Content uploaded by Samooel Jung
Author content
All content in this area was uploaded by Samooel Jung on May 28, 2015
Content may be subject to copyright.
INTRODUCTION
Strategy for poultry selection is typically focused on
a quantitative trait to improve growth rate and meat
yield. Thus, birds improved by selection can reach mar-
ket weight in a 6-wk raising term with high meat yield
(Fanatico et al., 2007). Recently, qualitative traits af-
fecting nutritional and sensory quality of meat have
been valued over quantitative traits because of in-
creased consumer demand for high-quality and health-
beneficial poultry products.
Among endogenous compounds in the skeletal muscle
of vertebrate animals, several compounds, such as car-
nosine, anserine, and creatine, are known to be bioactive
(Schmid, 2009). Carnosine is abundant in mammalian
skeletal muscles (Stenesh and Winnick, 1960), acts as a
pH buffer in muscle, and has antiaging, antiglycation,
antioxidation, and neurotransmitter functions (Chan
and Decker, 1994; Schmid, 2009; Bellia et al., 2011).
Carnosine can be used as a therapeutic substance for
suppressing various diseases, such as diabetes, cata-
racts, ischemia, and Alzheimer’s disease (Quinn et al.,
1992; Kawahara et al., 2007; Hipkiss, 2009). In addi-
tion, carnosine in the human body attenuates acido-
sis and a loss of force during exercise (Baguet et al.,
2010). Anserine is an N-methylated derivative of carno-
sine and is abundant mostly in nonmammalian species,
such as poultry (Abe and Okuma, 1995); it shows sim-
ilar biological activities as carnosine (Schmid, 2009).
Creatine is a nitrogenous organic acid (Schmid, 2009)
that supplies energy to muscles (Wyss and Kaddurah-
Daouk, 2000). Therefore, creatine is used by athletes
to increase performance capability (Volek and Rawson,
2004). In addition, creatine has been reported to show
neuroprotective effects (Adhihetty and Beal, 2008).
Although carnosine and creatine are endogenously
synthesized in the human body, supplementation of
Carnosine, anserine, creatine, and inosine 5 ′-monophosphate contents
in breast and thigh meats from 5 lines of Korean native chicken
Samooel Jung ,* Young Sik Bae ,† Hyun Joo Kim ,* Dinesh D. Jayasena ,† Jun Heon Lee ,†
Hee Bok Park ,‡ Kang Nyung Heo ,§ and Cheorun Jo *1
* Department of Agricultural Biotechnology and Research Institute of Agriculture and Life Science,
Seoul National University, Seoul 151-921, Republic of Korea; † Department of Animal Science and Biotechnology,
Chungnam National University, Daejeon 305-764, Republic of Korea; ‡ Institute of Agricultural Life Sciences,
Gyeongsang National University, Jinju 660-701, Republic of Korea; and § Poultry Science Division,
National Institute of Animal Science, Rural Development Administration, Cheonan 331-801, Republic of Korea
ABSTRACT The aim of this study was to examine the
effect of chicken line on the contents of endogenous
compounds, including carnosine, anserine, creatine,
and inosine 5 ′-monophosphate (IMP), in breast and
thigh meats from 5 lines of Korean native chicken for
the development of high-quality meat breeds. Addition-
ally, the effects of sex (male or female) and meat type
(breast or thigh meat) were examined. In total, 595 F1
progeny [black: 90 (male: 45, female: 45); gray-brown:
110 (male: 52, female: 58); red-brown: 136 (male: 68, fe-
male: 68); white: 126 (male: 63, female: 63); and yellow-
brown: 133 (male: 62, female: 71)] from 70 full-sib fami-
lies were used. The male chicken from the red-brown
line and the female chicken from the black line showed
the highest BW among the 5 lines. Carnosine content
was higher in female chicken and breast meat than in
male chicken and thigh meat, respectively. Breast meat
contained higher anserine content compared with thigh
meat. The sex effect on anserine was not consistent be-
tween breast and thigh meat. Creatine content was not
consistently influenced by sex between breast and thigh
meat, and no meat type effect was observed. The IMP
contents were higher in female chicken and breast meat
compared with male chicken and thigh meat, respec-
tively. In addition, we clearly observed line effects by
the comparison of the contents of carnosine, anserine,
creatine, and IMP for each meat type according to each
sex. These data are useful for selection and develop-
ment of high-quality, meat-type chicken breeds.
Key words: chicken , carnosine , anserine , creatine , inosine 5 ′-monophosphate
2013 Poultry Science 92 :3275–3282
http://dx.doi.org/ 10.3382/ps.2013-03441
3275
Received June 24, 2013.
Accepted August 8, 2013.
1 Corresponding author: cheorun@snu.ac.kr
© 2013 Poultry Science Association Inc.
these compounds is recommended to maintain or im-
prove health. The use of these supplements has been
particularly emphasized in older men because carnosine
synthesis and skeletal muscle mass decrease over time
(Gotshalk et al., 2002; Tallon et al., 2007). Carnosine,
anserine, and creatine can be acquired by consuming
meat, whereas foods of plant origin cannot supply these
compounds (Schmid, 2009). Nagai et al. (1996) ob-
served an improvement in recovery from mental fatigue
in subjects with heavy workloads when chicken that in-
cluded carnosine and anserine was ingested. Therefore,
carnosine, anserine, and creatine in meat have nutri-
tional properties, and increasing their concentrations in
meat may improve the nutritional value.
Inosine 5 ′-monophosphate (IMP) is also an endog-
enous compound in muscle. It is well known to affect
meat flavor (Kawai et al., 2002) and IMP contributes
to the umami taste (described as savory), alone or con-
jugated with monosodium glutamate for synergistic ef-
fects (Kawai et al., 2002; Koutsidis et al., 2008). There-
fore, increasing IMP in meat may improve the sensory
quality of meat.
Recently, a governmental organization in Korea has
been attempting to develop a new chicken breed. This
project primarily focused on developing a high-quality,
meat-producing breed by using Korean native chickens
(KNC) to meet the demands of consumers (Park et
al., 2012). The 5 lines of KNC (i.e., black, gray-brown,
red-brown, white, and yellow-brown) were proposed as
candidates for selection. The aim of this study was to
investigate the concentrations of carnosine, anserine,
creatine, and IMP in breast and thigh meats from 5
lines of KNC to obtain information helpful for the de-
velopment of selection strategies.
MATERIALS AND METHODS
Birds
A 2-generation resource pedigree using 5 lines of KNC
was established and managed in this study. Within each
line, 3 sires were mated with 14 to 15 dams to produce
F1 chicks. In total, 595 F1 progeny [black (B): 90 (male:
45, female: 45); gray-brown (G): 110 (male: 52, female:
58); red-brown (R): 136 (male: 68, female: 68); white
(W): 126 (male: 63, female: 63); yellow-brown (Y): 133
(male: 62, female: 71)] from 70 full-sib families were
used in this study. Chickens were raised at the Nation-
al Institute of Animal Science of Korea (Seonghwan,
Korea) and fed ad libitum a commercial formula feed
containing 18.2% concentrated protein and 2,859 kcal/
kg of ME. Chicken care facilities and the procedures
used in this study were performed to meet or exceed
the standards established by the Committee for Ac-
creditation of Laboratory Animal Care at the National
Institute of Animal Science in Korea. The study was
also conducted in accordance with recommendations
described in “The Guide for the Care and Use of Labo-
ratory Animals” published by the Institutional Animal
Care and Use Committee of the National Institute of
Animal Science of Korea (2012-C-037) in Korea. After
4 h of feed withdrawal at 20 wk of age, chickens were
weighed individually, slaughtered by conventional neck
cuts, bled for 2 min, defeathered, and eviscerated. The
carcasses were vacuum-packed after chilling at 4°C for
24 h and stored in a freezer at −20°C until analysis.
Sample Preparation
Before analysis, the frozen carcasses were thawed in
a refrigerator at 4°C for 24 h. Breast and thigh muscles
were dissected from each thawed carcass. Right and left
breast and thigh muscles from each chicken were then
minced separately using a food mixer. Minced meat
samples were used for analysis.
Carnosine, Anserine, and Creatine Content
The contents of carnosine, anserine, and creatine
were determined using the method described by Mora
et al. (2007). Minced meat samples (2.5 g) from each
chicken were homogenized with 7.5 mL of 0.01 N HCl at
1,130 × g for 1 min [T25b, Ika Works (Asia), Rawang,
Malaysia]. The homogenate was centrifuged at 17,030
× g for 15 min at 4°C (HM-150IV, Hanil Co. Ltd., Inc-
hun, Korea), and the supernatant (250 µL) was mixed
with 750 µL of acetonitrile. After storage at 4°C for
20 min and centrifugation at 17,030 × g for 10 min at
4°C (HM-150IV, Hanil), the supernatant was injected
into an HPLC column equipped with a Waters 1525
pump and a Waters 717 plus autosampler (Millipore
Co-Operative, Milford, MA). An Atlantis HILIC silica
column (4.6 × 150 mm, 3 µm; Millipore) was used. A
diode array detector (Waters 2487; Millipore) was used
at 214 nm to measure creatine, carnosine, and anserine
contents. The mobile phase A contained 0.65 mM am-
monium acetate in a water-acetonitrile mix (25:75, vol/
vol, pH 5.5) and the phase B contained 4.55 mM am-
monium acetate in a water-acetonitrile mix (70:30, vol/
vol, pH 5.5). The mobile phase B was supplied at 1.2
mL/min for 16 min with a linear gradient (0–100%).
The content of compounds was calculated by using
standard curve of each compound. Standards (creatine,
anserine, and carnosine) were obtained from Sigma Co.
(St. Louis, MO).
IMP Content
Minced meat samples (5 g) of each chicken were
mixed with 25 mL of 0.7 M of perchloric acid and ho-
mogenized (T25b, Ika Works) at 1,130 × g for 1 min to
extract nucleic acids. The homogenate was centrifuged
(Union 32R) at 2,090 × g for 15 min at 4°C and filtered
through Whatman No. 4 filter paper (Whatman Inc.,
Maidstone, UK). The supernatant was then adjusted to
pH 7 with 5 N of KOH (SevenEasy, Mettler-Toledo Int.
Inc., Schwerzenbach, Switzerland). The supernatant
was placed in a volumetric flask and adjusted to a vol-
3276 JUNG ET AL.
ume of 100 mL with 0.7 M of perchloric acid (pH 7, ad-
justed with 5 N of KOH). After 30 min of cooling, the
mixture was centrifuged (Union 32R) at 2,090 × g (4°C)
and the supernatant was analyzed using HPLC (ACME
9000, Younglin Instruments Inc., Seoul, Korea). The
analytical conditions for HPLC included a Waters-At-
lantis dC18 RP column (4.6 × 250 mm, 5-µm particles;
Waters Co., Milford, MA), with a mobile phase of 0.1
M of triethylamine in 0.15 M of acetonitrile (pH 7.0)
with a flow rate at 1.0 mL/min. The injection volume
was 10 µL and elution time was 25 min. The column
temperature was maintained at 35°C and detection was
monitored at a wavelength of 260 nm. The content of
IMP was calculated using a standard curve. Standard
of IMP was obtained from Sigma.
Statistical Analysis
All data were analyzed by multifactorial ANOVA us-
ing the general linear model to confirm the effect of
meat type (breast and thigh), sex (male and female),
and line (5 lines of KNC). After grouping the data by
each meat type with each sex, the data were analyzed
by one-way ANOVA using the general linear model to
confirm the line effect in each meat type with each sex,
and the sex effect in each meat type with line. Tukey’s
multiple range test was used to compare significant dif-
ferences between mean values (P < 0.05). Mean values
and SEM are reported. Additionally, Pearson correla-
tion coefficients were calculated (P < 0.05). For all sta-
tistical analyses, SAS software (version 9.3, SAS Insti-
tute Inc., Cary, NC) was used.
RESULTS AND DISCUSSION
BW
The mean value of BW at preslaughter of chickens
from lines B, G, R, W, and Y of KNC are presented in
Table 1. Male chickens from line B and R had signifi-
cantly higher BW than did those from line G, W, or
Y. The lowest BW among male chickens was recorded
for line G (P < 0.05). In female chickens, line B had a
significantly higher BW than did line G, W, or Y (P <
0.05). Lines G and W showed significantly lower BW
than did lines B, R, and Y.
Histidine Dipeptide Content in Breast
and Thigh Meats
The carnosine content of meat from KNC is presented
in Table 2. The male breast meat from line W exhibited
significantly higher carnosine content than did those
from line G. However, no significant difference between
carnosine content in female breast meat among the 5
lines of KNC was observed. In thigh meat, lines B,
R, and W had significantly higher carnosine contents
than did lines G and Y in male chicken, and line R
showed much higher carnosine content than did lines
G, W, and Y in female chicken (P < 0.05). This result
is similar to the results of a previous study that showed
varying carnosine contents between breeds of Thai in-
digenous and hybrid native chickens (Intarapichet and
Maikhunthod, 2005). The 5 lines of KNC had different
BW, and BW was positively correlated with carnosine
content in meat, except male breast meat. However, the
effect of the line on carnosine content of meat was still
demonstrated when BW was set as a covariate (data
not shown). Based on this analysis, carnosine content
of meat is influenced by not only the weight of the
chicken, but also other genotypic traits that could be
different among lines, such as enzymes and transport-
ers. Carnosine is composed of β-alanine and -histidine
and is produced by carnosine synthase (Stenesh and
Winnick, 1960). Among regulation factors involved in
skeletal muscle carnosine synthesis, β-alanine availabil-
ity is the major rate-limiting factor, and the levels of
β-alanine are influenced by various related transporters
and enzymes (Everaert et al., 2013). Therefore, it is
important to identify the biological basis to understand
differences in carnosine content among the 5 lines of
KNC.
A previous study showed that breast and thigh meat
of female individuals contained higher carnosine con-
tent than did breast and thigh meat of male individuals
with similar BW, which was thought to be due to the
old age of female chicken (Intarapichet and Maikhun-
thod, 2005). The results of our study agree with those
of the previous study. Female chicken of KNC showed
significantly higher carnosine content than did male
chicken in both breast and thigh meats, except for the
W line. However, the BW of the female chickens were
lower than those of the male chickens in KNC at the
same age. From previous studies, it seemed that the ef-
fect of sex on skeletal muscle carnosine content may dif-
fer depending on animal species. Peñafiel et al. (2004)
reported that carnosine content in the muscle of male
rats was higher than that in female rats and observed
a positive correlation between carnosine content and
testosterone. Mateescu et al. (2012) reported that the
carnosine content in bovine longissimus muscle was not
related to sex. Additionally, no significant effect of sex
on the carnosine content in the muscle of equines was
Table 1. Body weight of Korean native chicken breeds1
Line
Slaughter weight (g)
SEMMale Female
B 2,127a,x 1,647a,y 33.1
G 1,785c,x 1,308c,y 27.0
R 2,130a,x 1,564ab,y 26.6
W 1,893b,x 1,378c,y 30.0
Y 1,939b,x 1,489b,y 26.7
SEM 20.2 20.4
a–cDifferent letters among breeds differ significantly (P < 0.05).
x,yDifferent letters between sex differ significantly (P < 0.05).
1B = black, G = gray-brown, R = red-brown, W = white, and Y =
yellow-brown.
3277
CARNOSINE, ANSERINE, CREATINE, AND INOSINE 5 ′-MONOPHOSPHATE
noted (Marlin et al., 1989). In the present study, breast
meat contained higher amounts of carnosine than did
thigh meat, regardless of line or sex. Previous studies
indicated that breast meat contained a large amount of
carnosine when compared with thigh meat (Abe and
Okuma, 1995; Intarapichet and Maikhunthod, 2005).
This is due to the fact that there is a different com-
position of muscle fiber type I (slow-twitch oxidative
red fiber), IIA (fast-twitch oxidative-glycolytic white
fiber), and IIB (fast-twitch glycolytic white fiber) in
breast and thigh meat. Breast meat is predominantly
composed of type II muscle fibers, whereas thigh meat
is not (Jaturasitha et al., 2008). During exercise, type
IIA and IIB muscle fiber require large amounts of di-
peptides and histidine dipeptides as a physico-chemical
buffer against the protons produced through anaerobic
glycolysis in muscle, as compared with type I muscle
fibers, resulting in carnosine accumulation (Dunnett
and Harris, 1995). From the pooled data in the pres-
ent study, the carnosine content in meat from KNC
depended on meat type (breast and thigh meat), sex
(male and female), and line, in order of effectiveness.
Anserine is the predominant histidine dipeptide in
poultry meat, whereas carnosine is predominant in beef
and pork (Abe and Okuma, 1995). Anserine synthesis
is catalyzed by carnosine N-methyltransferase (Drozak
et al., 2013). The anserine content of meat from KNC
is shown in Table 3. Male breast meat contained sig-
nificantly higher amounts of anserine in lines W and Y
than in line R. In thigh meat, the male chicken from
line W showed significantly high anserine content com-
pared with that in lines B and R. No significant differ-
ence in anserine content was observed among the 5 lines
of female chicken for both breast and thigh meats. The
BW of the chicken was not correlated with anserine
content in meat from KNC.
The sex effect on the anserine content in meat was
inconsistent between breast and thigh meat. Female
thigh meat showed a significantly high anserine content
compared with male thigh meat, except for line W,
which coincides with the sex effect on carnosine content
in thigh meat. However, male breast meat exhibited
significantly higher anserine content than did female
breast meat in lines W and Y, and no significant dif-
Table 2. Carnosine content (mg/100 g) of breast and thigh meat from Korean native chicken breeds1
Item
Breast
SEM
Thigh
SEM Meat
type Sex LineMale Female Male Female
Line
B 155ab,y 173x8.1 85a,y 98ab,x 3.6
G 130b,y 169x7.3 66b,y 73c,x 2.1
R 153ab,y 183x6.4 92a,y 107a,x 3.4
W 159a177 7.4 81a85bc 3.1
Y 139ab,y 176x7.4 76b,y 93b,x 3.5
SEM 6.9 8.0 2.9 3.5
r/BW2NC30.17 0.24 0.25
P-value <0.0001 <0.0001 <0.0001
F-value 887.16 62.91 12.28
a–cDifferent letters among breeds differ significantly (P < 0.05).
x,yDifferent letters between sex differ significantly (P < 0.05).
1B = black, G = gray-brown, R = red-brown, W = white, and Y = yellow-brown.
2r/BW = correlation coefficient between carnosine content with BW at P < 0.05.
3NC = no correlation.
Table 3. Anserine content (mg/100 g) of breast and thigh meat from Korean native chicken breeds1
Item
Breast
SEM
Thigh
SEM Meat
type Sex LineMale Female Male Female
Line
B 880ab 834 21.2 321b,y 373x8.7
G 851ab 818 23.0 330ab,y 367x7.8
R 803b803 18.5 312b,y 343x7.6
W 921a,x 824y26.3 361a374 10.3
Y 914a,x 848y23.0 327ab,y 357x10.5
SEM 23.1 23.5 9.6 9.1
r/BW2NC3NC NC NC
P-value <0.0001 0.32 <0.0001
F-value 4,096.18 0.98 7.20
a,bDifferent letters among breeds differ significantly (P < 0.05).
x,yDifferent letters between sex differ significantly (P < 0.05).
1B = black, G = gray-brown, R = red-brown, W = white, and Y = yellow-brown.
2r/BW = correlation coefficient between anserine content with BW at P < 0.05.
3NC = no correlation.
3278 JUNG ET AL.
ference in anserine content was observed in the breast
meat between sex for lines B, G, and R. Anserine is the
methylated analog of carnosine. In the present study,
the correlation coefficient between anserine and carno-
sine content of meat was 0.67 (data not shown). How-
ever, the effects of line and sex on carnosine and anser-
ine content in breast or thigh meat did not completely
agree. In addition, the anserine content in meat was
not influenced by the BW of the chicken, whereas the
carnosine content in meat from the 5 lines of KNC was
affected by the BW of the chicken. The effect of meat
type on anserine content corresponded with that on
carnosine content. Breast meat contained high anserine
content compared with thigh meat. This is because of
the ability of anserine to act as a physico-chemical buf-
fer against proton production by anaerobic glycolysis
in breast muscle (Dunnett and Harris, 1995). Based
on our pooled data, the anserine content in meat from
KNC was influenced by meat type and line, in order of
effectiveness.
Creatine Content in Breast and Thigh Meats
Creatine [N-(aminoiminomethyl)-N-methyl-glycine] is
a nitrogenous organic acid synthesized from -arginine,
glycine, and -methionine (Schmid, 2009). Biosynthesis
of creatine principally consists of 2 phases. First, the
amidino group of arginine is transferred to glycine by
-arginine:glycine amidinotransferase (AGAT ), which
produces -ornithine and guanidinoacetic acid. Second,
methylation by S-adenosyl--methionine:N-guanidino-
acetate at the amidino group of guanidinoacetic acid
yields creatine. Biosynthesis of creatine takes place in
the kidney and liver, and, then, creatine is distributed
to skeletal muscles and other organs containing creatine
kinase, which catalyzes the generation of phosphoryl-
creatine from creatine (Wyss and Kaddurah-Daouk,
2000).
The creatine content in male breast meat was signifi-
cantly higher in lines W and Y than in lines G and R
(Table 4). The female breast meat showed no signifi-
cant difference in creatine content among the 5 lines of
KNC. Thigh meat showed high creatine content in line
W compared with that in line G for the male chicken
and in lines B, W, and Y compared with that in line G
for the female chicken (P < 0.05). The creatine content
of breast meat from both male and female KNC was
not related to the chicken BW. However, the creatine
content of thigh meat was correlated with chicken BW
in both male and female chickens. When BW was set as
the covariate, an effect of line on creatine content was
observed for male thigh meat, whereas the effect was
not observed for female thigh meat (P = 0.061) of KNC
(data not shown).
Sex hormone is known to influence creatine synthe-
tase activity. Zhu and Evans (2001) found that estrogen
treatment transiently upregulated AGAT, but long-
term estrogen exposure downregulated AGAT in chick
liver. In contrast, Lee et al. (1994) reported that female
mouse liver showed higher S-adenosyl--methionine:N-
guanidinoacetate expression than male mouse liver did.
In the present study, female thigh meat in lines B, G,
R, and Y had significantly higher creatine content than
did male thigh meat. However, the sex effect was in-
consistent. The creatine content in breast meat from
KNC was not significantly different between male and
female chicken, except for line W, in which the male
breast meat had significantly higher creatine content
than female breast meat.
The route of energy supply (adenosine triphosphate,
ATP) to do work using muscle differs depending on
the muscle fiber type. Type I muscle fibers are mito-
chondria rich and supplied with ATP, which is stable
and long-lasting as it is produced through oxidative
metabolism. Type II muscle fibers contain fewer mito-
chondria than type I muscle fibers do, with ATP main-
ly supplied by glycolytic metabolism, which is fast and
intense (Booth and Thomason, 1991). Thus, a large
amount of phosphorylcreatine is required for immediate
regeneration of ATP in type II muscle fibers (Wyss and
Table 4. Creatine content (mg/100 g) of breast and thigh meat from Korean native chicken breeds1
Item
Breast
SEM
Thigh
SEM Meat
type Sex LineMale Female Male Female
Line
B 417ab 409 6.7 401ab,y 431a,x 5.1
G 395bc 394 7.3 382b,y 404b,x 5.1
R 387c399 5.7 392ab,y 414ab,x 5.5
W 430a,x 402y8.1 415a412ab 6.8
Y 427a412 7.6 406ab,y 425a,x 6.7
SEM 7.3 7.5 6.4 5.8
r/BW2NC3NC 0.18 0.13
P-value 0.74 0.10 <0.0001
F-value 0.11 2.70 10.73
a–cDifferent letters among breeds differ significantly (P < 0.05).
x,yDifferent letters between sex differ significantly (P < 0.05).
1B = black, G = gray-brown, R = red-brown, W = white, and Y = yellow-brown.
2r/BW = correlation coefficient between creatine content with BW at P < 0.05.
3NC = no correlation.
3279
CARNOSINE, ANSERINE, CREATINE, AND INOSINE 5 ′-MONOPHOSPHATE
Kaddurah-Daouk, 2000). A previous study showed high
phosphorylcreatine content in type II muscle fiber com-
pared with type I muscle fiber of rodents, but showed
that creatine contents between type I and II muscle fi-
ber did not differ (Kushmerick et al., 1992). This result
is similar to the results of the present study. Breast and
thigh meat from KNC showed no significant differences
in creatine content, although the composition of muscle
fiber type between breast and thigh meat of chicken
could be distinguished.
Creatine content in skeletal muscle can be increased
by creatine supplementation. Additionally, the high
creatine content of meat may indicate a high nutri-
tional quality because it is a good creatine source for
consumers (Williams and Branch, 1998). However, con-
troversial results regarding creatine supplementation
and meat quality have been reported. Berg and Allee
(2001) suggested that the dietary creatine monohydrate
for 10 d restrained the decline of early postmortem (45
min) and ultimate pH (24 h) in the semimembranosus
of pork, but had no influence on the quality of loin
muscle. In contrast, dietary creatine reduced postmor-
tem pH (4 h) and, consequently, increased drip loss in
pectoralis major muscle of chicken (Young et al., 2004).
However, the creatine content in breast or thigh meat
was not correlated with early postmortem (15 min) and
ultimate pH (24 h) of breast or thigh meat in the pres-
ent study (data not shown).
IMP Content in Breast and Thigh Meats
The IMP content in meat from KNC is presented in
Table 5. Male breast meat in lines R, W, and Y had
significantly higher IMP content than did that in line
B. The IMP content of female breast meat was highest
in line Y compared with those in other lines (P < 0.05).
The line effect on IMP content in male thigh meat cor-
responded to that in male breast meat. In female thigh
meat, line R contained significantly more IMP than did
line W (P < 0.05). For both meat types in male and fe-
male chickens, the IMP content was slightly correlated
with BW. However, the effect of line on IMP content
remained when BW was set as a covariate (data not
shown). Inosine 5 ′-monophosphate is a purine nucle-
otide-breakdown product. During skeletal muscle con-
tractions, IMP accumulates in skeletal muscle when the
hydrolysis rate of ATP exceeds the phosphorylation rate
of adenosine diphosphate (Tullson and Terjung, 1999).
Additionally, accumulation of IMP occurs when muscles
are used as meat after slaughter because ATP degrades
rapidly to adenosine monophosphate, which then un-
dergoes enzymatic reaction by deaminase (Surette et
al., 1988). Previous studies have reported different
IMP contents among different genotypes. Jung et al.
(2011) reported that thigh meat from the commercial
meat-type native chicken line in South Korea contained
much more IMP than did broiler (Ross) at a similar
body weight. Additionally, Tang et al. (2009) reported
different IMP content between slow- and fast-growing
genotype chickens. Regarding the effect of genotype
on IMP content, the adenylosuccinatelyase gene and
glycinamide ribonucleotide synthetase-aminoimidazole
ribonucleotide synthetase-glycinamide ribonucleotide
transformylase gene have been suggested to determine
the IMP content of chicken meat (Li et al., 2010). Vani
et al. (2006) reported that the degradation rate of IMP
was greater at acidic pH than at neutral or alkaline
pH. However, a correlation between the IMP content of
meat and early or ultimate pH of meat was not observed
(data not shown). Vani et al. (2006) also reported that
breast meat contained more IMP than leg meat. This
result agrees with the results of the present study; IMP
content in breast meat was higher than that in thigh
meat from KNC. This difference may be attributed to
the different composition of muscle fiber types between
breast and thigh meats (Jaturasitha et al., 2008). Type
II muscle fiber exhibits high accumulation of IMP com-
pared with type I muscle fiber in rat skeletal muscle
(Arabadjis et al., 1993). In addition, the activity of 5
′-nucleotidase, which catalyzed the degradation of IMP
to inosine, was higher in type I muscle fiber than in
type II muscle fiber in rat skeletal muscle (Tullson and
Terjung, 1999). In the present study, an effect of sex on
IMP content was observed. The IMP content in female
breast meat was higher than that in male breast meat
for lines G and Y (P < 0.05). Except for line W, female
thigh meat showed higher IMP content than male thigh
meat (P < 0.05). Jiang et al. (2003) reported that IMP
content was higher in gilt than in barrow. However, the
effect of sex on IMP content in chicken meat has not
been reported. Based on our data, the IMP content in
meat from KNC was influenced by meat type, sex, and
line, in order of effectiveness.
The results from the present study reveal the effect
of line on the content of endogenous compounds, such
as carnosine, anserine, creatine, and IMP, in chicken
meat. In addition, our results show the influence of sex
and meat type on the content of these compounds in
chicken meat. Few studies examining the factors that
influence carnosine, anserine, and creatine content in
chicken meat have been performed, although carnosine,
anserine, and creatine in meat are important because of
their functionality. Therefore, the results of the present
study are valuable for poultry science.
Mateescu et al. (2012) found that the heritability
for carnosine, anserine, and creatine in the longissimus
muscle of beef was 0.383, 0.531, and 0.434, respectively.
Although the heritability of carnosine, anserine, and
creatine in chicken has not been studied, a trend may
exist in chicken. For IMP, high heritability (0.51–0.69)
was reported in chicken (Chen et al., 2002). The ex-
istence of heritability of compounds in meat implies
that compound content can be manipulated through
selection. Therefore, we conclude that these data will
provide useful information for selection in developing a
high-quality, meat-type chicken breed. However, com-
3280 JUNG ET AL.
parison analysis between endogenous compounds and
the genotype of each line is necessary to completely
understand the differences among the 5 lines of KNC.
ACKNOWLEDGMENTS
This work was supported by a grant from the Next-
Generation BioGreen 21 Program (no. PJ0081330),
Rural Development Administration, Republic of Korea.
REFERENCES
Abe, H., and E. Okuma. 1995. Discrimination of meat species in pro-
cessed meat-products based on the ratio of histidine dipeptides.
J. Jpn. Soc. Food Sci. 42:827–834.
Adhihetty, P. J., and M. F. Beal. 2008. Creatine and its potential
therapeutic value for targeting cellular energy impairment in
neurodegenerative diseases. Neuromolecular Med. 10:275–290.
Arabadjis, P. G., P. C. Tullson, and R. L. Terjung. 1993. Purine
nucleoside formation in rat skeletal-muscle fiber types. Am. J.
Physiol. 264:C1246–C1251.
Baguet, A., K. Koppo, A. Pottier, and W. Derave. 2010. Beta-al-
anine supplementation reduces acidosis but not oxygen uptake
response during high-intensity cycling exercise. Eur. J. Appl.
Physiol. 108:495–503.
Bellia, F., G. Vecchio, S. Cuzzocrea, V. Calabrese, and E. Rizzarelli.
2011. Neuroprotective features of carnosine in oxidative driven
diseases. Mol. Aspects Med. 32:258–266.
Berg, E. P., and G. L. Allee. 2001. Creatine monohydrate supple-
mented in swine finishing diets and fresh pork quality: I. A con-
trolled laboratory experiment. J. Anim. Sci. 79:3075–3080.
Booth, F. W., and D. B. Thomason. 1991. Molecular and cellular
adaptation of muscle in response to exercise: Perspectives of vari-
ous models. Physiol. Rev. 71:541–585.
Chan, K. M., and E. A. Decker. 1994. Endogenous skeletal-muscle
antioxidants. Crit. Rev. Food Sci. Nutr. 34:403–426.
Chen, G. H., H. F. Li, X. S. Wu, B. C. Li, K. Z. Xie, G. J. Dai, K.
W. Chen, X. Y. Zhang, and K. H. Wang. 2002. Factors affecting
the inosine monophosphate content of muscles in Taihe Silkies
chickens. Asian-australas. J. Anim. Sci. 15:1359–1363.
Drozak, J., L. Chrobok, O. Poleszak, A. K. Jagielski, and R. Derlacz.
2013. Molecular identification of carnosine -methyltransferase
as chicken histamine -methyltransferase-like protein (HNMT-
like). PLoS ONE 8:e64805.
Dunnett, M., and R. C. Harris. 1995. Carnosine and taurine con-
tents of type I, IIA, and IIB fibres in the middle gluteal muscle.
Equine Vet. J. 27:214–217.
Everaert, I., H. De Naeyer, Y. Taes, and W. Derave. 2013. Gene ex-
pression of carnosine-related enzymes and transporters in skeletal
muscle. Eur. J. Appl. Physiol. 113:1169–1179.
Fanatico, A. C., P. B. Pillai, J. L. Emmert, and C. M. Owens. 2007.
Meat quality of slow- and fast-growing chicken genotypes fed low
nutrient or standard diets and raised indoors or with outdoor ac-
cess. Poult. Sci. 86:2245–2255.
Gotshalk, L. A., J. S. Volek, R. S. Staron, C. R. Denegar, F. C.
Hagerman, and W. J. Kraemer. 2002. Creatine supplementation
improves muscular performance in older men. Med. Sci. Sports
Exerc. 34:537–543.
Hipkiss, A. R. 2009. Carnosine, diabetes and Alzheimer’s disease.
Expert Rev. Neurother. 9:583–585.
Intarapichet, K. O., and B. Maikhunthod. 2005. Genotype and gen-
der differences in carnosine extracts and antioxidant activities of
chicken breast and thigh meats. Meat Sci. 71:634–642.
Jaturasitha, S., T. Srikanchai, M. Kreuzer, and M. Wicke. 2008.
Differences in carcass and meat characteristics between chicken
indigenous to northern Thailand (Black-Boned and Thai native)
and imported extensive breeds (Bresse and Rhode Island Red).
Poult. Sci. 87:160–169.
Jiang, X. P., G. Q. Liu, Y. Z. Xiong, J. T. Ding, K. Z. Xie, J. Q.
Zhang, and B. Zuo. 2003. Phenotypic and genetic parameters for
inosine acid in relation to carcass and meat quality traits in pigs.
Asian -australas. J. Anim. Sci. 16:257–260.
Jung, Y., H. J. Jeon, S. Jung, J. H. Choe, J. H. Lee, K. N. Heo, B.
S. Kang, and C. Jo. 2011. Comparison of quality traits of thigh
meat from Korean native chickens and broilers. Korean J. Food
Sci. Anim. Resour. 31:684–692.
Kawahara, M., K. Konoha, T. Nagata, and Y. Sadakane. 2007. Pro-
tective substances against zinc-induced neuronal death after isch-
emia: Carnosine as a target for drug of vascular type of dementia.
Recent Pat. CNS Drug Discov. 2:145–149.
Kawai, M., A. Okiyama, and Y. Ueda. 2002. Taste enhancements be-
tween various amino acids and IMP. Chem. Senses 27:739–745.
Koutsidis, G., J. S. Elmore, M. J. Oruna-Concha, M. M. Campo, J.
D. Wood, and D. S. Mottram. 2008. Water-soluble precursors of
beef flavour. Part II: Effect of post-mortem conditioning. Meat
Sci. 79:270–277.
Kushmerick, M. J., T. S. Moerland, and R. W. Wiseman. 1992.
Mammalian skeletal-muscle fibers distinguished by contents of
phosphocreatine, ATP, and Pi. Proc. Natl. Acad. Sci. USA
89:7521–7525.
Lee, H., H. Ogawa, M. Fujioka, and G. L. Gerton. 1994. Guanidino-
acetate methyltransferase in the mouse—Extensive expression in
Sertoli cells of testis and in microvilli of caput epididymis. Biol.
Reprod. 50:152–162.
Li, H. F., W. Han, J. T. Shy, Y. F. Zhu, X. Y. Zhang, and K. W.
Chen. 2010. Improving muscle inosine monophosphate (IMP)
contents in Wenchang chicken by pyramiding favorable genotypes
of ADSL and GARS-AIRS-GART genes. J. Anim. Vet. Adv.
9:1791–1795.
Table 5. Inosine-5 ′-phosphate content (mg/100 g) of breast and thigh meat from Korean native chicken breeds1
Item
Breast
SEM
Thigh
SEM Meat
type Sex LineMale Female Male Female
Line
B 246b261b7.2 135b,y 162ab,x 4.9
G 253ab,y 264b,x 3.9 145ab,y 156ab,x 3.7
R 256ab 267b4.6 153a,y 168a,x 3.4
W 262ab 266b4.8 148a153b4.5
Y 268a,y 288a,x 4.3 151a,y 165ab,x 3.8
SEM 4.7 5.2 4.0 3.8
r/BW20.16 0.13 0.18 0.12
P-value <0.0001 <0.0001 <0.0001
F-value 2,951.74 42.29 9.86
a,bDifferent letters among breeds differ significantly (P < 0.05).
x,yDifferent letters between sex differ significantly (P < 0.05).
1B = black, G = gray-brown, R = red-brown, W = white, and Y = yellow-brown.
2r/BW = correlation coefficient between inosine-5 ′-phosphate content with BW at P < 0.05.
3281
CARNOSINE, ANSERINE, CREATINE, AND INOSINE 5 ′-MONOPHOSPHATE
Marlin, D. J., R. C. Harris, S. P. Gash, and D. H. Snow. 1989.
Carnosine content of the middle gluteal muscle in thoroughbred
horses with relation to age, sex and training. Comp. Biochem.
Physiol. A 93:629–632.
Mateescu, R. G., A. J. Garmyn, M. A. O’Neil, R. G. Tait, A. Abu-
zaid, M. S. Mayes, D. J. Garrick, A. L. Van Eenennaam, D. L.
VanOverbeke, G. G. Hilton, D. C. Beitz, and J. M. Reecy. 2012.
Genetic parameters for carnitine, creatine, creatinine, carnosine,
and anserine concentration in longissimus muscle and their as-
sociation with palatability traits in Angus cattle. J. Anim. Sci.
90:4248–4255.
Mora, L., M. A. Sentandreu, and F. Toldra. 2007. Hydrophilic chro-
matographic determination of carnosine, anserine, balenine, cre-
atine, and creatinine. J. Agric. Food Chem. 55:4664–4669.
Nagai, H., M. Harada, M. Nakagawa, T. Tanaka, B. Gunadi, M.
L. Setiabudi, J. L. Uktolseja, and Y. Miyata. 1996. Effects of
chicken extract on the recovery from fatigue caused by mental
workload. Appl. Human Sci. 15:281–286.
Park, H. B., D. W. Seo, N. R. Choi, J. S. Choi, K. N. Heo, B. S.
Kang, C. Jo, and J. H. Lee. 2012. Estimation of genetic param-
eters for serum clinical-chemical traits in Korean native chickens.
Korean J. Poult. Sci. 39:279–282.
Peñafiel, R., C. Ruzafa, F. Monserrat, and A. Cremades. 2004. Gen-
der-related differences in carnosine, anserine and lysine content
of murine skeletal muscle. Amino Acids 26:53–58.
Quinn, P. J., A. A. Boldyrev, and V. E. Formazuyk. 1992. Carno-
sine—Its properties, functions and potential therapeutic applica-
tions. Mol. Aspects Med. 13:379–444.
Schmid, A. 2009. Bioactive substances in meat and meat products.
Fleischwirtschaft 89:83–90.
Stenesh, J. J., and T. Winnick. 1960. Carnosine-anserine synthetase
of muscle. Biochem. J. 77:575–581.
Surette, M. E., T. A. Gill, and P. J. Leblanc. 1988. Biochemical ba-
sis of postmortem nucleotide catabolism in cod (Gadus-Morhua)
and its relationship to spoilage. J. Agric. Food Chem. 36:19–22.
Tallon, M. J., R. C. Harris, N. Maffulli, and M. A. Tarnopolsky.
2007. Carnosine, taurine and enzyme activities of human skeletal
muscle fibres from elderly subjects with osteoarthritis and young
moderately active subjects. Biogerontology 8:129–137.
Tang, H., Y. Z. Gong, C. X. Wu, J. Jiang, Y. Wang, and K. Li. 2009.
Variation of meat quality traits among five genotypes of chicken.
Poult. Sci. 88:2212–2218.
Tullson, P. C., and R. L. Terjung. 1999. IMP degradative capacity in
rat skeletal muscle fiber types. Mol. Cell. Biochem. 199:111–117.
Vani, N. D., V. K. Modi, S. Kavitha, N. M. Sachindra, and N. S.
Mahendrakar. 2006. Degradation of inosine-5 ′-monophosphate
(IMP) in aqueous and in layering chicken muscle fibre systems:
Effect of pH and temperature. LWT-Food Sci. Technol. 39:627–
632.
Volek, J. S., and E. S. Rawson. 2004. Scientific basis and practi-
cal aspects of creatine supplementation for athletes. Nutrition
20:609–614.
Williams, M. H., and J. D. Branch. 1998. Creatine supplementa-
tion and exercise performance: An update. J. Am. Coll. Nutr.
17:216–234.
Wyss, M., and R. Kaddurah-Daouk. 2000. Creatine and creatinine
metabolism. Physiol. Rev. 80:1107–1213.
Young, J. F., A. H. Karlsson, and P. Henckel. 2004. Water-holding
capacity in chicken breast muscle is enhanced by pyruvate and
reduced by creatine supplements. Poult. Sci. 83:400–405.
Zhu, Y., and M. I. Evans. 2001. Estrogen modulates the expression
of -arginine: Glycine amidinotransferase in chick liver. Mol.
Cell. Biochem. 221:139–145.
3282 JUNG ET AL.