JFS: Food Chemistry and Toxicology

Effects of Endpoint Temperature on the Internal

Color of Pork Patties of Different Myoglobin
Form, Initial Cooking State, and Quality
R. LIEN, M.C. HUNT, S. ANDERSON, D.H. KROPF, T.M. LOUGHIN, M.E. DIKEMAN, AND J. VELAZCO

Food Chemistry and Toxicology

ABSTRACT: The effects of several parameters on the development of internal cooked color in ground pork were
evaluated. Patties were made from normal or pale, soft, and exudative (PSE) pork and the pigment converted to
either oxymyoglobin or deoxymyoglobin. Patties from these 4 treatment combinations were cooked from the
frozen or thawed states to 5 endpoint temperatures. PSE patties and those containing oxymyoglobin exhibited
premature browning as they appeared cooked and were more (P < 0.05) tan at lower temperatures than normal
patties or those with deoxymyoglobin which had a slightly pink internal color at 71 °C. Percentage myoglobin
denaturation increased as cooking temperatures increased (P < 0.05) for both types of meat and was greater in
patties containing deoxymyoglobin than in those with oxymyoglobin. Patties cooked frozen had lower a* values
(P < 0.05) than thawed patties at every endpoint temperature.
Keywords: pork, cooking, color, myoglobin denaturation

Introduction tamination from either gas-fired ovens each batch was divided equally by weight

N UMEROUS CASES OF FOOD - BORNE ILL -

ness caused by pathogens have
been attributed to inadequate cooking of
meat products. It is difficult, however, to
reliably verify doneness. Although USDA
(1997) has issued instructions for verify-
ing internal temperature and cooking
time for meat patties, in the absence of a
thermometer, consumers tend to evalu-
ate the degree of doneness visually, us-
ing color of ground meat as an indicator of
thorough cooking. However, visual ap-
praisal of cooked color is not a reliable in-
dicator. Marksberry (1990) observed that
beef patties developed a cooked, well-
done appearance at temperatures much
lower than expected. This condition has
been termed premature browning
(Hague and others 1994). The occurrence
of premature browning was caused by
the presence of oxymyoglobin and met-
myoglobin but not deoxymyoglobin in
meat at the time of cooking, and to pH of
the meat (Hunt and others 1999).
Premature browning is not the only
condition that affects the abnormal ap-
pearance of cooked meat. Marksberry
(1990), Van Laack and others (1996b),
Berry (1998), Schoenbeck (1998), and
Berry and Bigner-George (1999) ob-
served beef patties that remained pink
when cooked to 74 °C or higher. This
hard-to-cook phenomenon seems to be
related to several factors, including car-
bon monoxide or oxides of nitrogen con-
(Pool 1956) or exhaust fumes (Froning
1983), differing concentrations of myo-
globin (Froning and others 1968), the
formation of a reduced nicotinamide-de-
natured globin hemochrome during
cooking (Cornforth and others 1986) and
higher muscle pH ( Trout 1989; Menden-
hall 1989).
Much of the research concerning
cooked color and doneness has been
done on beef, and few data are available
for cooked pork. Therefore, the objective
of this study was to evaluate the effects
of quality of meat, the form of myoglobin,
and the thermal state at the time of cook-
ing on cooked color of ground pork pat-
ties.
Materials and Methods
Meat selection and preparation
Inside ham (#402F, NAMP 1997) mus-
cles (semimembranosus and adductor)
were selected for normal and pale color at
48 h post mortem to fill 2 quality levels,
normal and pale, soft and exudative (PSE,
NPPC 1991). Fresh subcutaneous fat also
was collected. Each group of hams and fat
was allocated randomly to 3 experimental
replications. Ham groups were coarse-
ground through a 1.27 cm plate. The fat
was finely ground through a 0.32 cm plate
and added to the lean to create a 20% fat
blend. Lean and fat were mixed and fine
ground (0.32 cm plate) twice. Meat from
into 2 portions. One portion, which was
highly oxygenated, was formed immedi-
ately after grinding into 113 g patties (1.2
cm thick x 4.2 cm dia) using a Hollymatic
patty maker ( Jet Flow Super, Model 54,
Countryside, Ill., U.S.A.). These patties
were rapidly crust-frozen, individually
vacuum-packaged and stored at –40 °C in
the dark to maintain oxymyoglobin. After
grinding, the other portion was vacuum-
packaged in oxygen barrier bags and
deoxygenated for 3 d at 4 °C. Another
group of patties, which contained pre-
dominantly deoxymyoglobin, were
formed, quickly crust-frozen, vacuum-
packaged and stored at –40 °C. Each
group of patties subsequently was divid-
ed in half, for cooking either as frozen pat-
ties or after thawing.
Cooking procedures
Frozen patties containing oxymyoglo-
bin were removed from their vacuum
packages and loosely wrapped in polyvi-
nyl chloride film for thawing overnight at
1 °C to maintain the oxymyoglobin pig-
ment. Patties containing deoxymyoglobin
were thawed in their vacuum packages to
help maintain the deoxygenated pigment.
Thawed patties containing the 2 pigment
forms were scanned from 400 to 700 nm
(described in following section). Reflec-
tance ratios at 474nm/525nm (indicative
of deoxymyoglobin) were 1.30 and 1.01
for the deoxymyoglobin and oxymyoglo-

© 2002 Institute of Food Technologists Vol. 67, Nr. 3, 2001—JOURNAL OF FOOD SCIENCE 1011

jfsv67n3p1011-1015ms20010218-SR.p65 1011 5/3/2002, 11:50 AM

 Internal color of ground pork . . .

bin patties, respectively. Reflectance ra- Table 1—Least square means for pork patties differing in quality and cooked
tios at 610nm/525nm (indictive of oxy- to 5 endpoint temperatures
myoglobin) were 2.50 and 2.96 for the Endpoint temperature, °C
deoxymyoglobin and oxymyoglobin pat-
Trait Quality 62.8 65.6 71.1 76.7 82.2 SEf
ties respectively. These values are typical
for the specific pigments. Frozen and Visual colorgNormal x2.2a x2.7b x3.6 c x4.5d x4.9e 0.1
PSE y3.8a y4.1b y4.7 c y4.9cd x5.0d
thawed patties were cooked in an electric
SEf 0.2
skillet (Model 72024; The West Bend Co., a* value Normal x7.4 c x6.6b x6.2b x5.4a x5.2a 0.2
West Bend, Wis., U.S.A.) to 1 of 5 endpoint PSE y5.2ab x5.4b x5.0ab x4.7a x4.8a

time-temperature combinations: 62.8 °C SEf 0.9

b* value Normal x13.1 c x12.7b x12.4b x12.0a x11.9a 0.2
for 3 min, 65.6 °C for 1 min, and 71.1 °C, x11.3b x11.2b x10.9ab x10.8a x10.8a
PSE
76.7 °C, or 82.2 °C for 1 s. Care was taken SEf 1.3
to insure that the specified time require- Hue angle h Normal x58.8a x60.1b x60.9b x62.8 c x62.9 c 0.5
Food Chemistry and Toxicology

ment was met for the specified tempera- PSE x62.8ab x62.2a x62.9ab x63.7b x63.3b

ture; that is, patties were held for 3 or 1 SEf 5.1

Saturation Normal x16.3 c x15.5b x15.1b x14.2a x13.8a 0.2
min, or instantaneous (1 s) before the
indexh PSE y13.2bc y13.3 c y12.9ab y12.6a x12.6a
patties were allowed to cool. These time- SEf 0.8
temperature combinations meet FDA Myoglobin Normal x62.5a x69.4b x78.5 c x86.0d x89.0d 1.6
denaturation,% PSE y77.9a y79.6ab x81.5b x84.9 c x86.5 c
Food Code (FDA 1999). Patties were
turned at approximately 1 min intervals SEf 1.8
a-e Means in a row with a different superscript letter differ (P<0.05)
and removed from the skillet 2 °C to 3 °C f Standard errors for endpoint temperature (right column) and quality (quality column)
before reaching the target endpoint tem- g Visual color : 1 = purplish red to pinkish red, 2 = moderately pink, 3 = slightly pink, 4 = very slightly
perature to allow post-cooking tempera- pink to tannish white, 5 = tannish white, no evidence of pink
h Saturation index = (a* 2 + b* 2 ) 1/2 ; hue angle = (b*/a*) tan-1
ture rise. If necessary to meet the speci- x-y Means in a column for each trait with a different superscript letter differ (P < 0.05)

fied time at a temperature, patties were

replaced near or onto the heated surface.
Internal temperatures in the center of
patties were monitored using an Omega
Technologies hypodermic probe-type
thermocouple (Model HYP2-21-1-1/2-T-
G-48-OST-M) connected to a Doric Tren-
dicator (Model 410A; Omega Engineering,
Inc., San Diego, Calif., U.S.A.).
Color evaluations
Cooked patties were cut through the
center perpendicular to the flat surfaces
and immediately evaluated by 3 experi-
enced observers. Scores to the nearest
one-half point were recorded on a 5-point
scale (1 = purplish red to pinkish red, 2 =
moderately pink, 3 = slightly pink, 4 = very
slightly pink to tannish white, 5 = tannish
white, no evidence of pink). Illumination
was standardized at 538 lux of warm white
fluorescent lighting. Patties then were cut
parallel to the flat surface and color was in-
strumentally evaluated on 3 locations us-
ing the HunterLab Miniscan with an aper-
ture of 2.54 cm (Hunterlab, Reston, Va.,
U.S.A.). Reflectance ratio (630 nm/ 580
nm), hue angle [(b*/a*) tan-1] and satura-
tion index [(a*2 + b*2)1/2 ] were calculated
from reflectance data and Hunter L* a* b*
values (Illuminant C).
Myoglobin denaturation
A raw patty and the remaining portion
of each of the cooked patties (approxi-
mately 80 g) were blended with 5 volumes
of cold 40 mM phosphate buffer at pH 6.8
for 15 s (Warriss 1979). Mixtures were
stored at 1 °C for 1 h and centrifuged at
17,000 x g at 4 °C for 1 h. The supernatant
was filtered through a syringe filter (0.45
ìm) into spectrophotometer vials. To en-
sure pigment reduction, 3 to 4 crystals of
sodium hydrosulfite were added to the fil-
tered solution which was confirmed by
scanning the samples using a Hitachi U-
20101 Spectrophotometer (Hitachi Instru-
ments Inc., San Jose, Calif., U.S.A.). Myo-
globin was quantified using absorbency at
418 nm, appropriate dilution factors and
an extinction coefficient of 128,000 (Anto-
nini and Brunori 1971). Percentage myo-
globin denaturation was calculated as:
(% myoglobin in raw patties – % myoglo-
bin in cooked patties)/ % myoglobin in raw
patties x 100.
Statistical Analysis
Data were analyzed using a split-plot
design and 3 replications. Quality group (n
= 2) was the whole plot and endpoint tem-
perature (n = 5), myoglobin form (n = 2)
and cooking state (n = 2) were sub-plots.
PROC MIXED of the Statistical Analysis
System (SAS 1998) was used for analysis of
variance and protected least significant
differences (LSDs) were assigned at
P < 0.05.
Results and Discussion
Treatment group
The following sections discuss the sig-
nificant interactions that occurred be-
tween treatment groups (PSE and normal
meat patties) and endpoint temperatures
for each trait measured.
Color
The internal cooked color of pork loin
chops became progressively less reddish-
pink as endpoint temperatures increased
(Lien and others 2001). This color change
has been observed for many years but not
well documented. Patties made with nor-
mal quality pork muscle were more pink
(lower visual scores, P < 0.05) than those
made from PSE muscle (Table 1). Scores
for normal patties increased (P < 0.05)
from 2.2 at 62.8 °C to 4.9 at 82.2 °C; and
scores for PSE patties also increased
(P < 0.05) but over a narrower range (3.8 to
5.0). The incremental change in color was
more apparent for patties made with nor-
mal meat than for PSE meat because PSE
visual scores at 62.8 °C were nearly 2 times
greater for the PSE group compared to the
normal (3.8 against 2.2). PSE patties
looked as done at 62.8 °C as normal patties
at a medium degree of doneness (71.1 °C).
Furthermore, patties made with PSE mus-
cle did not appear pink at any endpoint
temperature, whereas the normal patties
were pink at 62.8 °C and 65.6 °C and very
slightly pink at 71.1 °C. These data indi-
cate that PSE patties were prone to prema-
ture browning, a condition in ground beef
where patties appear done at lower than
expected endpoint temperatures (Hague
and others 1994). Perhaps the greater
heat lability of PSE myoglobin is related to

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jfsv67n3p1011-1015ms20010218-SR.p65 1012 5/3/2002, 11:50 AM

 Internal color of ground pork . . .
Table 2—Least square means for pork patties differing in myoglobin form when
cooked to 5 endpoint temperatures
Trait Myoglobin form f 62.8
Visual scoreh Dmb x2.5a
Omb y3.5a
SEg 0.2
b* value Dmb x13.1 c
Omb x11.2 c
SEg 1.3
Myoglobin Dmb x64.0a
y76.4a
denaturation,% Omb
SEg 1.8
a-e Means in a row for each trait with a different superscript letter differ (P < 0.05)
f Dmb = deoxymyoglobin, Omb = oxymyoglobin
g Standard errors for endpoint temperature (right column) and myoglobin form (myoglobin column)
h Visual color: 1 = purplish red to pinkish red, 2 = moderately pink, 3 = slightly pink, 4 = very slightly
pink to tannish white, 5 = tannish white, no evidence of pink
x-y Means in a column for each trait with a different superscript letter differ (P < 0.05)
prerigor muscle conditions described by
Briskey (1994). The rapid accumulation of
lactic acid in warm muscle during chilling
may increase the sensitivity of the pig-
ment to heat in a manner similar to the de-
crease in color stability in fresh pork. In
addition, Trautman (1966) reported great-
er separation of the heme from the globin
as pH decreased, again perhaps leading to
a more heat labile pigment in the PSE
meat.
Instrumental measurements of color
were consistent with trends described for
visual evaluations. Although data were
not significant at each endpoint tempera-
ture, the values for a*, b*, and saturation
index decreased, and hue angle increased
(all indicators of less pink and more yel-
low) as endpoint temperature increased
for patties made from both normal and
PSE muscle (Table 1). Differences for in-
strumental color traits were greater for
patties made with normal quality pork
than PSE meat, a trend also evident in the
visual color scores. These color changes
were expected as the cooked color of pork
changed from pink (normal patties) to a
tan/tannish-white color as the degree of
doneness increased. Instrumental color
measurements for patties made with PSE
muscle were indicative of a more well-
done coloration (lower values for a*, b*,
and saturation index and higher hue an-
gles) than normal patties, especially at the
lower endpoint temperatures. Although
the differences for instrumental color
measurements were small between pat-
ties of normal and PSE muscle, the pattern
for greater pigment color loss in PSE meat
was consistent and typical of muscle con-
taining a small amount of myoglobin. Val-
ues for saturation index and hue angle for
patties made with PSE meat would be in a
jfsv67n3p1011-1015ms20010218-SR.p65 1013
Endpoint temperature, °C
65.6 71.1 76.7 82.2
x2.9b x3.8 c x4.5d x4.9e
y3.9b y4.5 c y4.9d x5.0d
x12.8bc x12.6b x12.2a y12.0a
x10.9bc x10.8ab x10.6a x10.7ab
x68.3b x75.6 c x82.8d x86.7e
y80.7b y84.4 c y88.2d x88.8d
more tan to yellow region of a CIE-Lab col-
or space than patties from normal meat,
indicating that myoglobin in the PSE pat-
ties prematurely browned.
Myoglobin denaturation
PSE meat had higher myoglobin dena-
turation (Table 1) than normal meat at
62.8 °C to 65.6 °C (P < 0.05). No differences
were observed between normal and PSE
meat at endpoint temperatures of 71.1 °C
and higher. As expected, myoglobin dena-
turation increased (P < 0.05) as endpoint
temperature increased for both normal
and PSE meat patties, and these data
compliment those for visual and instru-
mental color assessments. It is interesting
that the pigment in patties made from
PSE meat was more heat labile at lower
temperatures than was myoglobin in pat-
ties made with normal quality pork. The
postmortem conditions related to devel-
opment of PSE meat (lower muscle pH in
chilling carcasses) or the slightly lower pH
typical of postrigor PSE pork (Briskey
1964) may predispose the myoglobin to
greater heat denaturation at lower tem-
peratures than normal.
Myoglobin form
Table 2 contains the least square
means for the traits that were significant
between oxymyoglobin and deoxymyoglo-
bin and endpoint temperatures (P < 0.05).
For patties containing deoxymyoglobin,
differences in color were observed at every
endpoint temperature. Visual scores of
patties containing oxymyoglobin also in-
creased (P < 0.05) from 62.8 °C to 76.7 °C;
however, these patties were visually less
pink compared with patties containing
deoxymyoglobin. These results agree with
those of Hunt and others (1999) who
Vol. 67, Nr. 3, 2002—JOURNAL OF FOOD SCIENCE
found that oxygenated samples had a
more tannish color than deoxygenated
samples. No differences in b* values were
detected from 62.8 °C to 76.7 °C; however,
SEg
at 82.2 °C values were higher for those pat-
0.1 ties. These b* trends are similar to those
observed by Hunt and others (1999) in
0.2 ground beef where patties with oxymyo-
globin and deoxymyoglobin decreased in
b* value as endpoint temperature in-
1.3
creased, indicating that ground meat be-
comes less yellow as endpoint tempera-
ture increased.
Food Chemistry and Toxicology
Two effects were evident when per-
centage denaturation of myoglobin was
calculated for patties containing oxymyo-
globin and deoxymyoglobin. First, per-
centage denaturation of deoxymyoglobin
was lower (P < 0.05) at every endpoint
temperature except 82.2 °C than in patties
containing oxymyoglobin. These results
are consistent with previous work (Machlik
1965), Hunt and others 1999, Lavelle and
others 1995) where deoxymyoglobin dena-
tured at higher temperatures than oxy-
myoglobin. Secondly, both types of pig-
ment significantly increased in
percentage denaturation as endpoint
temperatures increased.
Initial cooking state
Significant interactions between end-
point temperatures and physical state of
the patties before cooking occurred for a*
values, saturation index, hue angle, and
myoglobin denaturation (Table 3).
Color
Patties cooked from the frozen state
had approximately 3-fold lower a* values
(P < 0.05) at every endpoint temperature
than those cooked as thawed. Patties
cooked frozen appeared fully cooked at
the lowest final temperature (62.8 °C).
Therefore, the endpoint temperature at
which these patties appear pink cannot be
determined from our data. As endpoint
temperatures increased, a* values de-
creased for patties cooked from thawed or
frozen; however, the changes were not al-
ways significant for frozen patties. The a*
value for frozen patties was higher (P <
0.05) only at 62.8 °C than at 76.7 °C.
Saturation index, an indicator of color
intensity, was similar for frozen and
thawed patties, except for values at
82.2 °C, in which cooked-from-frozen pat-
ties had more intense (P < 0.05) color than
cooked-from-thawed patties. As tempera-
ture increased, the saturation indices de-
creased for patties cooked from both fro-
zen and thawed. In the frozen group,
saturation index values at 62.8 °C and
1013
5/3/2002, 11:50 AM
 Internal color of ground pork . . .

Table 3—Least square means for pork patties cooked to 5 endpoint tempera- come less pink as internal temperatures
tures from either the frozen or thawed state increase. Patties made from PSE meat are
Endpoint temperature, °C prone to premature browning and will ap-
pear more well done than patties from
Trait Precook State f 62.8 65.6 71.1 76.7 82.2 SEf
normal quality pork at endpoint tempera-
a* value Frozen x2.8b x2.6ab x2.4ab x2.2a x2.4ab 0.2
y9.7 c y9.4 c y8.9b y8.0a y7.6a
tures from 62.8 °C to 82.2 °C. Patties
Thawed
cooked when they contain highly oxygen-
SEf 0.9
Saturation indexg Frozen x15.3b x14.9b x14.5a x14.2a x14.3a 0.2 ated pigment appear prematurely brown
Thawed x14.2d x13.9cd x13.5 c x12.6b y12.1a and will be less pink than patties contain-
SEf 0.8 ing deoxygenated myoglobin. Patties
Hue angleg Frozen x79.5a x79.9ab x80.6bc x81.1 c x80.2ab 0.5 cooked from the frozen state will be less
Thawed y42.1a y42.4ab y43.3b y45.3 c y46.1 c
pink internally than patties cooked after
SEf 5.1
Myoglobin Frozen x67.1a x72.6b x79.7 c x85.6d x87.5d 1.6 thawing and could appear more well done
Food Chemistry and Toxicology

denaturation, % Thawed y73.4a y76.4a x80.3b x85.4 c x88.0 c than they really are. Myoglobin denatur-
SEf 1.8 ation increases as endpoint temperatures
a-e Means in a row for each trait with a different superscript letter differ (P < 0.05) increase in patties of both normal and PSE
f Standard errors fro endpoint (right column) and precook form (precook column)
gSaturation index = (a* 2 + b* 2 ) 1/2 ; hue angle = (b*/a*) tan-1 quality.
x-y Means in a column for each trait with a different superscript letter differ (P < 0.05)

65.6 °C were higher (P < 0.05) than for the
higher endpoint temperatures.
Overall, the tendency for hue angles
was to increase as temperatures in-
creased. Thawed patties had lower hue
angle values at every endpoint tempera-
ture (P < 0.05) than cooked-from-frozen
patties. Hue angles for cooked-from-fro-
zen patties ranged from 79.5 to 81.1. Larg-
er hue angles indicate a more yellowish-
tan sample. Although the range was
narrow, some differences were found
among endpoint temperatures. At 62.8
and 65.6 °C, hue angles of frozen patties
did not differ (P > 0.05). At 76.7 °C, frozen
patties had a larger hue angle than all oth-
er endpoint temperatures except 71.1 °C.
Values for cooked-from-frozen patties
were much larger (P < 0.05) than hue an-
gles from those thawed before cooking.
Myoglobin denaturation
No differences in myoglobin denatur-
ation (P > 0.05) were observed between
frozen and thawed patties cooked above
65.6 °C, but values at 62.8 °C and 65.6 °C
were lower (P < 0.05) for the frozen patties
versus the thawed patties. Trout (1989)
found increasing percent myoglobin de-
naturation from 55 ° to 83 °C.
Consideration of the thermal
properties of meat and color
It is clear that patties cooked from fro-
zen had less red color and had greater
myoglobin denaturation at the lower end-
point temperatures relative to cooked
from thawed patties. This indicates that
frozen patties become more tan early in
the cooking process similar to premature
browning in ground beef. Similar results
have been reported for beef patties
cooked from the frozen state ( Van Laack
and others 1996ª; Bigner-George and Ber-
ry 2000). These differences might be due
to the presence of ice in the frozen patties.
When frozen patties are cooked, there
must be a phase change as the ice is con-
verted into water without a change in tem-
perature, and 80 cal/g would be absorbed
(latent heat of fusion). Even though the
thawed patties also underwent the
change from ice to water, it occured as a
separate event (thawing) and the energy
absorbed by the product was not cumula-
tive as it was in the frozen patties (Mohse-
nin 1980). When energy is transferred be-
tween 2 bodies of mass, a large part of that
energy is converted into heat, which rep-
resents a change in enthalpy. However,
the other part of the energy does not re-
flect as heat and it only causes a change in
the order of the molecules, that is, a
change in entropy. This means that not all
types of energy will change the actual
temperature of the product. Differential
energy absorbed by the frozen patties
could denature the pigment earlier than
in thawed patties, which could explain the
more well-done appearance of patties
cooked from frozen. Furthermore, the
thermal conductivity is 2 or 3 times greater
for frozen meat than for thawed meat.
Thus, at a common final endpoint temper-
ature, the frozen patties would have ab-
sorbed more energy than the thawed
meat.
Conclusions
P ATTIES MADE FROM NORMAL QUALITY
pork will develop cooked internal color
in a normal, predictable pattern and be-
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MS20010218 Submitted 5/4/01, Accepted 11/28/01,
Received 11/28/01
Contribution No. 01-340-J from the Kansas Agr. Exp. Sta-
tion, Manhattan.
The authors are with Kansas State Univ., Animal
Sciences and Industry, 232 Weber Hall, Manhat-
tan, KS 66506-0201. Direct inquiries to author
Hunt (E-mail: hhunt@oznet.ksu).
Food Chemistry and Toxicology
1015