Synchrotron fourier transform infrared microspectroscopy and scanning electron microscopy assessment of key physical meat properties of Thai native chickens for selection in breeding programs
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Published:
Aug 11, 2021
Keywords:
Synchrotron-based FTIR microspectroscopy Scanning electron microscopy α-helix secondary protein β-turn secondary protein Thai native chicken
Main Article Content
Abstract
In this study, synchrotron-based Fourier transform infrared spectroscopy (S-FTIR) microspectroscopy and scanning electron microscopy (SEM) were employed to examine the key physical meat properties of the muscle texture and secondary structure of protein from the chicken breast meat in Thai native chickens (TNCs), Thai synthetic chickens (TSCs), and Thai native crossbred chickens (TNC crossbreds) compared to commercial broilers (BRs). In total, 500 one-day-old chickens of all breeds were raised until the slaughter weight of each breed was reached. The experiment was a completely randomized design, and breast meat samples were collected from each breed at the market weight. SEM analysis was employed to identify the texture characteristics of chicken meat among different groups. Compared to BR birds, TNCs, TSCs, and TNC crossbreds exhibited higher numbers of muscle fibers and lower muscle fiber diameters. S-FTIR analysis revealed differences between the average original spectra and normalized spectra, reflective of the absorbance of the protein secondary structure and lipids among the groups. TNC meat contained protein with an increased content of α-helix and lower lipid content; therefore, TNC breeds can potentially provide chicken meat with a good texture and be suitable to be functional chicken meat; in addition, it can be beneficial for designing breeding programs for subsequent breed development.
Article Details
How to Cite
Charoensin, S., Boonkum, W., Thumanu, K., Laopaiboon, B., & Duangjinda, M. (2021). Synchrotron fourier transform infrared microspectroscopy and scanning electron microscopy assessment of key physical meat properties of Thai native chickens for selection in breeding programs. Asia-Pacific Journal of Science and Technology, 26(04), APST–26. https://doi.org/10.14456/apst.2021.39
Section
Research Articles
References
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[26] Wattanachant S, Benjakul S, Ledward DA. Composition, color, and texture of Thai indigenous and broiler chicken muscles. Poult Sci Poul Sci. 2004;83(1):123-128.
[27] Katemala S, Molee A, Thumanu K, Yongsawatdigul J. Infrared spectroscopy and textural properties of meat from 3 chicken breeds subjected to various thermal treatments. The 6th Meat Science Technology Conference; 2018 Jun 18-19; Bangkok, Thailand. p. 82-89.
[28] Yu P, McKinnon JJ, Christensen CR, Christensen DA. Using synchrotron-based FTIR microspectroscopy to reveal chemical features of feather protein secondary structure: comparison with other feed protein sources. J Agric Food Chem. 2004;52(24):7353-7361.
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[30] Da Silva-Buzanello RA, Schuch AF, Gasparin AW, Torquato AS, Scremin FR, Canan C, et al. Quality parameters of chicken breast meat affected by carcass scalding conditions. Asian-Australas J Anim Sci. 2019;32(8):1186-1194.
[2] Fanatico AC, Pillai PB, Emmert JL, Owens CM. Meat quality of slow- and fast-growing chicken genotypes fed low-nutrient or standard diets and raised indoors or with outdoor access. Poultry Sci. 2007;86(10):2245-2455.
[3] Devatkal SK, Naveena BM, Kotaiah T. Quality, composition, and consumer evaluation of meat from slow-growing broilers relative to commercial broilers. Poult Sci. 2019;98(11):6177-6186.
[4] Pellattiero E, Tasoniero G, Cullere M, Gleeson E, Baldan G, Contiero B, Dalle Zotte A . Are meat quality traits and sensory attributes in favor of slow-growing chickens?. Animals. 2020;10(6):12-14.
[5] Jaturasitha S, Kayan A, Wicke M. Carcass and meat characteristics of male chickens between Thai indigenous compared with improved layer breeds and their crossbred. Arch Tierz. 2008;51(3):283-294.
[6] Lee MA, Jung Y, Jo C, Park JY, Nam KC. Analysis of consumers’ preferences and price sensitivity to native chickens. Korean J Food Sci Anim Resour. 2017;37(3):469-476.
[7] Chumngoen W, Tan FJ. Relationships between descriptive sensory attributes and physicochemical analysis of broiler and Taiwan native chicken breast meat. Asian-Australas. J Anim Sci. 2015;28(7):1028-1037.
[8] Mookprom S, Boonkum W, Kunhareang S, Siripanya S, Duangjinda M. Genetic evaluation of egg production curve in Thai native chickens by random regression and spline models. Poult Sci. 2017;96(2):274-281.
[9] Miraglia D, Mammoli R, Branciari R, Ranucci D, Cenci Goga BT. Characterization of muscle fibre type and evaluation of the presence of giant fibres in two meat chicken hybrids. Vet Res Commun. 2006;30(S1):357-360.
[10] Verdiglione R, Cassandro M. Characterization of muscle fiber type in the pectoralis major muscle of slow-growing local and commercial chicken strains. Poult Sci. 2013;92:2433-2437.
[11] Yu P. Protein secondary structures (α-helix and β-sheet) at a cellular level and protein fractions in relation to rumen degradation behaviours of protein: a new approach. Br J Nutr. 2005;94(5):655-665.
[12] Yu P, McKinnon JJ, Soita HW, Christensen CR, Christensen DA. Use of synchrotron-based FTIR microspectroscopy to determine protein secondary structures of raw and heat-treated brown and golden flaxseeds: a novel approach. Can J Anim Sci. 2005;85(4):437-448.
[13] Choudhary OP, Priyanka. Scanning electron microscope: advantages and disadvantages in imaging components. Int J Curr Microbiol Appl Sci. 2017;6(5):1877-1882.
[14] Kang GH, Park GB, Joo ST, Lee M, Lee SK. Effects of muscle fiber types on gel property of surimi-like materials from chicken, pork and beef. J Muscle Foods. 2010;21(3)570-584.
[15] Wattanachant S, Benjakul S, Ledward DA. Microstructure and thermal characteristics of Thai indigenous and broiler chicken muscles. Poult Sci. 2005;84(2):328-336.
[16] Mehmood W, Zhang C. Correlations between muscle fibers characteristics and meat quality attributes of biceps femoris muscle: a comparative study of 2 distinctive broiler breeds. Rev Bras Cienc Avic. 2020;22(4):1-8.
[17] Sukprasert J, Thumanu K, Phung-On I, Jirarungsatean C, Erickson LE, Tuitemwong P. Synchrotron FTIR light reveals signal changes of biofunctionalized magnetic nanoparticle attachment on Salmonella sp. J Nanomater. 2020;2020:6149713.
[18] Guo XJ, Wang RQ. Changes in secondary structure of myofibrillar protein and its relationship with water dynamic changes during storage of battered and deep-fried pork slices. Food Sci Biotechnol. 2018;27(6):1667-1673.
[19] Rueden CT, Schindelin J, Hiner MC, DeZonia BE, Walter AE, Arena ET, et al. ImageJ2: ImageJ for the next generation of scientific image data. BMC Bioinform. 2017;18:529.
[20] Tunim S, Phasuk Y, Aggrey SE, Duangjinda M. Gene expression of fatty acid binding protein genes and its relationship with fat deposition of Thai native crossbreed chickens. J Anim Bios. 2021;34(4):751-758.
[21] Ismail I, Joo ST. Poultry meat quality in relation to muscle growth and muscle fiber characteristics. Korean J Food Sci Anim Resour. 2017;37(6):873-883.
[22] Muth PC, Valle Zárate A. Breast meat quality of chickens with divergent growth rates and its relation to growth curve parameters. Arch Anim Breed. 2017;60(4):427-437.
[23] Waritthitham A, Lambertz C, Langholz HJ, Wicke M, Gauly M. muscle fiber characteristics and their relationship to water holding capacity of longissimus dorsi muscle in Brahman and Charolais crossbred bulls. Asian-Australas J Anim Sci. 2010;23(5):665-671.
[24] Yu P. Application of advanced synchrotron radiation-based Fourier transform infrared (SR-FTIR) microspectroscopy to animal nutrition and feed science: a novel approach. Br J Nutr. 2004;92(6):869-885.
[25] Kong J, Yu S. Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochim Biophys Sin (Shanghai). 2007;39(8):549-559.
[26] Wattanachant S, Benjakul S, Ledward DA. Composition, color, and texture of Thai indigenous and broiler chicken muscles. Poult Sci Poul Sci. 2004;83(1):123-128.
[27] Katemala S, Molee A, Thumanu K, Yongsawatdigul J. Infrared spectroscopy and textural properties of meat from 3 chicken breeds subjected to various thermal treatments. The 6th Meat Science Technology Conference; 2018 Jun 18-19; Bangkok, Thailand. p. 82-89.
[28] Yu P, McKinnon JJ, Christensen CR, Christensen DA. Using synchrotron-based FTIR microspectroscopy to reveal chemical features of feather protein secondary structure: comparison with other feed protein sources. J Agric Food Chem. 2004;52(24):7353-7361.
[29] Carbonaro M, Maselli P, Nucara A. Relationship between digestibility and secondary structure of raw and thermally treated legume proteins: a Fourier transform infrared (FT-IR) spectroscopic study. Amino Acids. 2012;43(2):911-921.
[30] Da Silva-Buzanello RA, Schuch AF, Gasparin AW, Torquato AS, Scremin FR, Canan C, et al. Quality parameters of chicken breast meat affected by carcass scalding conditions. Asian-Australas J Anim Sci. 2019;32(8):1186-1194.