JFS R: Concise Reviews/Hypotheses in Food Science

R: Concise Reviews in Food Science

Does It Look Cooked? A Review of Factors
That Influence Cooked Meat Color
NICOLA J. KING (NÉE TURNER) AND ROSEMARY WHYTE

ABSTRACT: Adequate cooking of meat is necessary to inactivate microbial pathogens. This is particularly important
for ground meat products and some variety meats where pathogens can be present internally. Consumers are being
advised on appropriate temperatures to which meat products should be cooked, and to use a meat thermometer to
ensure these temperatures are reached. However, consumers are more likely to assess cooking status by the color of
the meat or juice. This article reviews the factors that can influence the final color of cooked meat. In most instances,
these factors influence color by modifying the meat pigment myoglobin prior to and during cooking. Many factors
can prolong the pink “uncooked” color in meat, including high pH, modified atmosphere packaging, rapid thawing,
low fat content, nitrite, and irradiation. Such factors may lead to overcooking and loss of food quality, and consumer
rejection. Alternatively, factors that cause “premature browning” of meat, where the interior of the product looks
cooked but a microbiologically safe temperature has not been reached, are food safety issues. Pale, soft exudative
meats can prematurely brown, as can meats packaged under oxygenated conditions, frozen in bulk or thawed over
long periods, or those that have had salts or lean finely textured beef added. Meats cooked from a frozen state or
irradiated in aerobic conditions might also be at risk, but this might depend on meat species. In summary, the color
of cooked meat is not a good indicator of adequate cooking, and the use of a food thermometer is recommended.
Keywords: meat color, cooked, myoglobin, pathogen, thermometer

Introduction The United States Dept. of Health and Human Services (USDHHS)

I n the opinion of most consumers, the cooking of meat produces

a product of favorable texture and taste. From a food safety per-
spective, the cooking of meat is necessary to eliminate any associ-
2005 Food Code (USDHHS 2005) specifies temperature/time rules
for food establishments. For example, comminuted fish and meats
must be cooked so that all parts of the food are held at 68 ◦ C or above
ated foodborne pathogens. Microorganisms are introduced to meat for at least 15 s. Poultry, wild game animals, and stuffed meats shall be
surfaces during carcass processing and handling. Pathogenic mi- held for 15 s at 74 ◦ C. These specifications are sufficient to inactivate
croorganisms may be transferred to meat from the skin, feathers, most microorganisms and produce a safe cooked meat product,
feet and eviscerated organs, and from the processing environment provided pre- and postcook conditions (e.g., storage temperatures)
(e.g., surfaces, wash water, worker’s hands) or with added ingredi- are also controlled.
ents such as spices or extenders (Jackson and others 1997). The United States Dept. of Agriculture (USDA) recommends con-
Bacterial contamination of whole pieces of red meat such as sumers use a food thermometer to ensure the internal temperature
steaks or chops is restricted to the external surfaces, and so long (IT) of steaks, roasts, and fish reaches 62.8 ◦ C, pork and ground beef
as these are heat seared, the internal tissue can be eaten “rare” with attains 71.1 ◦ C, and chicken breasts and whole chicken reaches 76.7
◦
safety. Raw minced meat products, or whole cuts of meat that have C and 82 ◦ C, respectively (USDA 2005). However, consumer use of
been injected or rolled, may have surface organisms spread through- thermometers is limited (McCurdy and others 2005). For example,
out the product. Internal tissues of livers have also been shown to most consumers determine whether ground beef is cooked by ob-
be contaminated with pathogenic bacteria (Barot and others 1983; serving the color and texture of the cooked meat (Rhee and others
Moore and Madden 1998). These meats, and those suspected of car- 2003). The message to cook meat until the internal portion is no
rying parasites, must be cooked throughout to inactivate pathogens. longer pink and the juices run clear is often still promoted (FSA
The food safety messages promoted to the U.S. consumer have 2006, for example).
changed from judging the doneness of cooked meat on the basis of The appearance of cooked meat can be influenced by pH, meat
its appearance to using a thermometer (detailed in Lyon and others source, packaging conditions, freezing history, fat content, added in-
2000). This was in response to increasing evidence that the visual gredients, and preservation treatments such as irradiation and pres-
appearance of cooked meats does not necessarily indicate that a sure. These factors change the ratio of different forms of myoglobin;
microbiologically safe cooking temperature has been achieved. Of the main pigments responsible for the ultimate color of meat. Most
most concern is the condition of “premature browning,” where the research on cooked meat color has focused on comminuted meats,
interior of cooked meat is brown and “looks cooked” before a safe particularly ground beef products, because of their association with
cooking temperature has been reached. infections of Escherichia coli O157:H7.
The objective of this article is to assemble the findings of pub-
lished research where the cooked color of meat products was stud-
MS 20060056 Submitted 1/26/06, Accepted 2/21/06. Authors are with the Inst. ied in relation to the characteristics and handling of the meat. From
of Environmental Science & Research (ESR) Limited, 27 Creyke Road, Ilam, this information, factors that are an issue for food safety can be sep-
Christchurch, New Zealand, PO Box 29–181, Christchurch, New Zealand.
arated from those that cause problems with product quality. It is
Direct inquiries to author King (E-mail: [email protected]).
the former group that food safety regulatory authorities are most


C 2006 Institute of Food Technologists Vol. 71, Nr. 4, 2006—JOURNAL OF FOOD SCIENCE R31
doi: 10.1111/j.1750-3841.2006.00029.x
Further reproduction without permission is prohibited
 Does it look cooked? Cooked meat color . . .
R: Concise Reviews in Food Science

interested in when defining the messages to be included in food ment that produces the favored bright red color of raw meat, and
safety promotional material. is formed rapidly in the presence of oxygen at normal atmospheric
pressure (Varnam and Sutherland 1995).
Myoglobin and Cooking While hemoproteins, mostly myoglobin, constitute only about

M yoglobin, an oxygen-binding protein found in muscle, is 0.5% of the wet weight of red meats, the response of these pigments
the pigment most responsible for the color of meat, though to heat largely determines the color of cooked meat (Lytras and oth-
hemoglobin (the oxygen-binding protein in blood, which has con- ers 1999). Heating causes denaturation of the globin, which then
siderable homology) may also be present in small quantities. Myo- precipitates with other meat proteins. Denaturation of myoglobin
globin consists of a globin protein and a heme group containing a and other proteins begins between 55 ◦ C and 65 ◦ C in meat, and most
central iron atom. The iron atom is attached to the globin and 4 ni- denaturation has occurred by 75 ◦ C or 80 ◦ C (Varnam and Sutherland
trogen atoms, and has a 6th coordination point that can link with 1995; Hunt and others 1999). The rate of myoglobin denaturation
structurally compatible substances, usually water or oxygen. While slows with increasing meat temperature, and this is likely to be re-
the basic structure of myoglobin does not differ between animal lated to the concurrent rise in meat pH with cooking (Geileskey and
species, small differences in amino acid composition and stability others 1998).
have been noted between pig myoglobin and that of cattle and sheep The 3 forms of myoglobin differ in their sensitivity to heat. De-
(Varnam and Sutherland 1995). oxymyoglobin is the least sensitive to heat denaturation, followed
Myoglobin exists in three main forms, each producing a dis- by oxyMb, then metMb, though the latter 2 have fairly similar heat
tinctive color (Figure 1). In living tissue, the physiologically active sensitivities (Van Laack and others 1996a; Hunt and others 1999). As
oxymyoglobin (oxyMb) and deoxymyoglobin (deoxyMb) forms are the globin is denatured, metMb forms the brown globin hemichro-
maintained through the activity of metmyoglobin (metMb) reduc- mogen, also known as ferrihemochrome. The other myoglobins are
tase enzymes. These processes decline postmortem, and storage denatured to the red globin hemochromogen, also known as ferro-
conditions become more important in determining the proportion hemochrome (Warren and others 1996b). The latter is readily oxi-
of each myoglobin form present (Warriss 2000). Deoxymyoglobin is dized to the former, so ferrihemochrome is present in larger amounts
found where oxygen is absent, such as in vacuum-packaged meats in cooked meats (Varnam and Sutherland 1995).
or in the center of meat portions. The ferrous iron becomes oxidized Adequate cooking of meat produces a color change to off-white,
by free radicals when meat is stored for long periods of time, pro- grey, or brown hues, depending on the type of muscle. The ultimate
ducing the brown pigment metMb, which also forms where oxygen- color depends on the extent of ferrihemochrome formation, which
dependent meat enzymes and aerobic microorganisms successfully in turn is a product of the initial proportionality of the myoglobins,
compete with meat pigments for oxygen. Oxymyoglobin is the pig- and the final concentration of undenatured oxyMb or deoxyMb

a
oxidation

oxidation
deoxygenationb (free radicals)c

Oxymyoglobin Deoxymyoglobin Metmyoglobin

(oxyMb) (DeoxyMb) (MetMb)
Iron state: Fe(II) Fe(II) Fe(III)
6th coordination: oxygenationd reduction
O2 H2O (metmyoglobin H2O
Color: Bright red Purple-red reductase)
e Brown

Application of heat (meat cooking)

Rate of denaturation
(sensitivity to heat): Fast Slow Fastest

Denatured globin: Ferrohemochrome Ferrihemochrome

oxidation Brown
Color: Red
a
Promoted in acid conditions (post mortem) Primary references: Lawrie 1974; Varnam and Sutherland
b
Where oxygen is absent 1995; Warren and others 1996b; Baron and Andersen 2002.
c
Produced by enzymes and spoilage bacteria Also see text.
d
Meat exposure to atmospheric oxygen
e
Enzymes progressively inactivated post mortem
Figure 1 --- Characteristics of the myoglobin pigments in meat, their dynamic relationships, and the denatured
products formed during cooking

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Does it look cooked? Cooked meat color . . .

R: Concise Reviews in Food Science

(Varnam and Sutherland 1995; Van Laack and others 1996a). The beef of normal pH, the proportion of myoglobin denatured during
color of meat can be measured visually, chemically, or instrumen- cooking in high-pH beef is less, and a more intense red color is mea-
tally. Visual assessments usually involve a panel of two or more surable. Using absorbance as a measure of myoglobin denaturation,
trained people who assign values according to a preset descriptive the proportion of myoglobin denatured in ground beef at a normal
scale. Chemical assessments typically measure the concentration of pH of 5.50 was higher than the same meat with the pH adjusted to
myoglobin as extracted from a sample. Instrumental methods mea- 6.50 when both formulations were cooked to a variety of ITs (Trout
sure light reflectance off a sample. A typical instrumental technique 1989). A range of beef cuts were used to produce patties with variable
uses a chroma meter to define color in terms of the values L∗ (light- pH and when grilled to an IT of 71 ◦ C, red and pink color was still ev-
ness), a∗ (redness), and b∗ (yellowness), commonly referred to as the ident to panelists in patties with a pH greater than 5.7 (Mendenhall
Hunter values. Further optical values can be calculated from these 1989). Similarly, when commercially prepared ground beef patties
measurements, such as hue angle (tan−1 (b∗ /a∗ )) (Warriss 2000). of variable pH were cooked to an IT of 71 ◦ C, those with a pH less
than 5.9 were invariably associated with a brown cooked color, and
The Influence of pH red cooked color occurred mostly in patties with a pH of 5.95 or

T he amount of ferrihemochrome formation from myoglobin

during cooking is affected by initial meat pH. While mammalian
muscle has a pH of around 7, normal fresh meat has a pH ranging
above (Van Laack and others 1996b). In ground beef with the pH
artificially adjusted, patties with elevated pH required higher final
endpoint temperatures to denature similar amounts of myoglobin
from 5.4 to 5.6 (Varnam and Sutherland 1995). The carbohydrate to patties with lower pH (Brewer and Novakofski 1999).
glycogen is held in the muscles, but with postmortem reduction of The effect of pH on the color of cooked meat has also been ob-
oxygen supply the glycogen is broken down to lactic acid, lower- served in meats other than pork or ground beef. The inside rounds
ing the pH. This acidification process will continue until either the of beef from young bulls were processed into roasts and cooked to
glycogen is consumed or the low pH inactivates glycolytic enzymes. an IT of 63 ◦ C in a waterbath. Slices from the anterior end and middle
Where glycogen is limited, such as in animals that are very active, were analyzed instrumentally, and roasts with high pH (>5.6, mean
stressed or exposed to cold over a long period prior to slaughter, 6.5) were found to have higher L∗ , a∗ , and b∗ values than normal pH
the ultimate pH of the meat is higher. Meat with a pH above 6.2 (5.3 to 5.6, mean 5.5) roasts, that is, they were significantly redder
tends to have tightly packed water-retaining fibers that impede oxy- (Swan and Boles 2002). Raw chicken breast of higher pH is associated
gen transfer and promote longer survival of oxygen-scavenging en- with a darker appearance, and this relationship somewhat persists
zymes, favoring deoxyMb rather than oxyMb. The purple-red myo- with cooking. Fletcher and others (2000) found that steam cooking
globin combines with the closed structure of the muscle to absorb “lighter than normal,” “normal,” and “darker than normal” chicken
rather than reflect light, making the meat appear dark. This condi- breast (pH 5.76, 5.84, and 5.93, respectively) produced cooked prod-
tion is commonly known as dark, firm, dry (DFD) (Adams and Moss ucts with Hunter optical values that could be related back to the raw
2000; Warriss 2000). meat pH and color. It was found, however, that the color variabil-
A pale, soft, exudative (PSE) condition can be found in meats with ity with pH was not as pronounced in the cooked product as when
a low ultimate pH. PSE mainly affects pigs, though PSE-like charac- in raw form. Even when the chicken was marinated prior to cook-
teristics have been observed in poultry meats, and occasionally beef. ing, cooked darker meat (mean pH 6.10) was associated with more
PSE meat forms when animals undergo acute stress immediately redness (Qiao and others 2002).
prior to slaughter. Postmortem, glycogen levels are still reasonably The extent to which pH affects the cooked color of meat appears
high, and the acidification processes are accelerated so that the pH to vary between meats from different animal species. In a compari-
falls rapidly, while the muscle is still warm. The combination of high son of ground pork, turkey and beef (pH adjusted to 5.5, 6.0, 6.5, or
temperature and low pH causes protein denaturation, water loss, 7.0) cooked to various target ITs, all meats had a redder appearance
and an open muscle structure. The low pH also tends to promote and lower myoglobin denaturation with higher pH, but at higher
oxidation of oxyMb and deoxyMb to brown metMb, which combined temperatures (76 ◦ C and 83 ◦ C), these effects were more persistent
with high light scattering from the meat surface, gives the meat its in the turkey, irrespective of pH. For example, at a target IT of 83 ◦ C,
pale color (Adams and Moss 2000; Warriss 2000). myoglobin denaturation was at or close to 100% in beef and pork at
The PSE and DFD conditions have been shown to influence the all pH levels, but turkey samples were still spread between 75% and
cooked color of pork. Ground pork patties made from PSE meat did 95% depending on pH. However, for all species any pH-induced dif-
not appear pink after cooking to time/temperature regimes rang- ferences in color were reduced with increased cooking temperature
ing from an IT of 62.8 ◦ C for 3 min to IT 82.2 ◦ C for 1 s. Equiv- (Trout 1989).
alent “normal” patties were pink at 62.8 ◦ C and 65.6 ◦ C (1-min Evidently, a relationship exists between pH, myoglobin content,
holding), and very slightly pink at 71.1 ◦ C (1-s holding) (Lien and and myoglobin denaturation, and the final color of cooked meat.
others 2002b). A similar pattern was observed for PSE boneless pork The influence of pH may even dominate other factors that can affect
chops cooked to the same time/temperature combinations. DFD cooked meat color, such as fat content, freezing, and rate of thawing
pork chops have also been tested, and under all cooking conditions, (Berry 1998; Berry and others 2001). A satisfactory explanation for
these were more pink than normal or PSE meat (Lien and others this relationship is currently lacking, though it is likely that several
2002a). Myoglobin denaturation is faster in PSE pork when com- factors might be interacting. These factors might include the initial
pared to normal pork, particularly at temperatures below 71 ◦ C. It is form of the myoglobin (for example, deoxyMb is less heat-sensitive
possible that the open fibers and lower pH of PSE meat may predis- and more stable at higher pH than other myoglobin forms), the con-
pose myoglobin to greater heat denaturation, and faster browning dition and structure of the muscle fibers (for example, DFD vs. PSE),
(Lien and others 2002a, 2002b). The lack of redness and the greater and the denaturation processes of other meat proteins, including
proportion of heat-sensitive metMb in raw PSE meat might also en- enzymes, which could also be affected by pH and to which myo-
hance yellowness. globin denaturation is intricately linked.
Several studies have identified a correlation between raw beef pH There have been some studies that suggest the pH-effect on color
and the amount of undenatured myoglobin remaining in the cooked is not always predictable, and this provides some evidence for the
product, which itself correlates with red color. When compared to complexity of the pH/color relationship. In the studies of Van Laack

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 Does it look cooked? Cooked meat color . . .
R: Concise Reviews in Food Science

and others (1996b), beef patties with higher pH values were not mulation and pH) and handling, batches of meat can inexplicably
always associated with a red cooked color and the authors admit to vary in the final cooked color.
the interference of “other (unknown) factors.” Thirty percent of the In chickens, meat from defrosting immature birds can be dark-
color variation that was observed in these studies was attributed to ened as hemoglobin moves out of the porous, incompletely calci-
the initial myoglobin concentration in the raw products. Certainly, fied walls of the bones to accumulate in the tissues. Temperature
meat from different animals or from muscles of the same animal change (for example, freezing, reheating) can also darken poultry
can vary in their myoglobin content (Varnam and Sutherland 1995). meat by causing cell degradation and migration of hemoglobin pig-
Additional variation (33%) was attributed to the reducing capacity ment from the bone. For example, darkening of meat on thigh pieces
of the meat (Van Laack and others 1996b). This has also been shown can be related to pigment migration from the femur (Lyon and Lyon
to influence the myoglobin form and the extent of meat browning, 2002). So, while myoglobin and hemoglobin are both important, the
but will be detailed in later sections. latter is more influential on poultry meat color (Boulianne and King
In another study, pork loin chops of 2 pH groups (pH 5.4 to 5.5, 1998). When cooked, tissues with more heme pigment will appear
pH 5.6 to 5.7) cooked to 3 endpoint temperatures could not be sep- darker than, for example, breast meat (Lyon and Lyon 2002). Chicken
arated by their Hunter values immediately after cooking (Mancini leg quarters (bone-in) were cooked to an IT of 75 ◦ C or 85 ◦ C. At 75
◦
and others 2005). The small difference in pH between these groups C, the meat adjacent to the bone retained more redness than the
could be one explanation, as could the high (>71 ◦ C) tempera- surface. The redness of the meat adjacent to the bone was amplified
tures studied. Ground lamb with a pH lower than normal (pH 5.38, if the portions were chilled above 0 ◦ C prior to cooking compared to
normal pH 5.70) demonstrated much slower denaturation of myo- chilling at <0 ◦ C, though cooking to 85 ◦ C negated color differences
globin when cooked (Lytras and others 1999). The authors suggested attributed to chill temperatures (Lyon and Lyon 2002).
that the low pH of the raw meat had denatured the proteins that Differences in cooked color have also been observed in beef
ordinarily would be available to interact with myoglobin during sourced from assorted muscles. The myoglobin in ground beef
cooking, so the myoglobin became more stable in the absence of patties prepared from sirloin (longissimus dorsi) denatured at a
these reactants. However, low pH favors the formation of brown faster rate during cooking than in patties made from shoulder steak
metMb, and also destabilizes deoxyMb (Varnam and Sutherland (chuck) or shin. The pH and concentration of myoglobin was sim-
1995). ilar in all raw cuts (Geileskey and others 1998). A similar effect has
While there can be some variation, there is enough evidence to been observed in ground lamb, where myoglobin denaturation dur-
suggest that a strong relationship exists between the pH of raw meat ing cooking was faster in sirloin than shoulder or leg steaks, though
and cooked meat color. Generally, meat with a pH above normal only at temperatures <70 ◦ C (Lytras and others 1999). Since the rate
slows the denaturation of myoglobin, and the meat can still remain of myoglobin denaturation was measured in these studies, the differ-
pink when cooked to the recommended IT. High pH meat is not ences cannot be explained by variability in gross myoglobin content.
uncommon in the domestic market, particularly if animals have The authors suggested that final meat color might be influenced by
been chronically stressed prior to slaughter (Trout 1989). Of 295 U.S. different concentrations and thermal stabilities of reactant proteins
samples of raw beef, 106 (36%) were above the normal pH range of in the muscle groups. The extent of denaturation of these proteins
5.3 to 5.7 (Mendenhall 1989). The pinkness associated with prop- during cooking would in turn influence the extent of interaction
erly cooked high pH meat is perhaps more an issue for food quality with, and denaturation of, the myoglobin, which itself compara-
than food safety. Consumers may perceive that high pH meat is less tively shows very little difference in stability and reactivity between
cooked, and will proceed to continue cooking to higher tempera- muscles (Geileskey and others 1998; Lytras and others 1999). This
tures or for a longer time, with subsequent losses in quality (e.g., theory has also been proposed to account for differences in the rate
texture, juiciness, yield). One potential food safety issue with high of myoglobin denaturation between animal species. For example,
pH meat is that consumers who use thermometers to judge done- minced lamb sirloin demonstrated a faster rate of myoglobin de-
ness may begin to doubt their accuracy when a meat product still naturation during cooking than beef sirloin (Geileskey and others
appears to be undercooked, and thermometer use might cease. Of 1998). However, the pH and hemoprotein content of the lamb was
more importance are meat products that visually appear cooked lower than that of the beef, which possibly influenced this result.
before a safe IT has been reached. This “premature browning” has Earlier work had suggested that meat sourced from older animals
been shown to occur in PSE pork products, and could be an issue would brown quicker than cuts from young animals during cook-
for other low pH meats. ing (Marksberry 1990). In another study (Hague and others 1994),
ground beef from A-maturity (young at slaughter) and E-maturity
The Influence of Meat Source (old at slaughter) carcasses were compared for color when cooked

T he species of animal, the age of the animal at slaughter, and the

anatomical location of the muscle from which meat is sourced
can all affect final cooked meat color. To an extent, this is explained
to a variety of ITs. No differences in meat color or color of expressed
juice were observed with carcass maturity at any temperature. Of
concern in this study was that patties cooked to 66 ◦ C and 71 ◦ C
by differences in myoglobin content. Beef, for example, contains were only distinguishable by instrumental measurements, and were
between 4 and 10 mg myoglobin/g wet tissue, but this value might not visually different. Patties cooked to different temperatures were
reach 20 in older animals. Pork contains no more than 3 mg myo- only visually different when observing the color of the expressed
globin/g wet tissue. Male animals typically have higher myoglobin juice (Hague and others 1994). The browning of these patties at
concentrations than females, and muscles with higher work loads, lower temperatures may have masked any effect on cooked color
such as the leg muscles, are darkened by greater myoglobin con- that might arise from carcass maturity.
tent (Varnam and Sutherland 1995). The condition of the animal at From a food safety perspective, meats that remain pink once a
slaughter and postslaughter processing influences meat quality and safe cooking temperature has been reached are not of concern. This
subsequent color changes, and in many aspects, this is related to the is the case for meats darkened by the proximity of bone and chill-
effects of pH, as described above. However, one study (Liu and Berry ing conditions. Premature browning could possibly occur in meats
1996) has found that even with strict control over manufacture (for- sourced from older carcasses, though current results are conflicting.

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Does it look cooked? Cooked meat color . . .

R: Concise Reviews in Food Science

The Influence of Packaging under 80% O 2 was between “slightly pink” and “tan, no pink,” and

T he extent of myoglobin oxygenation or oxidation of the iron

moiety (redox potential) plays an influential role in rate of
browning and the final cooked color of meat (Figure 1). In most
they were visually done at 71 ◦ C. Steaks stored in the presence of
0.4% CO retained a comparatively redder appearance after cooking,
and were very similar to cooked steaks that had been stored under
raw meat products the myoglobin form will be largely influenced vacuum. Meat from these treatments was easily identified as being
by the atmospheric conditions created by packaging and display undercooked at 66 ◦ C, and internal redness was prolonged such that
conditions. it was still visually detected at an IT of 79 ◦ C. The same trend has
Well-oxygenated ground meat contains a higher concentration of been found in similar studies with ground beef (Van Laack and oth-
oxyMb, though the extent of oxyMb formation can vary with animal ers 1996a; John and others 2004), though in the study of Van Laack
species (Varnam and Sutherland 1995). Deoxymyoglobin is more and others (1996a) the beef stored under oxygen-permeable film
prevalent where oxygen interaction with the meat has been inhib- contained a significant concentration of metMb rather than oxyMb,
ited, such as in vacuum packaged meat. OxyMb is more sensitive probably as a result of precook freeze-thaw handling. Storage of
to heat denaturation than deoxyMb, and well-oxygenated meats, injected beef steaks under an alternative oxygen-free atmosphere,
such as fresh meats without packaging or in aerobic packaging, will 80% nitrogen and 20% CO 2 , still resulted in cooked steaks that had
brown faster when cooked. In a series of cooking experiments, oxy- less myoglobin denaturation and more red color when compared to
genated pork was found to appear visually less pink than deoxy- those stored under 80% O 2 (Seyfert and others 2004a).
genated pork when cooked to temperatures ranging between 65.6 ◦ C To summarize, the oxidation and oxygenation state of myoglobin
and 76.7 ◦ C (Lien and others 2002b). Beef patties where myoglobin is dynamic in meats and will be influenced by storage conditions
was predominantly oxyMb were very red in the raw state compared and packaging. The pigment state at time of cooking could in-
to purple-red deoxyMb-dominant beef, but once cooked to 55 ◦ C, fluence the cooked color appearance (Warren and others 1996a).
the well-oxygenated meat was brown while the deoxygenated meat Meats that contain higher concentrations of oxyMb or metMb will
still appeared red and undercooked (Hunt and others 1999). brown quicker with cooking than those with higher proportions of
Even small changes in the length of time a product is packaged can deoxyMb (Lien and others 2002b). Meat stored under normal at-
alter myoglobin oxygenation. Killinger and others (2000) compared mospheric conditions that is either very fresh (high oxyMb) or has
the cooked color of patties made from ground beef freshly pack- had prolonged storage (high metMb), or storage of meat under a
aged under oxygen-permeable film to the same packaged product modified atmosphere of 80% O 2 (high oxyMb), could appear visu-
stored overnight in a refrigerator. Patties made from stored meat ally well cooked when a safe internal cooking temperature has not
contained more deoxyMb and were redder when cooked compared been achieved.
to freshly packaged ground beef. Similarly, patties made from the
outer portion of a meat pack were browner than those from the The Influence of Freezing History
inner portion when cooked, and contained less deoxyMb.
Similarly, the oxidative state of the iron moiety will affect cooked
meat color. Long-term storage of meat increases the proportion of
I n a study by Van Laack and others (1996a), the internal color of
beef patties cooked from fresh was redder than the same formu-
lation of patties cooked from a frozen state. In turn, the internal
metMb, which results in the brown color not favored by consumers. color of patties cooked from frozen was redder than that of patties
MetMb is also the most sensitive to heat denaturation, the browning thawed prior to cooking, and premature browning was evident in
of meat during cooking is rapid. Ground beef artificially oxidized or the thawed samples (Van Laack and others 1996a). This indicated
reduced to increase the proportion of metMb or deoxyMb, respec- that a relationship existed between the freezing history of the patties
tively, then cooked to an IT of 55 ◦ C were easily distinguishable by prior to cooking and the final cooked color. The effect does not ap-
color. When compared to cooked patties with an unaltered redox po- pear to be predictable and may depend on the species from which
tential (visually pink), reduced meat appeared the most red inside, meat is sourced. Pork patties cooked after thawing retained a redder
and oxidized meat the least (Warren and others 1996a). In a similar appearance than those cooked from frozen, with the latter appear-
study the oxidized meat was notably brown, even when raw (Hunt ing fully cooked at the lowest target IT (62.8 ◦ C) (Lien and others
and others 1999). The variation in reducing capacity measured from 2002b).
samples of commercially prepared beef patties was found to corre- The lengths of time under frozen storage or thawing both affect
late with myoglobin denaturation during cooking, such that patties the cooked color of beef patties. When 17 beef patty products were
with lower reducing capacity browned internally at lower tempera- cooked from a frozen state after a brief period in storage, the internal
tures (Van Laack and others 1996b). color of 47% of the products was visually classified as red or pink at
Modified atmosphere packaging is used to prolong meat shelf- an IT of 71 ◦ C. After frozen storage for a year, 94% of the products
life. The most common condition used for fresh beef is an atmo- were red or pink when cooked from frozen to IT 71 ◦ C (Van Laack
sphere of 80% oxygen and 20% carbon dioxide. Under these condi- and others 1996b). When investigating the effect of thawing time,
tions the oxygen promotes production of oxyMb and the red color is frozen ground beef patties were cooked (IT 71 ◦ C) from frozen, after
stabilized. The use of 0.4% carbon monoxide (CO) with 30% car- 30 min thaw at 25 ◦ C, or after 6, 12, 18, or 24 h thaw at 7 ◦ C. Products
bon dioxide and the balance as nitrogen has been approved for cooked after thawing had a more well-done appearance than those
meat packaging in the United States. The CO binds with myoglobin cooked from frozen, and had lower a∗ values and higher hue angles
and forms the pigment carboxymyoglobin, which gives meat a sta- (so less pink-red), and increased Mb denaturation, despite having
ble cherry red color. Vacuum packaging promotes formation of de- shorter cooking times than those cooked from frozen. The effect was
oxyMb, and meat appears a purple color, which is not so highly enhanced with longer thawing. It was also observed in this study
favored by consumers (John and others 2005). that one product with a pH of >6.0, which would usually appear
John and others (2005) observed differences in beef steak color undercooked at safe cooking temperatures, still appeared well done
when grilled to a variety of ITs after storage under modified atmo- when cooked after thawing. The link between pH and color may be
spheres or vacuum (John and others 2005). Meat stored under 80% lost after a freeze thaw cycle (Van Laack and others 1996a), though
O 2 was less red and had significantly more myoglobin denaturation this is contradicted by other authors (Berry 1998; Berry and others
after cooking. At an IT of 66 ◦ C, the visual panel score for steaks stored 2001).

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 Does it look cooked? Cooked meat color . . .
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Several publications (USDA 1998; Lyon and others 2000, 2001; were less cohesive than other preparations, so heat transfer was
Berry and others 2001) have addressed the relationship between better during cooking and browning was more rapid. Lien and oth-
freezing history and cooked meat color through more detailed inves- ers (2002b) proposed that pork patties cooked from frozen might
tigations. All of these studies investigated the impact on the cooked brown earlier through a combination of greater thermal conductiv-
color of ground beef with different freezing history (stored frozen as ity (2 to 3 times greater in frozen than thawed meat) and absorption
patties or as bulk mince) and thawing conditions (2 h at room tem- of more energy (the energy released as ice crystals convert to water
perature, 4h under refrigeration or microwaved). Cooking involved is absorbed). So at a common endpoint temperature, frozen pat-
grilling to ITs of 52.7 ◦ C, 65.6 ◦ C, 71.1 ◦ C, and 79.4 ◦ C. The freez- ties would have absorbed more energy than thawed patties, and
ing history and thawing conditions interacted to modify the cooked this should increase browning. This does not explain the opposite
color of the patties when compared to freshly prepared and cooked observation for beef patties, where those cooked from frozen re-
beef patties, and a large number of outcomes were observed. Typi- main redder than those cooked after thawing (Van Laack and others
cally, ground beef stored as bulk and formed into patties just prior 1996a).
to cooking showed a higher incidence of premature browning. For It is clear that freezing history will affect the color of cooked
example, as many as two thirds of the patties formed from ground ground meat so that cooking to an IT of 71 ◦ C will not predictably pro-
beef frozen in bulk and thawed overnight in a refrigerator had turned duce a patty that “looks cooked,” though further studies are needed
brown at IT 65.6 ◦ C, despite incomplete thawing and shorter cook- to investigate the mechanisms behind these observations. Cooking
ing times (USDA 1998; Berry and others 2001). It was also more from frozen or after rapid thawing generally prolongs pink color,
common for the juices of patties formed from bulk frozen ground though this might differ with meat type. Alternatively, patties that
beef to have no pink or red color at temperatures less than 71 ◦ C have been formed from bulk frozen beef or that have been slowly
(Lyon and others 2000). While patties prepared from bulk-frozen thawed could appear brown at unsafe cooking temperatures.
beef were the least red upon thawing and cooking, at equivalent ITs
fresh beef patties were significantly redder, and beef stored frozen
as patties and thawed before cooking were the reddest. The cooked
colors of the patties stored frozen did not significantly change with The Influence of Fat Content
thawing method (room temperature, under refrigeration or in the
microwave) in any of the studies. All of these methods were rapid
thawing techniques, and it is more likely that the time of thawing has
T here is an increasing trend for consumers to favor meat products
lower in fat, such as beef patties prepared with lean meat. Some
publications have indicated that fat content does not influence the
more effect than the method, which might account for the greater cooked color of meat in any readily discernable way (Troutt and
browning observed in the bulk frozen beef (Van Laack and others others 1992b; Berry 1994; Berry and others 2001). For example, beef
1996a; Lyon and others 2001). patties with fat content between 5% and 30% were cooked to an IT
There is uncertainty over the changes in myoglobin chemistry of 71 ◦ C or 77 ◦ C. When raw, the lower fat patties were distinctively
brought about by freezing history that influences color. Van Laack darker red, but when cooked the concentration of fat did not affect
and others (1996b) could not attribute changes in myoglobin denat- surface color, uniformity of surface color, or internal color (Troutt
uration or a∗ value brought about by frozen storage to any differences and others 1992b).
in reducing capacity, concentration of metMb or cooking method, Other studies suggest that the fat content of meat may have some
though the differences in product formulation and cooking from effect on the final cooked color, with higher fat patties appearing less
frozen are likely to have had some influence in their study. Ben Ab- pink (Berry 1998; Berry and others 2001). In beef, the oxidation state
dallah and others (1999) compared the concentration of each form of lipids and pigments are closely linked, so that an increase in one
of myoglobin between raw beef cuts that had undergone a freeze– similarly increases the other (Varnam and Sutherland 1995). There is
slow thaw cycle and fresh beef cuts. When both were stored at 2 ◦ C enough evidence to confirm that, at least in raw meat, myoglobin has
in the dark in gas-impermeable film, the previously frozen meat an important role in the oxidation of polyunsaturated lipids (Baron
contained significantly more metMb and less oxyMb than the fresh and Anderson 2002). While the oxidation processes involved in meat
meat for most of the experiment. The high concentration of metMb cooking will alone increase metMb and ferrihemochrome, the effect
would have increased the rate of formation of brown color if this could be augmented where the fat content is higher. The relationship
meat were cooked. between lipid and metMb oxidation is not fully understood, though
Several hypotheses have been summarized by Ben Abdallah and it might involve the formation of free radicals or oxygen depletion
others (1999) to explain the increase in metMb brought about by during lipid oxidation (Monahan and others 2005).
freezing. Proposed processes include autooxidation (the nonenzy- While fat content might influence the cooked color of meat, it
matic spontaneous oxidation of myoglobin by free oxygen), cell is probably not as influential as other factors that alter cooked
membrane disruption brought about by freezing, which allows cat- color, particularly high pH and freezing history (Berry 1998; Berry
alysts of oxidative reactions to come into contact with myoglobin and Bigner-George 2000). None of the publications cited above ex-
(perhaps in a more concentrated form in unfrozen liquid pockets), pressed any concern over premature browning due to fat concentra-
and disruption of the metaglobin-reducing enzyme system through tion alone. The only food safety concern relating to fat and meat color
disruption of enzyme structure or function during freezing. Lyon lies where commercial establishments, such as burger restaurants,
and others (2001) have also suggested that slow freeze–thaw rates cook meat products according to set time/temperature regimes that
may damage the myoglobin protein, promoting faster denaturation have been based on producing a safe and visually cooked product.
or oxidation during cooking and increasing the possibility of pre- Fat is an efficient conductor of heat, and higher fat meats will reach
mature browning. However, none of these hypotheses account for target ITs quicker than those with less fat (Troutt and others 1992b;
patties that are cooked from frozen or after a short thaw (for ex- Liu and Berry 1996). If these regimes are applied to lower fat for-
ample, microwaving), where the formation of brown color during mulations without modification, it is possible that meat products
cooking is limited (Lyon and others 2000). will fail to reach safe ITs. However, visual assessment of the low fat
Physical factors are probably also important. Berry and others product after the established cooking structure will quickly indicate
(2001) suggested that patties prepared from bulk frozen beef mince that a food safety problem may exist.

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Does it look cooked? Cooked meat color . . .

R: Concise Reviews in Food Science

The Influence of Added Ingredients injection of water and phosphate will not affect cooked color devel-

A number of ingredients may be added to meat prior to cooking.

This is more common for comminuted meats, where ingredi-
ents might include extenders such as soy protein, nonfat dried milk
opment (Lien and others 2002a). Addition of 2% olive oil to ground
lamb did not denature myoglobin during cooking at a rate any dif-
ferent to an oil-free control, and myoglobin denaturation during
or cereals (for example, bread crumbs, rusk), as well as salt and the cooking of ground beef with added polyphosphates (0.3%), soya
spices (ICMSF 1998). The composition of ground beef might also be proteins (1% or 3%), caseinate (2%) or whey (3%) was not signifi-
altered by the addition of lean finely textured beef (Van Laack and cantly different from unmodified controls (Lytras and others 1999).
others 1997). Some of these ingredients have been shown to affect Finally, the addition of dietary fibers (sugarbeet, oat or pea), potato
the cooked color of meat. starch and polydextrose did not affect the internal color of beef
The addition of sodium chloride (NaCl) or sodium tripolyphos- patties cooked to at IT of 71 ◦ C or 77 ◦ C (Troutt and others 1992a).
phate (Na 5 O 10 P 3 ) can increase myoglobin denaturation. Trout
(1989) demonstrated that when ground beef patties with concen- The Influence of Preservation Treatments
trations of NaCl between 0% and 3% were cooked to a range of ITs,
the higher NaCl concentrations increased the percentage of myo-
globin denatured. The browner color was particularly obvious at
P ressure treatment is sometimes used to improve microbiologi-
cal quality and color of meat, and may impact on cooked color.
Jung and others (2003) pressure treated vacuum packed beef steak
lower temperatures (52 ◦ C to 66 ◦ C). In the same study, the myo- prior to cooking (IT 65 ◦ C), and analyzed for changes in color. While
globin denaturation in ground beef with 0.5% Na 5 O 10 P 3 was 5% to pressure treatment increased the redness of raw beef, once cooked
10% greater than without the additive. This result was not affected the color differences between pressurized and nontreated controls
by modification of the pH (Trout 1989). In a similar study, the rate of disappeared.
myoglobin denaturation in ground beef with 1.5% to 3% NaCl was al- Ionising radiation is being increasingly used to extend the shelf-
most twice that of salt-free meat, and in ground lamb with 2% NaCl, life of fresh meat by inactivating bacteria and parasites. The most
the myoglobin denaturation rate was 2 to 3 times faster than the common form of irradiation is gamma radiation, where isotopes
salt-free control at lower temperatures (55 ◦ C and 60 ◦ C), and still (principally 60 Co and 137 Cs) are used to emit electromagnetic radia-
consistently faster at higher temperatures (65 ◦ C to 75 ◦ C) (Lytras tions (Jay 1996). Low level irradiation does not induce detectable
and others 1999). The presence of salt will cause faster browning of organoleptic changes in most meat products (Adams and Moss
meat, and may cause meat to be visually assessed as cooked before 2000), though some rancidity might be noticeable (Chirinos and
microbiologically safe cooking has occurred. others 2002), but it can cause color changes that appear to vary by
Nitrite is usually used in the curing process of meats and gen- irradiation dose, species and packaging conditions (Grant and Pat-
erates the characteristic and heat-stable red color by binding with terson 1991; Nanke and others 1998).
myoglobin. Seyfert and others (2004b) suggested that some cross- The color change in raw beef with irradiation has been investi-
contamination might occur in facilities producing both fresh and gated, and most report a dose-dependant browning effect (less red,
cured meats, whereby fresh meats could unintentionally be exposed more yellow). The loss of red color is more evident when the beef is ir-
to nitrite or nitric oxide. They demonstrated that contamination of radiated in the presence of oxygen (e.g., in oxygen-permeable pack-
precooked ground pork with nitrite would cause a heat-stable pink aging), but minimal when the beef is vacuum-packaged or in carbon
color to develop upon further cooking. While this might be an issue monoxide MAP (Fu and others 1995; Nanke and others 1998; Giroux
for meat quality, from a food safety perspective the meat will appear and others 2001; Kusmider and others 2002), though an increase
undercooked to a consumer and will be rejected. in redness with irradiation has also been reported in raw vacuum
Lean finely textured beef (LFTB) is often incorporated into ground packaged beef (Peirson and others 2005). The effects of irradiation
beef to produce a lower fat product. The pH of meat products in- are transmitted to cooked color. In a recent study (Peirson and oth-
creases with the addition of LFTB, however the myoglobin in LFTB ers 2005), the cooked color (IT 60 ◦ C or 71 ◦ C) of ground beef stored
denatures quickly with heat and meat products containing LFTB briefly under aerobic or vacuum packaging, either fresh or frozen,
will brown quicker upon cooking. The processes involved in the pro- and irradiated prior to patty formation and cooking, was compared
duction of LFTB render the myoglobin in LFTB more heat sensitive to equivalent nonirradiated samples. Though statistically significant
and might also modify the state of other proteins that interact with differences were lacking, some trends were evident, particularly at
myoglobin, increasing the rate of myoglobin denaturation during IT 60 ◦ C. Compared to their equivalent controls, the cooked color
cooking. LFTB also contains a higher proportion of metMb; metMb of patties irradiated in aerobic conditions was less red, and an in-
being the most heat sensitive myoglobin form (Van Laack and oth- crease in redness was reported for patties irradiated under vacuum.
ers 1997). Van Laack and others (1997) compared the cooked color However, irrespective of packaging, cooked patties that were frozen
of normal and high pH beef patties when LFTB was added incre- prior to irradiation were less pink than fresh samples. Bulk freezing
mentally. Without LFTB, the high pH meat was predictably redder and the long overnight thaw are likely to have contributed to this
and visually less well done than beef with normal pH. Addition of effect (see earlier section on freezing history). Importantly, when
LFTB to the high pH formulation increased myoglobin denaturation cooked to only 60 ◦ C, the color of this prefrozen irradiated beef was
and decreased redness when cooked. Interestingly the pH was not indistinguishable from nonirradiated beef (fresh or prefrozen) that
significantly altered, even with 75% LFTB. In contrast, addition of had been cooked to 71 ◦ C.
LFTB to the normal pH formulation increased the pH significantly, Alternative results have been reported for poultry meats and pork.
and visually the cooked color did not change significantly. It is pos- Raw, irradiated chicken, turkey, and pork are all redder than equiv-
sible that with addition of LFTB to the normal pH meat the dual alent nonirradiated meats (Grant and Patterson 1991; Nanke and
effects of increased pH (expect increased redness in cooked meat) others 1998; Nam and Ahn 2002). The red color is intensified with
and increased myoglobin denaturation (expect decreased redness in increased radiation dose and varies with packaging conditions (e.g.,
cooked meat), balanced one another. Certainly more work is needed more development of red color with vacuum packaging), but persists
to understand this observation. with cooking. Breast meat from chickens were packaged under vac-
Other additives do not appear to be important for influencing uum or aerobic conditions, irradiated, and the color compared to
cooked meat color. Provided the pH of pork chops is controlled, equivalent nonirradiated samples after cooking to an IT of 74 ◦ C. The

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 Does it look cooked? Cooked meat color . . .
R: Concise Reviews in Food Science

irradiated fillets were redder than controls, though aerobic storage radiation of precooked products (Holownia and others 2003). There
reduced irradiation-induced redness (Du and others 2002). In test- is a large body of literature on this topic, but the condition is an issue
ing the effect of irradiation on the cooked color of meats from differ- for food quality, not food safety. Pinkiness in cooked meat will cause
ent poultry species, Millar and others (2002) found that all irradiated consumers to reject the meat as undercooked, or subject the meat
cuts were redder than controls, though there were differences be- to further cooking. Pink defect will not be reviewed further in this
tween species and muscle type (leg, breast). An increase in red color paper.
has also been reported for irradiated precooked pork sausages, par-
ticularly if stored under vacuum (Jo and others 2000). Conclusions
Several hypotheses have been suggested to explain irradiation-
induced color change. Nanke and others (1998) suggest that the in-
crease in yellowness of raw beef irradiated aerobically could be due
T he color of a meat product once cooked is not a good indication
that the food has reached a microbiologically safe IT. Ground,
rolled, injected or variety meats require thorough cooking to inac-
to formation of metMb, which would increase the rate of brown- tivate any pathogenic microorganisms that might be present inter-
ing upon cooking. Under aerobic conditions the radiation stimu- nally. The greatest issue for food safety is when the interior of cooked
lates lipid oxidation (Kusmider and others 2002) and reacts with meat is visually brown and “well done,” yet the IT is not high enough
water to form free radicals such as hydroxyl (OH) (Chirinos and to ensure the inactivation of microbiological pathogens. This condi-
others 2002). Free radicals promote myoglobin oxidation (Giroux tion, termed premature browning, may occur with PSE meats, and
and others 2001), enhancing development of metMb. The addition can be induced by storage in high-oxygen modified atmospheric
of free radical scavengers to beef and pork prior to irradiation has packaging, bulk storage in the frozen state, prolonged thawing, the
been shown to stabilize color (Zhao and Sebranek 1996; Giroux and addition of salts or LFTB, and where beef is irradiated in aerobic con-
others 2001). It has been suggested that the increased redness ob- ditions (Table 1). At the other extreme, there are numerous factors
served in irradiated pork and poultry meats and irradiated vacuum- that prolong pink color in meats, so that they do not appear to be
packaged beef is due to the formation of a carboxy heme pigment, adequately cooked. This condition is more an issue for food quality,
when carbon monoxide produced during irradiation of meat links to where products will be overcooked, and also may bring about eco-
the 6th coordination point in the myoglobin and/or hemoglobin to nomic losses in food service industries through consumer rejection
produce red carboxymyoglobin and/or carboxyhemoglobin (Millar and loss of yield (Table 1).
and others 2002). Nam and Ahn (2002) also propose that irradiation Clearly, all of the factors reviewed in this paper—pH, meat source,
generates reduced conditions that encourage reduction of the myo- packaging, freezing history, fat content, added ingredients, preser-
globin iron, and indeed an oxyMb-like pigment has been detected vation treatments, and cooking method—will combine to holisti-
in vacuum packaged irradiated pork and beef (Nanke and others cally influence the color of cooked meat. Taken independently, the
1998). mechanisms by which the properties of the meat are altered by each
There is insufficient evidence to suggest that preservation treat- of these factors appear to be highly complex and often based on
ments involving pressure generates an issue for food safety, at least hypotheses. Overall, there is little known about the biochemical in-
in beef, as pressure-induced color change appears to be eliminated teractions between myoglobin and other proteins or lipids in meat
with cooking. The persistent pink color of cooked, irradiated pork during the cooking process; understanding these will provide some
and poultry, and in many cases beef irradiated under vacuum, will explanation for the observations summarized in this review. This
more likely be interpreted as undercooking, and the product will be review has identified several information gaps that might be inves-
rejected, or overcooked with subsequent losses in quality. However, tigated further. Good biochemical experimentation might better ex-
premature browning does appear to be an issue for beef irradiated pose the changes in meat induced by pH (e.g., proteins, structure,
in aerobic conditions or after freeze–thaw. myoglobin state) and explain how pH appears to influence the rate of
myoglobin denaturation during cooking. Other questions that arise
from this review are why rapid thawing of frozen meat reduces myo-
Cooking Method
globin denaturation during cooking yet slow thawing increases this,
C ooking method influences the rate of heat transmission
through a meat product and the extent of cooking. There are
publications that report the temperature patterns within meat prod-
how myoglobin denaturation is increased in the presence of salt,
why the changes induced by addition of LFTB are so dependant on
meat pH, and what biochemical processes are responsible for the
ucts cooked using various methods (Chen and Marks 1997; Singh
color changes induced by irradiation. Some of these information
and others 1997; Rhee and others 2003), but only one study was
gaps might be addressed by future research on meat color. The most
identified that compared cooking method with cooked color. Bow-
recent studies reviewed in this article indicate that the direction of
ers and others (1987) observed that the internal color of beef steaks
future research is likely to focus on addressing the need for the meat
cooked to the same IT were visually browner when oven broiled
industry to control meat appearance and spoilage. Specifically, fur-
compared to roasting. This indicates that cooked color could also
ther studies to better understand the oxidation processes in meat
be influenced by the method of cooking, though more studies would
(before and during cooking) and the effect of emerging packaging
be needed to report the extent of this effect.
and preservation technologies are likely.
In summary, the character of raw meat products available to the
Pink Defect consumer at the point of purchase will vary with meat source and

P ink defect is a condition where well-cooked white meat (pork,

poultry) still retains a pink color or develops pinkiness with
storage after cooking. The proposed causes include the types of pig-
processing, and will continue to change with postpurchase han-
dling. The history of the meat will directly affect the color when
cooked. On this basis, there can be no confidence in visually in-
ments in the meat, preslaughter factors such as genetics, feed, haul- specting a meat product to ascertain if it is safely cooked, and use
ing and handling, heat and cold stress and gaseous environment, of a food thermometer is the most reliable method for guaranteeing
stunning techniques, incidental nitrate/nitrite contamination, wa- the inactivation of foodborne pathogens in cooked meat.
ter supply, freezing and processing equipment, and processing in- This conclusion has significant implications for food regulatory
gredients, the use of nonmeat ingredients, cooking methods, and ir- agencies whose mandate is to release regulations and advice for

R38 JOURNAL OF FOOD SCIENCE—Vol. 71, Nr. 4, 2006 URLs and E-mail addresses are active links at www.ift.org
Does it look cooked? Cooked meat color . . .

R: Concise Reviews in Food Science

Table 1 --- Factors that influence the cooked color of meat
Potential for (on meat cooking)
Factor Premature browninga Prolonged pink-redb
pH High 
DFDc 
PSEc 
Meat source Close to bone 
Older carcasses ?d
Packaging Aerobic/oxygenated 
Carbon monoxide 
Vacuum 
Freezing history Cooked from frozen  (pork)  (beef)
Short thaw 
Long thaw 
Frozen in bulk 
Fat Low 
Added ingredients Salts 
Nitrite 
LFTBc 
Preservation Irradiation  (beef/aerobic)  (pork, poultry, vacuum)
a
An issue for food safety.
b
An issue for food quality and/or economic loss.
c
DFD = dry, firm, dark; PSE = pale, soft, exudative;
LFTB = lean finely textured beef.
d
? indicates conflicting results make the outcome uncertain.

the food industry and the domestic consumer. Fortunately for ma- Chen H, Marks B. 1997. Evaluation previous thermal treatment of chicken patties by
visible/near-infrared spectroscopy. J Food Sci 62:753–56, 780.
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This review was partially funded by the New Zealand Food Safety Holownia K, Chinnan MS, Reynolds AE. 2003. Pink color defect in poultry white meat
as affected by endogenous conditions. J Food Sci 68:742–7.
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