be avoided because metmyoglobin
is useless as a oxygen store.
• In the case of meat, metmyoglobin formation must
be avoided because this pigment is brown and not
the attractive bright red that consumers value
• The reaction of oxymyoglobin to form
metmyoglobin is termed autoxidation because it
occurs with oxymyoglobin as the sole reacting
species.

• Although autoxidation is a comparatively slow

reaction, it is still commercially important because
meat on retail display in air or in an
oxygen-enriched atmosphere must maintain a
bright-red color for several days
Effect of pH and Temperature on Autoxidation
• The rate is high around pH 5.5 and decreases
markedly as the pH increases to around 6.0
then slowly levels out.
• This result suggests that autoxidation will
proceed at different rates in meat of different
pH values.
• As might be expected, the higher the
temperature the higher the autoxidation rate.
• A decrease in temperature from 22° to 2°C
resulted in a 40-fold decrease in the rate of
autoxidation, whatever the pH.
Reactions of Myoglobin with NO and CO
• The complexes, nitric oxide myoglobin (Mb2NO)
and carboxymyoglobin (Mb2CO) maintain
myoglobin in the ferrous form.
• Although NO dissociates from the myoglobin
complex far more slowly than does oxygen, Mb2NO
is still considered unstable.
• This is because in meats, oxygen is often present in
much higher concentrations than NO, which is
usually added by way of traces of sodium nitrite
during conventional salting.
• Excess oxygen can displace NO, which in turn
can be lost to through oxidation to nitrate.
• In curing technology, the loss of NO is
prevented by cooking, which generates a stable
pink compound, nitrosylhemochrome, which is
responsible for the characteristic pink color of
cured meats.
• Carbon monoxide (CO) has a stronger affinity
for myoglobin (and hemoglobin) than oxygen.
• When pale meats like pork are cooked in a gas
oven, pinking is sometimes evident on the
outer layers of the meat
• Combustion generates small quantities of CO
or NO that bind to the myoglobin, forming
stable pink compounds that are visible on a
pale background
Metmyoglobin Reductase
• In the live animal, concentrations of
metmyoglobin in muscle are kept very low due
to reductase activity in the muscle tissue.
• Metmyoglobin reductase activity is located
predominantly on the mitochondrial surface.
• The enzyme requires the reductant NADH,
and cytochrome b5 as an electron transfer
mediator.
• The pH activity profile shows a peak around
pH 6.5, falling steeply as pH falls.
• The enzyme does not lose activity in stored
meat and is unaffected by oxygen.
• Therefore it will be active both in the
oxygenated surface layer of meat or deeper in
anaerobic tissue, provided NADH is also
present.
• Each of these properties is important in
understanding the color behavior of meat on
display.
• oxygen consumption decreases with time
postmortem so the balance between metabolic
oxygen consumption and oxygen binding by
myoglobin changes with time.
• The enzyme metmyoglobin reductase remains
active in meat and providing the reductant
NADH is present, metmyoglobin can be
reduced to the ferrous form (myoglobin)
capable of binding oxygen to produce
oxymyoglobin.
Main Factors affecting meat color
Chronology of Meat Color from Slaughter to Display
• At slaughter, the vascular system ceases to deliver oxygen
to muscle, and within minutes the muscle becomes anoxic.
• Using the human heart muscle as an analogy, anoxia in
skeletal muscles can be viewed as a “muscle attack.”
• The oxymyoglobin present in muscle at the time of
slaughter becomes depleted of oxygen that is consumed in
mitochondria to sustain respiration.
• The muscle takes on the purple-red hue of (deoxy)
myoglobin.
• At this time the muscle pH is still close to 7.0, the normal
pH in live, rested muscle.
• In the absence of oxygen, glycolysis is
accelerated in muscle, generating lactate as the
end product and hydrogen ions from the
associated cycling of ATP and ADP.
• The pH falls and if sufficient glycogen is
present, a final (ultimate) pH of about 5.5 is
attained.
• As the pH falls towards 5.5, the myofibrillar
proteins—principally actin and
myosin—approach their isoelectric points and
in that state they bind less water, creating gaps
between the myofibrils.
• This creates steps in refractive indices which bend
light as it crosses from one medium to another
resulting in light scattering and increased
reflectivity
• The degree of scatter increases with the size of the
gap and the extent to which proteins are denatured.
• For muscle in rigor at a normal pH, translucency is
much reduced, and muscle takes on the familiar
appearance of meat, particularly as atmospheric
oxygen contacts exposed meat surfaces and turns
them red.
• In the meat trade, the meat is said to “bloom” and
is the color consumers associate with freshness and
high quality.
• If the meat remains on display in the meat case, it
will eventually turn brown and become unsaleable.
• The brown pigment metmyoglobin is responsible
for this color change, and where this pigment first
appears in a meat cut on display can be predicted
from the biochemistry of its formation.
• Metmyoglobin slowly forms wherever oxygen
penetrates, but provided NADH is present and
metmyogloin reductase is active, metmyoglobin is
reduced back to the oxygen-binding form,
myoglobin.
• In the degradative, oxidative environment of
muscle as meat on display, NADH eventually
becomes depleted, and the rate of
metmyoglobin formation begins to exceed the
rate of its reduction to myoglobin.
• Because the rate constant for metmyoglobin
formation is greatest at low oxygen
concentrations
• It is unsurprising that metmyoglobin is first
evident at the interface between the outer
oxymyoglobin layer and the inner bulk of
anoxic meat where deoxymyoglobin prevails
• The three different colors can often be seen if
meat is cut with sharp blade at right angles to
the exposed surface.
• As time on display increases, the brown layer
migration occurs both inward and outward
until the surface of the steak is completely
brown.
• Migration toward the center of the meat occurs
because as the oxygen-consuming activity of
the meat declines, the concentration of oxygen
rises ultimately leading to metmyoglobin
formation.
MEASUREMENT OF MEAT COLOR
• Meat color is measured for many reasons, including
grading, matching customer specifications, measuring
consumer response to color, measuring color changes,
and determining the causes of discoloration.
• Meat mainly reflects light in a diffuse way from the
surface.
• There is some spectral reflectance from the glossy
surface of wet meat, and because meat is partially
translucent, a portion of the incident light is
transmitted below the surface and reflected internally.
• When the reflected color of meat is assessed or
measured, samples must be sufficiently thick to
ensure that no light is reflected from the background.
• Meat colour important as it attributes to
eye-appeal. A colour has three attributes-hue,
chroma, value.
• Hue -That normally think of as a colour-yellow,
green, red, blue etc. It is the wave length of the
light radiation.
• Chroma - Refers to purity or saturation-depth or
intensity of the fundamental colour with respect
to the white light mixed in with it.
• Value (Brightness, luminosity) overall reflectance
of the colour-in the other words it reflects the
extent to which the hue is diluted with black.)
• Three primaries are –red, blue and green. Any
colour may be matched exactly by a suitable
mixture of three primaries.
• Tristimulus value- the relative amounts of the
primaries required to match a given colour.
• Instruments used to measure colour: 1.
Lovibond Tintometer (Colorimeter) 2. Hunter
Colorimeter (tricolorimetric system) 3.
Portable colour comparator-developed by
Steinhauf (1964), Lohse and Pfan (1964
• Above all, the measurement of meat color
demands a systematic approach to data collection,
whether color is scored by a sensory panel
(subjective assessment) or measured by an
instrument (objective assessment).
• In the case of panel assessment, the usual
techniques of discrimination are used— triangle
tests, intensity, preference.
• For instance, panelists scoring the color
acceptability of lean meat can be unconsciously
influenced by the color of the associated fat.
• Objective (instrumental) measurements are
based on three-dimensional “color space”
parameters and are usually performed with
reflectance colorimeters.
• A recent reference method for meat color
measurement specifies the L*, a*, b* color
scale .L* is a measure of lightness where 0
equals black and 100 equals white Values of
a* indicate redness and greenness, and b*
values indicate yellowness and blueness.
•
APPLIED ASPECTS OF COLOR IN MEAT
A. Species, Animal Age, and Muscle Type
• The concentration of myoglobin in muscle varies
not only with species, breeds, and individual
muscles but also with age.
• Concomitantly, the oxidative activity due to
mitochondria also increases with animal age.
• With higher concentrations of myoglobin, the
potential for bright red meat is higher.
• Opposing this effect is the oxygen-consuming
activity of muscle, which tends to lower the
concentration of oxygen in the meat, so raising the
potential for metmyoglobin formation
Effect of Vitamins on Color Stability Supplementation of
livestock diets with the vitamin E (-tocopherol)
• Results in a reduced oxidation of lipids in the meat
from animals fed those diets
• This vitamin, which is fat soluble and occurs in the
membranes that ramify all cells, not only helps prevent
lipid oxidation but also retards metmyoglobin
formation in meat exposed to air so improving color
stability.
• Vitamin E is not synthesized in animal cells; instead it
must be obtained from plants through the diet.
• Meat from unsupplemented grain-finished cattle has a
vitamin E content of around 0.5 g/g of lean meat
whereas a typical content in equivalent pasture-fed
animals is 5 g/g
• If browned meat is sprayed with a dilute
solution of ascorbic acid (vitamin C) or sodium
ascorbate, metmyoglobin is rapidly reduced to
myoglobin.
• In the presence of air, the bloomed appearance
is restored. This effect is due to the reducing
power of this vitamin.
• Vitamin C occurs naturally in muscle, and in
the living cell, it regenerates vitamin E,
suggesting it plays an integral role in
maintaining the color stability of meat.
Effect of Processing Conditions of carcasses
• Have major effects on meat quality,
particularly tenderness. However, processing
also affects other qualities such as color.
• The rate of postmortem pH fall in pig muscle
is typically double that in ruminant muscle.
• As a result, pig muscle is subjected to
relatively low pH values at relatively high
temperatures.
• Under these conditions, myofibrillar proteins
tend to denature, and in this state are more
reflective and so the meat appears lighter.
• A parallel condition is seen in fish, where
biochemically unstable fish proteins denature when
exposed to an acidic sushi marinade even at chill
temperatures.)
• Because porcine muscles contain significant
concentrations of myoglobin, the net color attained on
rapid pH fall when muscles are warm is light red, a
color most consumers consider attractive for pork.
Effect of Packaging, Temperature, Storage, and Display
Conditions
• The packaging of meat to protect it against microbial
contamination, and low temperature storage to slow
microbial growth are relatively recent innovations in
the history of the meat trade.
Frozen Meat
• When meat freezes, the formation of ice crystals
within what was once a uniformly hydrated
product changes its optical properties.
• The meat becomes less reflective, so frozen meat
looks darker than chilled.
• On exposure to air, frozen meat blooms or
maintains the blooming existing at the time of
freezing.
• If bloomed frozen meat remains exposed to air,
blooming is maintained for a time but is eventually
lost.
• The color of the frozen meat becomes dark
red-brown that is a combination of low light
reflection, surface drying, and metmyoglobin
formation.
• Historically, much frozen meat in international
trade was stored and transported exposed to air,
producing a very unattractive product. Frozen meat
may be cut and thawed before display.
• After thawing, a freshly exposed surface of meat
will bloom, but the meat remains less reflective
than meat that was never frozen and so appears
darker and less attractive than chilled meat
Chilled Meat
• Meat freezes at 1.5°C, and meat stored at
any temperature between this and ambient
temperature.
• The temperature/time history between
these limits has a significant effect on
bloomed color stability, which in turn
translates to the display life before meat
turns brown.
•
Light
• During retail display the pack is exposed to
light, whether natural through windows, or by
incandescent or fluorescent lights in display
cabinets.
• Specific profiles are used to emphasize the
quality sought by consumers, often by
enhancing the red end of the spectrum so
reflected red wavelengths strike the eye.
• However, light also promotes metmyoglobin
formation through photochemical autoxidation.
Effect of Abnormal Rigor Conditions on Meat Color
• The abnormal appearance of pale, soft, exudative
pork (PSE pork) and of dark-cutting meat can be
explained in biochemical and biophysical terms.
• PSE pork is pale for several reasons. First, the
rapid fall in muscle pH while the muscles are
warm causes denaturation of muscle proteins that
increase reflectivity beyond the normal reflectivity
of myofibrillar proteins in rigor
• Second, the excessive drip takes myoglobin with
it.
• Dark-cutting meat is dark red for roughly the
opposite reasons. Relatively undenatured
proteins are unreflective, so the meat appears
darker due to absorption of light.
• The water binding capacity of dark-cutting
meat is high, so no myoglobin is lost through
drip.
• Finally, the oxygen consumption rate is high
so surface blooming is poor
Effect of Ionizing Radiation
• Ionizing radiation is used to reduce or eliminate
microbiological contamination in foods.
• The radiation is generated by radioactive isotopes
( -radiation from 60Co), x-rays, or beams of
high-energy electrons.
• Whatever the source, the radiation produces free
radicals and electrons as primary species that
decay to produce charged and neutral free radicals.
• The use of ionizing radiation to reduce
contamination by pathogenic and spoilage
organisms is generally regarded as safe up to a
limit.
.
• However, the generation of free radicals in any
food is likely to cause some adverse effects,
particularly where oxygen-containing free radicals
formed in a high-moisture food like meat can react
with fats and proteins.
• Free radicals accelerate the onset of rancidity.
However, the concern here is color.
• Irradiation of meats often causes an increase in
redness, although the degree is dose- and meat
species–dependent.
• Poultry and pork tend to redden more than beef
and lamb.
Cooked Meat
• Color On cooking, meat tends to lighten in
color and also tends to turn a brown-gray hue.
• The lightening is due to an increased
reflection of light arising from light scattering
by denatured proteins.
• The loss of chroma and change in hue arise
from changes to myoglobin. The compound
largely responsible for the browngray hue is
globin hemichrome(s).
FAT COLOR
• White or cream-white intermuscular and
marbling fat
• Fat can be colored by carotenoid pigments
from the animal’s feed and heme pigments
from blood or drip.
• Fat from pasture-fed animals always contains
a mixture of yellow/orange carotenoid
pigments, mainly –carotene.
• Concentrations of carotene in fat vary
between breeds and with animal management
practices.
• Yellow fat is not a problem when animals are
fed on grain. When pasture-fed animals are
finished on grain, at least four weeks are
required to reduce the carotene in fat to
acceptable levels.
• Yellow discoloration is much most apparent in
hot fat on freshly slaughtered animals.
• As the fat cools and crystallizes, it appears
progressively paler.
• This is because warm fat is more translucent
than cold fat.