ARTICLE

Taste-Active and Nutritional Components of Thai Native Chicken Meat: A Perspective of Consumer Satisfaction

Phatthawin Lengkidworraphiphat1https://orcid.org/0000-0002-4458-5106, Rawiwan Wongpoomchai2https://orcid.org/0000-0001-6999-8436, Thanaporn Bunmee3https://orcid.org/0000-0001-8117-0690, Arpamas Chariyakornkul2https://orcid.org/0000-0002-0463-2289, Niraporn Chaiwang4https://orcid.org/0000-0001-8220-7256, Sanchai Jaturasitha1,5,*https://orcid.org/0000-0003-0762-3748
Author Information & Copyright
1Department of Animal and Aquatic Sciences, Faculty of Agriculture, Chiang Mai University, Chiang Mai 50200, Thailand
2Department of Biochemistry, Faculty of Medicine, Chiang Mai University, Chiang Mai 50200, Thailand
3Division of Animal Sciences, School of Agriculture and Natural Resources, University of Phayao, Phayao 56000, Thailand
4Department of Agricultural Technology and Development, Faculty of Agricultural Technology, Chiang Mai Rajabhat University, Chiang Mai 50300, Thailand
5Science and Technology Research Institute, Chiang Mai University, Chiang Mai 50200, Thailand
*Corresponding author : Sanchai Jaturasitha, Department of Animal and Aquatic Sciences, Faculty of Agriculture, Chiang Mai University, Chiang Mai 50200, Thailand, Tel: +66-53-221667 (ext 123), Fax: +66-53-357601, E-mail: ja.sanchai@gmail.com

© Korean Society for Food Science of Animal Resources. This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Received: Jul 17, 2020 ; Revised: Nov 08, 2020 ; Accepted: Nov 18, 2020

Published Online: Mar 01, 2021

Abstract

The taste-active and nutritional components of Thai native, broilers, black-boned, and spent hen chickens were analyzed. The amounts of tasty amino acids especially glutamic acid were the highest in Thai native chicken. The black-boned chicken had the highest arginine content, related to the least amount of consumer satisfaction. Concerning nutritional quality, choline, and taurine were deemed important for brain function. The black-boned chicken showed the highest choline and taurine contents, unlike that of the spent hens. In contrast, broilers presented the highest betaine content, which might be attributed to their lipid metabolism. L-carnitine content was abundant in black-boned and Thai native chickens. Moreover, the amounts of essential amino acids were high in Thai native chicken. In conclusion, black-boned chicken proved to be an excellent nutritional source for health-conscience consumers, whereas the Thai native chickens were flavourful and delicious.

Keywords: bioactive compounds; free amino acid; taste-active components; nutritional components; Thai native chickens

Introduction

White meat, such as chicken and pork, are considered superior to red meat in terms of human health, due to their comparably lower fat and higher protein contents. Consumer perceptions, as well as the associated lower prices, convenience, and lack of religious restrictions further aid in their popularity and consumption (Jaturasitha et al., 2008). Nutritional value and meat quality are influenced by several factors; such as age, body weight, growth performance, and environmental conditions (Jung et al., 2011). Chicken meat also contains numerous endogenous bioactive compounds, which, in routine dietary inclusion, can reduce the incidence of many diseases and provide several health benefits (Jayasena et al., 2013).

The bioactive compound; such as choline, betaine, L-carnitine, creatine, and taurine are essential nutrients related to brain development, the metabolism of fatty acids, osmoregulatory properties, supply energy to muscles, and for the regulation of the central nervous system (De Zwart et al., 2003; Flanagan et al., 2010; Li et al., 2015; Mora et al., 2010; Wu and Shiau, 2002; Wyss and Kaddurah-Daouk, 2000) and have been shown to possess health-promoting characteristics. Free amino acids (FAAs) contribute to the taste of many foods (Zhao et al., 2016). Additionally, glutamic acid, a savory amino acid, is well known for its umami taste, and is one of the most important amino acids in chicken meat (Ali et al., 2019).

Several studies have shown that Korean indigenous chickens possess higher amounts of bioactive compounds than commercial broiler chickens, which are affected by genotype, muscle fiber, meat portion, gender, age, and cooking method (Ahn and Park, 2002; Jayasena et al., 2014; Jayasena et al., 2015; Jung et al., 2013). Similarly, the meat from Japanese native chickens is considered more palatable than that of typical broiler chickens, due to its high nutritional value (Rikimaru and Takahashi, 2010). In Thailand, four main commercial chicken are raised: broiler; spent hen; black-boned chicken; and the Thai native chicken. Broilers, which are generally imported, have high growth performance and a low cost of production and have become a staple meat-product in Thai markets. Spent hen, another potential source of chicken meat, is discharged at the age of 80 to 100 wk. The texture of spent hen is tough due to the accumulation of collagen (Chuaynukool et al., 2007); however, spent hen chickens are occasionally fattened in Thailand to complement indigenous chickens in times of high demand for meat of indigenous origin (Jaturasitha et al., 2008). The black-boned chicken and Thai native chicken, which are indigenous strains, have slow growth rates, which limit their production. While some Thai consumers prefer the taste of meat from native chickens; the market is small, although gaining in popularity (Wattanachant et al., 2005). Raised in rural and mountainous areas of Thailand, black-bone chickens have other special properties and their skin, bones, and meat are black (Tu et al., 2009), which accounts for their notable consumer demand (Jaturasitha et al., 2008).

Numerous studies of chicken meat in Thailand have focused on growth performance, carcass quality, and meat quality; including our former study on the macronutrient composition and antioxidant capacities of chicken breast meat. While the findings showed that the chemical composition, amounts of protein, and the antioxidant biomarkers, including carnosine and anserine, were affected by genotype; little information has been provided on the nutritional properties and bioactive compounds of different chicken breeds. The objective of the present study was to compare the unique taste, nutritional properties and endogenous bioactive compounds across four chicken genotypes: commercial broiler; spent hen; black-boned; and Thai native. We intend that the results may be used to identify which genotypes would be most suitable to certain situations, resulting in the promotion of meat production, as well as influencing consumer consumption.

Materials and Methods

Sample preparation

Each of the four genotypes of chicken in this study; broiler, spent hen, Thai native, and black-boned, were reared in one flock on a single farm under identical conditions. The chickens were fed formulated diets obtained from a commercial feed, according to their genetic requirements. Feed and water were provided for ad libitum intake. The broilers were fed until they were six weeks old; whereas spent hen, black-boned chicken, and Thai native chicken were fed until they were 72 wk old, 20 wk old, and 16 wk old; respectively. The average live weights of each chicken genotype were 2.1±0.2 kg (broiler), 1.7±0.1 kg (spent hen), 1.2±0.1 kg (black-boned), and 1.3±0.1 kg (Thai native). At the end of the experiment, ten chickens of each genotype were slaughtered using standard methods. Their carcasses were chilled at 4°C for 24 h, and the breast meat without fat was immediately separated. The breast meat was then minced with a meat grinder, immediately cooled in an ice bath, and stored at –20°C before freeze-drying. Freeze-dried meat samples were ground to powder using a mortar and pestle and stored at –20°C before analyses.

Free amino acid and taurine analysis

The FAA and taurine contents were measured according to the method of Bidlingmeyer et al. (1984) with some modifications. Each sample was mixed with 10 mM hydrochloric acid (HCl) and acetonitrile (ACN). The homogenate was centrifuged at 10,000×g for 10 min at 4°C (TOMY MX-301, Tokyo, Japan). The supernatant was neutralized by adding a mixture of methanol (MeOH)/water/triethylamine (TEA) (2:2:1, v/v); then dried completely in a vacuum. Then, the samples were dissolved with a mixture of MeOH/water/TEA/phenyl isothiocyanate (PITC) (7:1:1:1, v/v) for derivatization and incubated for 20 min for phenylthiocarbamyl amino acid production. The mixtures were then filtered through a 0.45 μm PVDF syringe filter (Whatman International, Maidstone, UK). Phenylthiocarbamyl amino acids and taurine were separated using an HPLC system with an L-column3 C18, 5 μm particle size (250×4 mm; Nacalai Tesque, Kyoto, Japan). A binary linear gradient was used with 100% ACN as mobile Phase A, and 150 mM ammonium acetate, pH 6.2 containing 5% ACN as mobile Phase B at a flow rate of 0.6 mL/min. The column temperature was maintained at 40°C. The gradient program was as follows: 0–3 min, 0%–6% B; 3–20 min, 6%–22% B; 20–25 min, 22%–60% B; 26–37.1 min, 100%–0% B; 37.1–50 min, 0% B. The separation was monitored using a diode array detector at wavelengths of 214 and 254 nm.

Total amino acid analysis

The total amino acid contents of the samples were determined by the method outlined by Bidlingmeyer et al. (1984) with slight modifications. The samples were digested with 6 N HCl at 150°C for 1 h. The resultant amino acids were derivatized with PITC, and the PTC-amino acids were resolved using the same method as that for the FAAs.

Betaine, carnitine, creatine, and choline analysis

The betaine, carnitine, creatine, and choline contents were determined through liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-MS/MS, LCMS 8040; Shimadzu, Kyoto, Japan). The standards and samples were dissolved in distilled water and centrifuged at 10,000×g for 20 min. The supernatant was then mixed with ethanol and filtered. An Inertsil ODS-3 column (2 mm inner diameter×250 mm; GL Science, Tokyo, Japan) was used for the LC separation. The column temperature was controlled at 40°C. The mobile Phase A contained 0.1% formic acid, and B contained 0.1% formic acid in 80% ACN. The gradient program used was as follows: 0–10.01 min, 100% B; 10.01–15.01 min, 100% B; and 15.01–25 min, 0% B. The flow rate of the mobile phase was 0.2 mL/min. The total ion intensity was monitored in a positive mode. Several scan modes, including a precursor ion scan, product ion scan, and multiple reaction monitoring were used to quantify the betaine L-carnitine, creatine, and choline contents.

Statistical analysis

All experiments were carried out as mean±SD of three independent measurements and were subjected to One-way Analysis of Variance (ANOVA), and the significance of mean differences was determined by the Duncan Multiple Range test using SPSS version 23.0 (SPSS Inc., Chicago, IL, USA), in which p-value less than 0.05 were considered significant.

Results and Discussion

Amino acid contribution to the taste-active compound

FAAs have long been associated with the characteristic tastes of food (Wu and Shiau, 2002). The FAA concentrations of breast meat in broiler, spent hen, black-boned, and Thai native chickens are presented in Table 1. For essential amino acids, the dominant FAAs of all genotypes were leucine and valine, whereas threonine was found in higher amounts in broiler and black-boned chickens (p<0.05). Alanine, a non-essential amino acid, was greatest in all genotype contents (p<0.05). Alanine was the predominant non-essential amino acid in chicken fillets (Ali et al., 2019). Furthermore, asparagine showed the lowest content in broilers, whereas the highest content was found in the spent hen, Thai native, and black-boned chickens (p<0.05). Glutamic acid is one of the most important amino acids in chickens, which enhances the palatability of chicken meat (Rikimaru and Takahashi, 2010). In the present study, glutamic acid content was the highest in Thai native chickens, followed by black-boned, broiler, and spent hen chickens (p<0.05). These results agree with the study of Wattanachant et al. (2004) which indicated that the glutamic acid contents in native chickens were higher than those in broilers. Asparagine, threonine, serine, glutamic acid, glycine, and alanine have been classified as tasty amino acids (Ali et al., 2019), which were most prevalent in Thai native, broiler, black-boned, and spent hen chickens, respectively (Fig. 1). Flavor-related amino acids (valine, isoleucine, leucine, phenylalanine, arginine, proline, and methionine) are related to the tangy flavor in meat (Ali et al., 2019; Meinert et al., 2009). These flavor-related amino acids were found to be highest in content in black-boned chicken, and lowest in Thai natives and broilers (Fig. 1). Arginine, which is associated with an undesirable flavor complexity (Schiffman and Dackis, 1975), was highest in the black-boned chicken. This suggests that different genetic variants of chickens may be associated with different free-amino acids. According to Mir et al. (2017) indigenous chickens are higher in flavor and taste compounds than broilers, due to variations in their content of amino acids; including aspartic acid, threonine, serine, glycine, alanine, tyrosine, lysine, and arginine.

Table 1. Amino acid (% of total amino acids) contribution to the taste-active compounds of breast meat from four chicken genotypes
Item Broiler Spent hen Black-boned Thai native
Alanine 16.2±0.09b 13.1±0.19d 13.5±0.05c 18.6±0.48a
Arginine 0.47±0.03c 1.28±0.13b 1.61±0.09a 1.21±0.08b
Asparagine 1.77±0.02d 4.15±0.08a 1.91±0.01c 3.23±0.12b
Aspartic acid 4.82±0.06a 2.28±0.03d 4.51±0.03b 3.75±0.03c
Glutamic acid 9.63±0.10b 5.55±0.42c 10.3±0.10b 14.4±1.39a
Glutamine 6.89±0.06d 12.3±0.02a 7.25±0.02c 9.02±0.26b
Glycine 9.55±0.03b 10.56±0.04a 8.90±0.04c 10.5±0.19a
Histidine 2.89±0.03b 4.72±0.03a 2.71±0.01b 2.03±0.20c
Isoleucine 3.39±0.18b 4.10±0.10a 3.54±0.01b 2.74±0.09c
Leucine 6.39±0.37b 6.98±0.08a 7.32±0.21a 5.67±0.10c
Lysine 5.59±0.02a 4.07±0.07b 5.13±0.02a 2.90±0.58c
Methionine 2.41±0.01c 3.16±0.03a 2.43±0.02c 2.67±0.02b
Phenylalanine 2.95±0.03b 2.63±0.01c 3.47±0.02a 2.73±0.30bc
Proline 3.67±0.02a 2.93±0.04b 3.73±0.02a 3.80±0.34a
Serine 8.90±0.06c 9.84±0.04a 8.98±0.03b 7.62±0.17a
Threonine 6.15±0.04b 2.27±0.26c 6.61±0.41a 1.15±0.22d
Tyrosine 3.26±0.04b 3.65±0.09a 1.88±0.01d 2.96±0.10c
Valine 5.05±0.10c 6.40±0.09a 6.20±0.11b 5.02±0.05c

Results are expressed as mean±SD (n=3).

a–d Values in different letters within the same row differ significantly (p<0.05).

Download Excel Table
kosfa-41-2-237-g1
Fig. 1. Taste and flavour-related amino acids of breast meat from four chicken genotypes. Results are expressed as mean±SD (n=3). Tasty amino acids mean asparagine, threonine, serine, glutamic acid, glycine, and alanine. Flavour-related amino acids mean valine, isoleucine, leucine, phenylalanine, arginine, proline, and methionine. a–d Different letters indicate a significant difference (p<0.05) within the same bar graph.
Download Original Figure
Bioactive compounds and amino acid as an indicator of nutritional quality

The amount of choline was significantly different in spent hen, black-boned, and Thai native chickens, compared to that of the broiler (p<0.05). Black-boned chicken also had the highest choline content, while spent hen and Thai native chickens had the lowest (Fig. 2A). Any variability found among the samples could be attributed to the differences of genetic origin. Broilers had 2.7-fold and 8-fold higher choline contents than spent hen and Thai native chickens, respectively. Cohen et al. (1995) suggested that the uptake of circulatory choline decreased with age. Within the present study, all chickens were slaughtered at market age, in which the spent hen and Thai native chickens were older than the broilers. Therefore, the different choline contents in our results may be due to slaughter age. The effect of chicken genotype on the amount of betaine was significantly lower across all genotypes in comparison to the broilers (p<0.05), shown in Fig. 2B. Jayasena et al. (2015) also determined that broilers had significantly higher betaine contents in Korean native chickens, which also decreased with chicken age (Jayasena et al., 2014). Our results confirmed these findings, in which spent hen chickens had the lowest betaine content compared to other genotypes (p<0.05). Moreover, betaine is synthesized by the oxidation of choline in mitochondria through betaine aldehyde dehydrogenase (Meier and Seitz, 2008). It could be assumed that high choline content leads to an increase in betaine content. Thus, the black-boned chicken showed significantly higher betaine content than the Thai native chicken (p<0.05). The amount of L-carnitine content was significantly different in spent hen, black-boned, and Thai native chickens, compared to that of the broiler chickens (p<0.05), but it did not significantly differ between black-boned and Thai native chickens (Fig. 2C). The L-carnitine content was different in chicken meat due to myofiber type (Shimada et al., 2004) regardless of the age of the chickens (Jayasena et al., 2014). However, it has been reported that the Thai native chicken had significantly higher muscle fiber Types I and IIA than imported fast-growing breeds, such as the Rhode Island Red chicken (Jaturasitha et al., 2008). Type I and IIA fibers contained greater amounts of mitochondria and produced higher levels of acetyl groups than Type IIB fibers. Thus, they need higher L-carnitine content to buffer the excess acetyl groups. This may explain why Thai native and black-boned chickens have high L-carnitine contents. Moreover, the impact of over-supplied L-carnitine may depend on its endogenic biosynthesis from lysine and methionine, which are essential amino acids (Ghoreyshi et al., 2019). Our findings showed that lysine and methionine contents of spent hens were lower than those of the broiler, black-boned, and Thai native chickens (Table 2). We may, therefore, conclude that the lower amounts of these amino acids in spent hens result in lower L-carnitine contents. Creatine and its derivative creatine phosphate play a pivotal role in muscle energy metabolism by donating its phosphate groups to adenosine diphosphate to regenerate adenosine triphosphate (Balsom et al., 1994; Wyss and Kaddurah-Daouk, 2000). The creatine content in chicken breast meat was not significantly different between genotypes (Fig. 2D). Several previous studies reported that numerous factors; such as age, cooking method, meat portion, and body weight, had no significant effect on the creatine content (Jayasena et al., 2014; Jung et al., 2013). Biosynthesis of creatine occurs in the liver, and is then distributed to skeletal muscles through creatine kinase activity, which catalyses the generation of phosphorylcreatine from creatine (Wyss and Kaddurah-Daouk, 2000). The taurine contents in all genotypes were significantly different from that in the broilers (Table 2). Black-boned chicken contained the highest amount of taurine, followed by broiler and Thai native chicken (p<0.05). Notably, the spent hen in our study, which was the oldest at 72 wk, produced no taurine content in their breast meat (p<0.05). The major route for the biosynthesis of taurine is from methionine and cysteine through cysteine sulfinic acid decarboxylase (Scicchitano and Sica, 2018). Wu and Shiau (2002) reported that high amounts of taurine can also be found in dark meat, which coincides with our findings of high taurine content in black-boned chickens. Similarly, the Thai native chicken showed low taurine contents compared to the broiler, due to their higher lightness (Wattanachant et al., 2004).

kosfa-41-2-237-g2
Fig. 2. Bioactive compounds of breast meat from four chicken genotypes. Results are expressed as mean±SD (n=3). a–d Different letters indicate a significant difference (p<0.05) among genotypes. A, choline; B, betaine; C, L-carnitine; D, creatine.
Download Original Figure
Table 2. Bioactive compounds (mg/g sample) and amino acid profiles (% of total amino acids) as indicators of nutritional quality of breast meat from four chicken genotypes
Item Broiler Spent hen Black-boned Thai native
Taurine 0.66±0.03b ND 1.07±0.25a 0.26±0.07c
Alanine 8.99±0.11 8.90±0.06 8.87±0.04 8.96±0.02
Arginine 4.97±0.02b 4.94±0.03b 5.11±0.01a 5.14±0.01a
Aspartic acid 10.0±0.32a 9.51±0.07b 9.68±0.00b 9.69±0.02b
Cysteine 0.13±0.00b 0.13±0.02b 0.16±0.00a 0.15±0.01a
Glutamic acid 13.3±0.30c 13.6±0.17bc 13.6±0.02b 14.1±0.01a
Glycine 7.91±0.03c 8.72±0.06a 7.90±0.01c 8.07±0.01b
Histidine 2.86±0.04c 3.49±0.01a 2.74±0.01d 3.07±0.03b
Isoleucine 4.29±0.14b 4.22±0.04b 4.46±0.01a 4.24±0.00b
Leucine 8.11±0.01b 7.95±0.03c 8.27±0.03a 8.26±0.03a
Lysine 7.98±0.03c 7.86±0.06d 8.15±0.01b 8.31±0.03a
Methionine 2.87±0.01a 2.74±0.05b 2.88±0.01a 2.85±0.02a
Phenylalanine 3.16±0.01a 3.04±0.01c 3.14±0.01b 3.08±0.02b
Proline 4.18±0.03b 4.33±0.02a 4.16±0.03b 4.16±0.02b
Serine 5.42±0.11a 5.18±0.03b 5.25±0.01b 5.25±0.01b
Threonine 7.45±0.04c 7.77±0.03b 7.27±0.01d 8.18±0.02a
Tyrosine 2.60±0.02 2.54±0.13 2.54±0.01 2.51±0.01
Valine 5.16±0.09ab 5.13±0.05b 5.29±0.01a 5.11±0.01b
Total essential AA 47.1±0.13b 47.1±0.23b 47.3±0.03b 48.0±0.16a
Total non-essential AA 52.9±0.13a 52.7±0.23a 52.7±0.03a 52.0±0.16b

Results are expressed as mean±SD (n=3).

a–d Values in different letters within the same row differ significantly (p<0.05).

ND, not detected; AA, amino acid.

Download Excel Table

The amino acid profile is considered the most crucial nutritional property concerning consumer perceptions of meat. The total amino acid compositions of breast meat from four genotypes of chicken are shown in Table 2, in which seventeen amino acids were detected in this experiment, which differed significantly (p<0.05), except for alanine and tyrosine. Moreover, leucine, lysine, and threonine were the major constituent amino acids within all genotypes. We further noted that leucine content was significantly higher in black-boned and Thai native chickens than in broilers (p<0.05). The lysine content of the Thai native chicken was also significantly higher than in the broilers. The Thai native chicken also contained the highest threonine and glutamic acid contents among all genotypes (p<0.05), whereas cysteine content was lowest in the non-essential amino acid group. Thai native chicken had the highest glutamic acid content, followed by black-boned chicken, spent hen, and broilers (p<0.05). Meat is a source of food that has enriched branched-chain amino acids (Górska-Warsewicz et al., 2018). The study of Kim et al. (2017) found that arginine, leucine, and lysine were major essential amino acids in chicken meat, and were found in higher contents than other essential amino acids. We confirmed this in our findings, in that Thai native and black-boned chickens showed a higher content of essential amino acids compared with those of the commercial broiler. Several factors affected protein digestibility and deposition; such as species, age, and gender (Wu et al., 2014). The age and genotype of the chicken may be major factors that influence muscle composition. The Thai native chicken and black-boned chicken had slower growth rates than that of the broiler, and were classified as a ‘slow-growing’ type. The age difference may have affected protein deposition, due to the protein turnover rate (Tesseraud et al., 2000). Furthermore, the amount of lysine significantly differed between native chicken (120 d old) and broiler (42 d old) (Zhao et al., 2011). Therefore, our results indicate that levels of amino acid composition in breast meat are influenced by chicken genotype and slaughter age.

Conclusion

Our results showed that the levels of amino acids that were associated with the flavor and taste of chicken meat. The meat of the Thai native chicken and black-boned chicken were shown to be high in nutritional value and had some unique features and advantages over commercial broiler and spent hen chickens. We intend that the data from this study will provide valuable information concerning the functional meat for both Thai producers and consumers, where black-boned chicken proved to be an excellent source of nutrition, and Thai native chicken is both flavourful and luscious.

Conflicts of Interest

The authors declare no potential conflicts of interest.

Acknowledgements

The authors would like to express their gratitude to Professor Kenji Sato, Laboratory of Marine Biological Function, Division of Applied Biosciences, Graduate School of Agriculture, Kyoto University for equipment facilities. This research was supported by grants from the Royal Golden Jubilee Scholarship Ph.D Program (Grant No. PHD/0044/2558) and the Functional Food for Well-being Research Center, Chiang Mai University, Thailand.

Author Contributions

Conceptualization: Wongpoomchai R, Jaturasitha S. Methodology: Lengkidworraphiphat P, Wongpoomchai R, Chariyakornkul A. Validation: Bunmee T. Investigation: Lengkidworraphiphat P, Chariyakornkul A. Writing - original draft: Lengkidworraphiphat P, Bunmee T, Chaiwang N. Writing - review & editing: Lengkidworraphiphat P, Wongpoomchai R, Bunmee T, Chariyakornkul A, Chaiwang N, Jaturasitha S.

Ethics Approval

Animal experiment designs were approved by the Animal Ethics Committee of the Faculty of Medicine, Chiang Mai University (No. 36/2562).

References

1.

Ahn D, Park S. 2002; Studies on components related to taste such as free amino acids and nucleotides in Korean native chicken meat. J Korean Soc Food Sci Nutr. 31:547-552

2.

Ali M, Lee SY, Park JY, Jung S, Jo C, Nam KC. 2019; Comparison of functional compounds and micronutrients of chicken breast meat by breeds. Food Sci Anim Resour. 39:632-642

3.

Balsom PD, Söderlund K, Ekblom B. 1994; Creatine in humans with special reference to creatine supplementation. Sports Med. 18:268-280

4.

Bidlingmeyer BA, Cohen SA, Tarvin TL. 1984; Rapid analysis of amino acids using pre-column derivatization. J Chromatogr B Biomed Sci Appl. 336:93-104

5.

Chuaynukool K, Wattanachant S, Siripongvutikorn S, Yai H. 2007; Chemical and physical properties of raw and cooked spent hen, broiler and Thai indigenous chicken muscles in mixed herbs acidified soup (Tom Yum). J Food Technol. 5:180-186.

6.

Cohen BM, Renshaw PF, Stoll AL, Wurtman RJ, Yurgelun-Todd D, Babb SM. 1995; Decreased brain choline uptake in older adults: An in vivo proton magnetic resonance spectroscopy study. JAMA. 274:902-907

7.

De Zwart F, Slow S, Payne RJ, Lever M, George PM, Gerrard JA, Chambers ST. 2003; Glycine betaine and glycine betaine analogues in common foods. Food Chem. 83:197-204

8.

Flanagan JL, Simmons PA, Vehige J, Willcox MD, Garrett Q. 2010; Role of carnitine in disease. Nutr Metab. 7:30

9.

Ghoreyshi SM, Omri B, Chalghoumi R, Bouyeh M, Seidavi A, Dadashbeiki M, Lucarini M, Durazzo A, van Den Hoven R, Santini A. 2019; Effects of dietary supplementation of L-carnitine and excess lysine-methionine on growth performance, carcass characteristics, and immunity markers of broiler chicken. Animals. 9:362

10.

Górska-Warsewicz H, Laskowski W, Kulykovets O, Kudlińska-Chylak A, Czeczotko M, Rejman K. 2018; Food products as sources of protein and amino acids-the case of Poland. Nutrients. 10:1977

11.

Jaturasitha S, Srikanchai T, Kreuzer M, Wicke M. 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

12.

Jayasena DD, Jung S, Bae YS, Kim SH, Lee SK, Lee JH, Jo C. 2014; Changes in endogenous bioactive compounds of Korean native chicken meat at different ages and during cooking. Poult Sci. 93:1842-1849

13.

Jayasena DD, Jung S, Bae YS, Park HB, Lee JH, Jo C. 2015; Comparison of the amounts of endogenous bioactive compounds in raw and cooked meats from commercial broilers and indigenous chickens. J Food Compos Anal. 37:20-24

14.

Jayasena DD, Jung S, Kim HJ, Bae YS, Yong HI, Lee JH, Kim JG, Jo C. 2013; Comparison of quality traits of meat from Korean native chickens and broilers used in two different traditional Korean cuisines. Asian-Australas J Anim Sci. 26:1038-1046

15.

Jung S, Bae YS, Kim HJ, Jayasena DD, Lee JH, Park HB, Heo KN, Jo C. 2013; Carnosine, anserine, creatine, and inosine 5′-monophosphate contents in breast and thigh meats from 5 lines of Korean native chicken. Poult Sci. 92:3275-3282

16.

Jung Y, Jeon HJ, Jung S, Choe JH, Lee JH, Heo KN, Kang BS, Jo C. 2011; Comparison of quality traits of thigh meat from Korean native chickens and broilers. Korean J Food Sci Anim Resour. 31:684-692

17.

Kim H, Do HW, Chung H. 2017; A comparison of the essential amino acid content and the retention rate by chicken part according to different cooking methods. Korean J Food Sci Anim Resour. 37:626-634

18.

Li B, Li W, Ahmad H, Zhang L, Wang C, Wang T. 2015; Effects of choline on meat quality and intramuscular fat in intrauterine growth retardation pigs. PLOS ONE. 10e0129109

19.

Meier P, Seitz HK. 2008; Age, alcohol metabolism and liver disease. Curr Opin Clin Nutr Metab Care. 11:21-26

20.

Meinert L, Tikk K, Tikk M, Brockhoff PB, Bredie WL, Bjergegaard C, Aaslyng MD. 2009; Flavour development in pork. Influence of flavour precursor concentrations in longissimus dorsi from pigs with different raw meat qualities. Meat Sci. 81:255-262

21.

Mir NA, Rafiq A, Kumar F, Singh V, Shukla V. 2017; Determinants of broiler chicken meat quality and factors affecting them: A review. J Food Sci Technol. 54:2997-3009

22.

Mora L, Hernández-Cázares AS, Sentandreu MA, Toldrá F. 2010; Creatine and creatinine evolution during the processing of dry-cured ham. Meat Sci. 84:384-389

23.

Rikimaru K, Takahashi H. 2010; Evaluation of the meat from Hinai-jidori chickens and broilers: Analysis of general biochemical components, free amino acids, inosine 5′-monophosphate, and fatty acids. J Appl Poult Res. 19:327-333

24.

Schiffman SS, Dackis C. 1975; Taste of nutrients: Amino acids, vitamins, and fatty acids. Percept Psychophys. 17:140-146

25.

Scicchitano BM, Sica G. 2018; The beneficial effects of taurine to counteract sarcopenia. Curr Protein Pept Sci. 19:673-680

26.

Shimada K, Sakuma Y, Wakamatsu J, Fukushima M, Sekikawa M, Kuchida K, Mikami M. 2004; Species and muscle differences in L-carnitine levels in skeletal muscles based on a new simple assay. Meat Sci. 68:357-362

27.

Tesseraud S, Chagneau AM, Grizard J. 2000; Muscle protein turnover during early development in chickens divergently selected for growth rate. Poult Sci. 79:1465-1471

28.

Tu YG, Sun YZ, Tian YG, Xie MY, Chen J. 2009; Physicochemical characterisation and antioxidant activity of melanin from the muscles of Taihe Black-bone silky fowl (Gallus gallus domesticus Brisson). Food Chem. 114:1345-1350

29.

Wattanachant S, Benjakul S, Ledward DA. 2004; Composition, color, and texture of Thai indigenous and broiler chicken muscles. Poult Sci. 83:123-128

30.

Wattanachant S, Benjakul S, Ledward DA. 2005; Microstructure and thermal characteristics of Thai indigenous and broiler chicken muscles. Poult Sci. 84:328-336

31.

Wu G, Bazer FW, Dai Z, Li D, Wang J, Wu Z. 2014; Amino acid nutrition in animals: Protein synthesis and beyond. Annu Rev Anim Biosci. 2:387-417

32.

Wu HC, Shiau CY. 2002; Proximate composition, free amino acids and peptides contents in commercial chicken and other meat essences. J Food Drug Anal. 10:170-177

33.

Wyss M, Kaddurah-Daouk R. 2000; Creatine and creatinine metabolism. Physiol Rev. 80:1107-1213

34.

Zhao CJ, Schieber A, Gänzle MG. 2016; Formation of taste-active amino acids, amino acid derivatives and peptides in food fermentations: A review. Food Res Int. 89:39-47

35.

Zhao GP, Cui HX, Liu RR, Zheng MQ, Chen JL, Wen J. 2011; Comparison of breast muscle meat quality in 2 broiler breeds. Poult Sci. 90:2355-2359

Change of publication charge


As day of June 1, 2021 (based on date of article submission), article processing charges (APC) will be applied to papers accepted after peer review as follows:
 

Author APC Remark
Member 1,000,000 KR won First and corresponding authors should pay membership fee to Korean Society for Food Science of Animal Resources.
Non-member in Korea 1,200,000 KR won
Other countries except Korea 500 US $ Affiliation of corresponding author

I don't want to open this window for a day.

Special Issue: 67th ICoMST 2021


The 67th International Congress of Meat Science and Technology (ICoMST) is currently accepting abstracts.

The deadline for submitting abstracts has been extended to April 15th, 2021, and FSAR will apply a 50% publishing fee discount to this special issue.

For more information, please check the website below.

https://www.icomst2021.com/

 


I don't want to open this window for a day.