PROCESSING AND PRODUCTS
Effect of Calcium Marination on Biochemical and Textural Properties of
Peri-Rigor Chicken Breast Meat
L. L. YOUNG and C. E. LYON
*Richard B. Russell Agricultural Research Center, USDA, Agricultural Research Service,
P. O. Box 5677, Athens, Georgia 30604-5677
ABSTRACT The objective of this study was to
evaluate effects of marinades containing varying calcium
concentrations on the biochemical and texture charac-
teristics of peri-rigor chicken breast fillets. Breast
muscles from 200 broiler chickens were excised immedi-
ately post-mortem and marinated in 0, 50, 100, 150, or
200 mM CaCl2. The treatments had no effect on meat pH
either before or after cooking, but as calcium concentra-
tion increased, the normal post-mortem conversion of
adenosine triphosphate (ATP) to inosine monophos-
(Key words: calcium, marination, tenderness, moisture binding, chicken meat)
INTRODUCTION
For many years, poultry was sold in the U.S.
primarily as whole, ready-to-cook birds; but beginning
in the 1950s, changes occurred in the marketplace that
resulted in birds being sold as parts or deboned
products. As the practice of cutting carcasses moved
from the retail meat market to the processing plant, it
became clear that a 6 to 8 h post-mortem aging period
prior to cutting up was necessary to prevent toughening
(de Fremery and Pool, 1963; Klose, et al., 1972; Lyon and
Wilson, 1986). Because nearly 90% of the poultry is sold
in the U.S. today as parts or as further processed
products (W. P. Roenigk, National Broiler Council, 1155
15th St. N.W., Washington, DC 20005, personal commu-
nication), the practice of aging front halves or whole
carcasses has become an important cost consideration.
Numerous studies have been conducted to better
understand the post-mortem toughening and tenderiz-
ing process and to develop methods for eliminating the
aging practice for both poultry muscle and for muscle of
other species (Lyon and Wilson, 1986; Lyon and Lyon,
1991; Sams and Janky, 1991; Papinaho and Fletcher,
1995; Papinaho et al., 1995). These studies have led to an
improved understanding of the rigor process that begins
shortly after the death of an animal. At that time,
glycolytic activity results in the depletion of adenosine
Received for publication April 15, 1996.
Accepted for publication August 30, 1996.
197
phate (IMP) increased, according to the IMP:ATP ratios
(R-values). Calcium treatment at all levels tested im-
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proved meat tenderness, but both marinade absorption
and cooking losses increased as the calcium concentra-
tion in the marinades increased. It was concluded that
although treating peri-rigor breast muscle with calcium
might be useful in reducing or eliminating the condi-
tioning period to assure tender chicken, methods must
be developed for restoring the moisture binding proper-
ties that are damaged by the calcium.
1997 Poultry Science 76:197–201
triphosphate (ATP) and accumulation of lactate in the
sarcoplasm. Consequently, the sarcoplasmic reticulum
loses its ability to control cytosolic calcium concentra-
tion, resulting in up to a 10-fold Ca2+ concentration
increase (Goll et al., 1983). This increase activates myosin
adenosine triphosphatase, resulting in contraction of the
muscle (rigor mortis).
Because rigor develops much faster in avian than in
mammalian muscle (Sams and Janky, 1991), broiler
carcasses are usually in the early stages of rigor when
they emerge from the chiller and the muscles are rigid,
firm, and inextensible. However, within 6 to 8 h, the
muscles become less rigid and regain some of their
extensibility (resolution of rigor). Resolution remains an
incompletely understood phenomenon, but evidence
indicates that certain structures—most notably the Z-
disks and elements of the cytoskeleton—in the myofibril
undergo degradation (Sayer, 1970; Henderson et al.,
1970; Penny, 1980; Nelson and Traub, 1983; Ouali et al.,
1983; Ouali, 1984; Koohmaraie et al., 1988b; Whipple and
Koohmaraie, 1991).
There are two main theories than explain the
tenderization process. The first suggests that the in-
creased ionic strength of the sarcoplasm due to the post-
mortem influx of calcium ions solubilizes myofibrillar
structural elements, resulting in their degradation (Ou-
ali, 1990). The second theory supports the notion that
endogenous calcium-activated proteinases (calpains) are
activated by the influx of calcium ions and that they
subsequently proteolyze some of the structural elements,
leading to degradation of the myofibrillar matrix
198 YOUNG AND LYON
(Koohmaraie, 1992). There is no preponderance of
evidence to support either view, but results indicate that
proteolysis is, at least in part, responsible for post-
mortem tenderization (Koohmaraie et al., 1987, 1988b;
Koohmaraie, 1988, 1992; Wheeler et al., 1990; Whipple
and Koohmaraie, 1991; Kendall et al., 1993).
Several attempts have been made to take advantage
of the ability of the calpains to hasten tenderization of
mammalian muscle tissue (Koohmaraie et al., 1988a,
1989, 1990). These attempts have generally involved
infusion of calcium salts into the carcass via the
circulatory system or injection of the salts into the
muscle tissue. These processes reportedly lead to
tenderization of some mammalian muscles within hours
post-mortem compared to days post-mortem for un-
treated muscles (Koohmaraie et al., 1988a).
Even though extensive research has been conducted
on effects of calcium treatment on mammalian muscles,
little information is available on effects of such treat-
ments on poultry muscle tissue. Young et al. (1991)
reported that calcium chloride marination of chicken
fillets that had been harvested immediately post-mortem
produced fillets that were more tender than similar
fillets marinated in NaCl, MgCl2, or MnCl2 solutions.
However, prerigor fillets marinated in solutions contain-
ing divalent cations had depressed water-holding capac-
ity as compared to the fillets marinated in solution
containing only monovalent cations. Previous work
suggested that the effects of calcium might be related to
calcium effects on ATP metabolism and muscle pH. The
objective of this study was to evaluate the effects of
various calcium marinades on texture, moisture binding
characteristics, pH, and ATP metabolism of chicken
breast fillets harvested immediately post-mortem (peri-
rigor).
MATERIALS AND METHODS
Treatments
Fifty commercially reared broilers were obtained from
a local poultry processor, transported to the laboratory,
and held overnight in order to minimize effects of
catching and handling. The birds were stunned electri-
cally (50 V alternating current for 10 s) and killed by
exsanguination. They were not scalded or picked. After a
2-min bleeding period, the left Pectoralis major from each
bird was immediately excised and weighed (wti). Batches
of 10 muscles each were vacuum-tumbled1 for 15 min with
10% (wt/vol) of 0, 50, 100, 150, or 200 mM CaCl2 plus
sufficient NaCl so that all solutions were isoionic (0.6 M).
The solutions were formulated thus to ensure that any
1Roschermatic TU 120 tumbler, Roscherwerk GMBH, Postfach 3566,
Osnabruck, Germany.
2Orion Research Inc., Boston, MA 02129.
3Instron Corp., Canton, MA 02021.
effects were specific to calcium and not general ionic
effects. Each muscle was immediately sampled for R-
value analysis, weighed again (wtt), and its pH recorded
(pHt). Each muscle was then cooked, weighed (wtc),
sealed in a plastic bag, cooled overnight in a 4 C
refrigerator, and sampled for shear analysis. The experi-
ment was repeated for a total of four replicates.
Cooking Procedure
Each muscle was vacuum-sealed in an individual
cooking bag. Two of the muscles had meat thermometers
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inserted into their geometric centers. The bagged muscles
were then immersed in a 90 C water bath and cooked until
internal temperatures of those equipped with the ther-
mometers reached 78 C (about 20 min).
Moisture Binding Properties
Marinade absorption and cooking loss were calculated
as
Absorption = 100 × (wtt – wti)/wti
and
Cooking loss = 100 × (wtt – wtc)/wtt
pH Measurements
The pH of marinated and cooked samples was
measured with the aid of a pH meter equipped with a
needle electrode.2 The probe was inserted into the
geometric center of the thickest part of the muscle and pH
recorded when a stable reading on the meter was
observed for 10 s.
R-Values
The ratios of adenine:inosine nucleotide (R-values) in
the muscle tissue were observed according to the
procedure of Honikel et al. (1981). Briefly, the procedure
was to extract the nucleotides in 1 M HClO4 and then
observe the ratio of light absorption at 250 and 260 nm. All
samples for R-value analysis were stored in the 1 M HClO4
until the absorption characteristics could be evaluated (no
more that 6 h).
Shear Values
The cooked fillets were tempered in a 20 C water bath
for 30 min prior to removing them from the plastic bags. A
1.27-cm wide template was used as a guide to cut each
muscle to a standard size. The template was oriented from
anterior to posterior because of the extreme contraction of
some of the muscles. The force required to shear the
samples was observed with an Instron Universal Testing
Machine3 equipped with a Warner-Bratzler shear device.
 CALCIUM AND POULTRY MEAT QUALITY 199
TABLE 1. Effect of calcium chloride marinades on moisture binding and
biochemical and textural properties of peririgor chicken Pectoralis major

Marinade Cooking Marinated Cooked Shear

Treatment (n) absorption loss pH pH R-value value
(mM Ca++) (%) (kg)
0 40 4.64b 14.9a 6.33 6.23 0.958c 7.4a
50 40 5.74a 17.3ab 6.31 6.32 0.979bc 5.4b
100 40 6.12a 18.2b 6.35 6.31 0.989bc 5.4b
150 50 6.16a 18.6b 6.26 6.29 1.001ab 5.1b
200 30 6.01a 19.7c 6.29 6.30 1.025a 5.5b
SEM 0.12 0.24 0.003 0.001 0.01 0.15
a–cMeans within a column with no common superscript differ significantly (P < 0.05).

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Full scale load was 100 kg and cross head speed was 50
cm/min. Duplicate observations were made on each
sample, and the duplicate mean was recorded as the shear
value (in kilograms) for the sample.
Statistical Analysis
The data were analyzed by analysis of variance using
treatments (i.e., marinades) and replicates as main effects.
As the treatment by replicate interaction was not
significant, the data were pooled over replicates and
treatments tested for statistical significance using the
overall error mean square. Treatment means were
separated by Duncan’s multiple range test at the 0.05 level
of probability (Steel and Torrie, 1960).
RESULTS AND DISCUSSION
Moisture Binding Properties
As calcium content of the marinades increased,
moisture absorption also increased (Table 1). However,
muscles that received the highest calcium treatment and,
thus absorbed the most moisture, also had the highest
cooking losses. These results differ from those of Young
and Lyon (1986), who found that moisture absorption by
CaCl2 plus NaCl-treated breast fillets was similar to that of
fillets treated with NaCl alone, but that cooked yield of the
fillets treated with CaCl2 and NaCl was greater than that
of controls treated with NaCl alone. However, the former
study was conducted with commercially processed, fully
aged muscles, whereas the present study was conducted
with peri-rigor muscles. High cooking loss is economi-
cally important, so a method must be found to reduce
cooking losses in order to take advantage of any beneficial
effects of calcium treatment. In the previous study with
aged meat (Young and Lyon, 1986), moisture absorption
was greater and cooked yield was the same for muscles
treated with calcium plus sodium tripolyphosphate
(STPP) compared to those treated with STPP alone.
However, because the previous study involved only
postrigor muscle, application of STPP to the cooking loss
problem will require further study.
Muscle pH
Calcium treatments had no significant effect on either
marinated pH or cooked pH (Table 1). Post-mortem pH
values of avian muscle declines very rapidly from near
neutrality to about 5.6 to 5.8 within 6 to 8 h (Stewart et al.,
1984). Because an increase in cytosolic calcium is a
precipitating factor in the onset of rigor mortis, one would
expect that the addition of calcium would hasten the
process and lower the pH of calcium-treated muscles
within 1 to 2 h post-mortem. It is possible the post-mortem
pH decline was so precipitous that small effects caused by
the treatments could not be detected with the methods
that were employed. Differences in moisture binding
properties by meat tissue are often ascribed to pH effects.
However, in the present case, differences in moisture
binding properties must be ascribed to other, as yet
undefined, factors because pH was unaffected by treat-
ment.
R-value
The R-value is a measure of the degree of conversion of
adenosine to inosine nucleotides and can, therefore, be
used to monitor development of rigor (Papa and Fletcher,
1988). They indicated that R-values of P. major muscles
typically reach 0.95 to 0.97 within 15 to 30 min post-
mortem and 1.2 to 1.3 within 2 to 4 h post-mortem. The
present data (Table 1) indicate that the onset of rigor was
significantly hastened by the calcium treatments. In fact,
R-values for the highest levels of calcium were equivalent
to 2 to 4 h post-mortem even though they were observed
only 15 to 30 min post-mortem. However, ultimate R-
values typically are 1.35 (Papa and Fletcher, 1988; Young
et al., 1991), indicating that the muscles were in a peri-rigor
state when cooked.
Shear Values
Calcium-treatment, regardless of concentration, signifi-
cantly reduced shear values when compared to controls
(Table 1). Thus, it appears that peri-rigor avian muscle
responds to calcium in a manner similar to that of
mammalian muscle by becoming more tender (Kooh-
200 YOUNG AND LYON
TABLE 2. Distribution of shear values of cooked control and
calcium-treated chicken Pectoralis major muscles according to
the sensory categories of Lyon and Lyon (1991)
Sensory tenderness Calcium-
(shear value) Control treated
(%)
Very tender 2.5 9.5
(shear value < 3.62 kg)
Moderately to slightly tender 35.0 72.8
(shear value 3.62 to 6.61 kg)
Slightly tender to slightly tough 42.5 15.2
(shear value 6.62 to 9.60 kg)
Slightly to moderately tough 20.0 1.9
(shear value 9.61 to 12.60 kg)
Very tough 0.0 0.6
(shear value > 12.60 kg)
maraie, 1988, 1992; Koohmaraie et al., 1988a; Koohmaraie
and Shackelford, 1991). Using the standards established
by Lyon and Lyon (1991), mean shear values of control
muscles (0 calcium) corresponded to a sensory score of
“slightly tender to slightly tough”, whereas those of the
calcium-treated muscles corresponded to “moderately to
slightly tender”. However, of greater practical interest
than the mean shear values are the extremes. Table 2
shows the percentages of muscles with shear values in
each of the five tenderness groups described by Lyon and
Lyon (1991). Twenty percent of the controls exhibited
shear values greater than 9.61 (slightly to moderately
tough) compared to 2.5% for the calcium-treated muscles.
Shear values indicate that treating early harvested breast
meat with calcium would reduce toughness and could
improve consumer satisfaction. However, other quality
attributes, such as yield and juiciness, must also be
considered before technology can be developed to take
full advantage of this potential.
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