Quality, Storage Stability, and Effect of Cryoprotectants onUltrastructure of Superchilled Chicken

Authors

  • Rituparna Banerjee ICAR-National Meat Research Institute, Chengicherla, Hyderabad, Telangana 500092, India
  • Naveena B Maheswarappa ICAR-National Meat Research Institute, Chengicherla, Hyderabad, Telangana 500092, India
  • M Muthukumar ICAR-National Meat Research Institute, Chengicherla, Hyderabad, Telangana 500092, India
  • Sowmya Dasoju ICAR-National Meat Research Institute, Chengicherla, Hyderabad, Telangana 500092, India

DOI:

https://doi.org/10.48165/jms.2023.18.02.06

Keywords:

Superchilling, Chicken meat, Shelf-life, SDS-PAGE, Cryoprotectants, Ultrastructure

Abstract

The concept of superchilling, an alternative to traditional chilling and  freezing methods, is to reduce the temperature 1-2 °C below the initial  freezing point of the food enabling safe, and high-quality product. This  work was aimed to explore the effects of superchilling (-2±0.5°C), chilling  (4±1°C), and freezing (−18±1°C) on the quality and storage stability of  dressed chicken and also to evaluate the role of cryoprotectants during  superchilling for enhanced meat quality. In superchilled samples,  improved water holding capacity (WHC) and lower shear force values  were observed relative to frozen chicken. SDS-PAGE analysis revealed  the appearance of 29 kDa protein bands in superchilled samples on  7th and 14th day, indicating troponin degradation and tenderization.  Scanning electron microscopy (SEM) studies indicated minimal damage  to muscle fibre ultrastructure in superchilled chicken relative to frozen  samples. Integrity of fibre structure was well maintained in superchilled  samples treated with sorbitol as a cryoprotectant relative to sucrose and  polyphosphate. Results demonstrated the potential use of superchilling  process along with cryoprotectants for improved quality and enhanced  shelf-life of chicken. 

Downloads

Download data is not yet available.

References

Alonso V, Muela E, Tenas J, Calanche JB, Roncalés P, Beltrán JA (2016). Changes in physicochemical properties and fatty acid composition of pork following long-term frozen storage. European Food Research and Technology 242: 2119–2127.

Anese M, Manzocco L, Panozzo A, Beraldo P, Foschia M, Nicoll MC (2012). Effect of radiofrequency assisted freez ing on meat microstructure and quality. Food Research International 46: 50–54.

Bahuaud D, Mørkøre T, Langsrud Ø, Sinnes K, Veiseth E, Ofstad R, Thomassen M S (2008). Effects of -1.5 °C superchilling on quality of Atlantic salmon (Salmo salar) pre-rigor fil lets: Cathepsin activity, muscle histology, texture and liquid leakage. Food Chemistry 111: 329–339.

Ballin NZ, Lametsch R (2008). Analytical methods for authenti cation of fresh vs. thawed meat — A review. Meat Science 80: 151–158.

Banerjee R, Maheswarappa NB (2017). Superchilling of muscle foods: Potential alternative for chilling and freezing. Critical Reviews in Food Science and Nutrition 59: 1–8.

Bellés M, Alonso V, Roncalés P, Beltrán JA (2017). The combined effects of superchilling and packaging on the shelf life of lamb”. Meat Science 133: 126–132.

Bozzola JJ, Russell LD (1992). Electron Microscopy: Principles and Techniques for Biologists. Jones and Bartlett Publishers Inc., Boston.

Cao L, An Y, Xiong S, Li S, Liu R (2016). Conformational changes and kinetic study of actomyosin from silver carp surimi

with modified starch–sucrose mixtures during frozen stor age. Journal of Food Quality 39: 54–63.

Ding D, Zhou C, Ge X, Ye K, Wang P, Bai Y, Zhou G. (2019). The effect of different degrees of superchilling on shelf life and quality of pork during storage. Journal of Food Processing and Preservation 44: e14394.

Duun AS, Hemmingsen AKT, Haugland A, Rustad T (2008). Quality changes during superchilled storage of pork roast. LWT – Food Science and Technology, 4: 2136–2143.

Duun AS, Rustad T (2007). Quality changes during superchilled storage of cod (Gadus morhua) fillets. Food Chemistry 105: 1067–1107.

Harris SE, Huff-Lonergan E., Lonergan, SM, Jones, WR, Rankins D (2001). Antioxidant status affects color stability and tenderness of calcium chloride-injected beef. Journal of Animal Science 79: 666-77.

He XY, Kong BH, Liu Q. Li PJ (2012). Effect of superchilling on quality characteristics of common carp during storage. Food Science 33: 309-312.

Hunter RS, Harold RW (1987). Uniform Color Scale. Chap. 8 in The Measurement of Appearance. John Wiley and Sons Inc., New York.

Jiménez SM, Salsi M S, Tiburzi MC, Rafaghelli RC, Tessi MA, Coutaz VR. (1997). Spoilage microflora in fresh chicken breast stored at 4°C: influence of packaging methods. Journal of Applied Microbiology 83: 613-618.

Kaale LD, Eikevik TM, Rustad T, Kolsaker K (2011). Superchilling of food, a review. Journal of Food Engineering 107: 141– 146.

Laemmli UK (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680- 685.

Lan Y, Shang Y, Song Y, Dong Q (2016). Changes in the quality of superchilled rabbit meat stored at different temperatures. Meat Science 117: 173–181.

León JG, López JH, Lozano JM, Muñoz Ramirez AP (2019). Cryoprotective effect of sorbitol on the muscle microstruc ture of Yamú (Brycon amazonicus) during storage at 2 and 18 °C. Revista Facultad Nacional de Agronomía Medellín 72: 8763-8774.

Liu DS, Liang L, Xia WS, Regenstein JM, Zhou P (2013). Biochemical and physical changes of grass carp (Ctenopharyngodon idella) fillets stored at -3 and 0 °C. Food Chemistry 140: 105-114.

Liu Q, Chen Q, Kong B, Han J, He X. (2014). The influence of superchilling and cryoprotectants on protein oxidation and structural changes in the myofibrillar proteins of common carp (Cyprinus carpio) surimi. LWT - Food Science and Technology 57: 603-611.

Lu X, Zhang Y, Zhu L, Luo X, Hopkins DL (2019). Effect of superchilled storage on shelf life and quality characteristics of M. longissimus lumborum from Chinese yellow cattle. Meat Science 149: 79–84.

Lu X, Zhang Y, Xu B, Zhu L, Luo X (2020). Protein degradation and structure changes of beef muscle during superchilled storage. Meat Science. 168: 108180.

Magnussen OM, Haugland A, Torstveit Hemmingsen AK, Johansen S, Nordtvedt TS (2008). Advances in superchilling of food-process characteristics and product quality. Trends in Food Science and Technology 19: 418–424.

Montowska M, Pospiech E (2013). Species-specific expression of various proteins in meat tissue: proteomic analysis of raw and cooked meat and meat products made from beef, pork and selected poultry species. Food Chemistry, 136: 1461-

Muela E, Sanudo C, Campo MM, Medel I, Beltran JA (2010). Effect of freezing method and frozen storage duration on instrumental quality of lamb throughout display. Meat Science 84: 662–669.

Olsson GB, Ofstad R, Lødemel JB, Olsen RL (2003). Changes in water-holding capacity of halibut muscle during cold stor age. LWT - Food Science and Technology 36: 771–778.

Olsson GB, Seppola MA, Olsen RL (2007). Water-holding capac ity of wild and farmed cod (Gadusmorhua) and haddock (Melanogrammus aeglefinus) muscle during ice storage. LWT - Food Science and Technology 40: 793–799.

Pomponio L, Bukh C, Ruiz-carrascal J (2018). Proteolysis in pork loins during superchilling and regular chilling storage. Meat Science 141: 57–65.

Qian S, Li X, Wang H, Sun Z, Zhang C, Guan W, Blecker C (2018). Effect of subfreezing storage (−6, −9, and −12 °C) on quality and shelf life of beef. International Journal of Food Science and Technology 53: 2129–2140.

Scherer R, Augusti PR, Steffens C, Bochi VC, Hecktheuer LH, Lazzari R, Radünz‐neto J, Pomblum SCG, Emanuelli T (2005). Effect of slaughter method on postmortem changes of grass carp (Ctenopharyngodon idella) stored in ice. Journal of Food Science. 70: C348–C353.

Stonehouse GG, Evans JA (2015). The use of supercooling for fresh foods: A review. Journal of Food Engineering 148: 74-79.

Suman SP, Hunt MC, Nair MN, Rentfrow G (2014). Improving beef color stability: Practical strategies and underlying mechanisms. Meat Science 98(3): 490–504.

Taub IA, Singh RP (1998). Food Storage Stability. CRC Press, Boca Raton, USA.

Trout GR (1989). Variation in myoglobin denaturation and color of cooked beef, pork, and turkey meat as influenced by pH,

with modified starch–sucrose mixtures during frozen stor age. Journal of Food Quality 39: 54–63.

Ding D, Zhou C, Ge X, Ye K, Wang P, Bai Y, Zhou G. (2019). The effect of different degrees of superchilling on shelf life and quality of pork during storage. Journal of Food Processing and Preservation 44: e14394.

Duun AS, Hemmingsen AKT, Haugland A, Rustad T (2008). Quality changes during superchilled storage of pork roast. LWT – Food Science and Technology, 4: 2136–2143.

Duun AS, Rustad T (2007). Quality changes during superchilled storage of cod (Gadus morhua) fillets. Food Chemistry 105: 1067–1107.

Harris SE, Huff-Lonergan E., Lonergan, SM, Jones, WR, Rankins D (2001). Antioxidant status affects color stability and tenderness of calcium chloride-injected beef. Journal of Animal Science 79: 666-77.

He XY, Kong BH, Liu Q. Li PJ (2012). Effect of superchilling on quality characteristics of common carp during storage. Food Science 33: 309-312.

Hunter RS, Harold RW (1987). Uniform Color Scale. Chap. 8 in The Measurement of Appearance. John Wiley and Sons Inc., New York.

Jiménez SM, Salsi M S, Tiburzi MC, Rafaghelli RC, Tessi MA, Coutaz VR. (1997). Spoilage microflora in fresh chicken breast stored at 4°C: influence of packaging methods. Journal of Applied Microbiology 83: 613-618.

Kaale LD, Eikevik TM, Rustad T, Kolsaker K (2011). Superchilling of food, a review. Journal of Food Engineering 107: 141– 146.

Laemmli UK (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680- 685.

Lan Y, Shang Y, Song Y, Dong Q (2016). Changes in the quality of superchilled rabbit meat stored at different temperatures. Meat Science 117: 173–181.

León JG, López JH, Lozano JM, Muñoz Ramirez AP (2019). Cryoprotective effect of sorbitol on the muscle microstruc ture of Yamú (Brycon amazonicus) during storage at 2 and 18 °C. Revista Facultad Nacional de Agronomía Medellín 72: 8763-8774.

Liu DS, Liang L, Xia WS, Regenstein JM, Zhou P (2013). Biochemical and physical changes of grass carp (Ctenopharyngodon idella) fillets stored at -3 and 0 °C. Food Chemistry 140: 105-114.

Liu Q, Chen Q, Kong B, Han J, He X. (2014). The influence of superchilling and cryoprotectants on protein oxidation and structural changes in the myofibrillar proteins of common carp (Cyprinus carpio) surimi. LWT - Food Science and Technology 57: 603-611.

Lu X, Zhang Y, Zhu L, Luo X, Hopkins DL (2019). Effect of superchilled storage on shelf life and quality characteristics of M. longissimus lumborum from Chinese yellow cattle. Meat Science 149: 79–84.

Lu X, Zhang Y, Xu B, Zhu L, Luo X (2020). Protein degradation and structure changes of beef muscle during superchilled storage. Meat Science. 168: 108180.

Magnussen OM, Haugland A, Torstveit Hemmingsen AK, Johansen S, Nordtvedt TS (2008). Advances in superchilling of food-process characteristics and product quality. Trends in Food Science and Technology 19: 418–424.

Montowska M, Pospiech E (2013). Species-specific expression of various proteins in meat tissue: proteomic analysis of raw and cooked meat and meat products made from beef, pork and selected poultry species. Food Chemistry, 136: 1461-

Muela E, Sanudo C, Campo MM, Medel I, Beltran JA (2010). Effect of freezing method and frozen storage duration on instrumental quality of lamb throughout display. Meat Science 84: 662–669.

Olsson GB, Ofstad R, Lødemel JB, Olsen RL (2003). Changes in water-holding capacity of halibut muscle during cold stor age. LWT - Food Science and Technology 36: 771–778.

Olsson GB, Seppola MA, Olsen RL (2007). Water-holding capac ity of wild and farmed cod (Gadusmorhua) and haddock (Melanogrammus aeglefinus) muscle during ice storage. LWT - Food Science and Technology 40: 793–799.

Pomponio L, Bukh C, Ruiz-carrascal J (2018). Proteolysis in pork loins during superchilling and regular chilling storage. Meat Science 141: 57–65.

Qian S, Li X, Wang H, Sun Z, Zhang C, Guan W, Blecker C (2018). Effect of subfreezing storage (−6, −9, and −12 °C) on quality and shelf life of beef. International Journal of Food Science and Technology 53: 2129–2140.

Scherer R, Augusti PR, Steffens C, Bochi VC, Hecktheuer LH, Lazzari R, Radünz‐neto J, Pomblum SCG, Emanuelli T (2005). Effect of slaughter method on postmortem changes of grass carp (Ctenopharyngodon idella) stored in ice. Journal of Food Science. 70: C348–C353.

Stonehouse GG, Evans JA (2015). The use of supercooling for fresh foods: A review. Journal of Food Engineering 148: 74-79.

Suman SP, Hunt MC, Nair MN, Rentfrow G (2014). Improving beef color stability: Practical strategies and underlying mechanisms. Meat Science 98(3): 490–504.

Taub IA, Singh RP (1998). Food Storage Stability. CRC Press, Boca Raton, USA.

Trout GR (1989). Variation in myoglobin denaturation and color of cooked beef, pork, and turkey meat as influenced by pH,

with modified starch–sucrose mixtures during frozen stor age. Journal of Food Quality 39: 54–63.

Ding D, Zhou C, Ge X, Ye K, Wang P, Bai Y, Zhou G. (2019). The effect of different degrees of superchilling on shelf life and quality of pork during storage. Journal of Food Processing and Preservation 44: e14394.

Duun AS, Hemmingsen AKT, Haugland A, Rustad T (2008). Quality changes during superchilled storage of pork roast. LWT – Food Science and Technology, 4: 2136–2143.

Duun AS, Rustad T (2007). Quality changes during superchilled storage of cod (Gadus morhua) fillets. Food Chemistry 105: 1067–1107.

Harris SE, Huff-Lonergan E., Lonergan, SM, Jones, WR, Rankins D (2001). Antioxidant status affects color stability and tenderness of calcium chloride-injected beef. Journal of Animal Science 79: 666-77.

He XY, Kong BH, Liu Q. Li PJ (2012). Effect of superchilling on quality characteristics of common carp during storage. Food Science 33: 309-312.

Hunter RS, Harold RW (1987). Uniform Color Scale. Chap. 8 in The Measurement of Appearance. John Wiley and Sons Inc., New York.

Jiménez SM, Salsi M S, Tiburzi MC, Rafaghelli RC, Tessi MA, Coutaz VR. (1997). Spoilage microflora in fresh chicken breast stored at 4°C: influence of packaging methods. Journal of Applied Microbiology 83: 613-618.

Kaale LD, Eikevik TM, Rustad T, Kolsaker K (2011). Superchilling of food, a review. Journal of Food Engineering 107: 141– 146.

Laemmli UK (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680- 685.

Lan Y, Shang Y, Song Y, Dong Q (2016). Changes in the quality of superchilled rabbit meat stored at different temperatures. Meat Science 117: 173–181.

León JG, López JH, Lozano JM, Muñoz Ramirez AP (2019). Cryoprotective effect of sorbitol on the muscle microstruc ture of Yamú (Brycon amazonicus) during storage at 2 and 18 °C. Revista Facultad Nacional de Agronomía Medellín 72: 8763-8774.

Liu DS, Liang L, Xia WS, Regenstein JM, Zhou P (2013). Biochemical and physical changes of grass carp (Ctenopharyngodon idella) fillets stored at -3 and 0 °C. Food Chemistry 140: 105-114.

Liu Q, Chen Q, Kong B, Han J, He X. (2014). The influence of superchilling and cryoprotectants on protein oxidation and structural changes in the myofibrillar proteins of common carp (Cyprinus carpio) surimi. LWT - Food Science and Technology 57: 603-611.

Lu X, Zhang Y, Zhu L, Luo X, Hopkins DL (2019). Effect of superchilled storage on shelf life and quality characteristics of M. longissimus lumborum from Chinese yellow cattle. Meat Science 149: 79–84.

Lu X, Zhang Y, Xu B, Zhu L, Luo X (2020). Protein degradation and structure changes of beef muscle during superchilled storage. Meat Science. 168: 108180.

Magnussen OM, Haugland A, Torstveit Hemmingsen AK, Johansen S, Nordtvedt TS (2008). Advances in superchilling of food-process characteristics and product quality. Trends in Food Science and Technology 19: 418–424.

Montowska M, Pospiech E (2013). Species-specific expression of various proteins in meat tissue: proteomic analysis of raw and cooked meat and meat products made from beef, pork and selected poultry species. Food Chemistry, 136: 1461-

Muela E, Sanudo C, Campo MM, Medel I, Beltran JA (2010). Effect of freezing method and frozen storage duration on instrumental quality of lamb throughout display. Meat Science 84: 662–669.

Olsson GB, Ofstad R, Lødemel JB, Olsen RL (2003). Changes in water-holding capacity of halibut muscle during cold stor age. LWT - Food Science and Technology 36: 771–778.

Olsson GB, Seppola MA, Olsen RL (2007). Water-holding capac ity of wild and farmed cod (Gadusmorhua) and haddock (Melanogrammus aeglefinus) muscle during ice storage. LWT - Food Science and Technology 40: 793–799.

Pomponio L, Bukh C, Ruiz-carrascal J (2018). Proteolysis in pork loins during superchilling and regular chilling storage. Meat Science 141: 57–65.

Qian S, Li X, Wang H, Sun Z, Zhang C, Guan W, Blecker C (2018). Effect of subfreezing storage (−6, −9, and −12 °C) on quality and shelf life of beef. International Journal of Food Science and Technology 53: 2129–2140.

Scherer R, Augusti PR, Steffens C, Bochi VC, Hecktheuer LH, Lazzari R, Radünz‐neto J, Pomblum SCG, Emanuelli T (2005). Effect of slaughter method on postmortem changes of grass carp (Ctenopharyngodon idella) stored in ice. Journal of Food Science. 70: C348–C353.

Stonehouse GG, Evans JA (2015). The use of supercooling for fresh foods: A review. Journal of Food Engineering 148: 74-79.

Suman SP, Hunt MC, Nair MN, Rentfrow G (2014). Improving beef color stability: Practical strategies and underlying mechanisms. Meat Science 98(3): 490–504.

Taub IA, Singh RP (1998). Food Storage Stability. CRC Press, Boca Raton, USA.

Trout GR (1989). Variation in myoglobin denaturation and color of cooked beef, pork, and turkey meat as influenced by pH,

sodium chloride, sodium tripolyphosphate, and cooking temperature. Journal of Food Science 54(3): 536–544. Wang Z, He Z, Gan X, Li H (2018). Interrelationship among fer rous myoglobin, lipid and protein oxidations in rabbit meat during refrigerated and superchilled storage. Meat Science 146: 131–139.

Wardlaw FB, Mccaskill LH, Acton JC (1973). Effect of postmor tem muscle changes in poultry meat loaf properties. Journal of Food Science 38: 421−424.

Warris PD (1979). The extraction of haem pigments from fresh meat. Journal of Food Technology 14: 75−80.

Witte VC, Krauze GF, Bailey ME (1970). A new extraction method for determining 2-thiobarbituric acid values of pork and beef during storage. Journal of Food Science 35: 582–585.

Xia X, Kong B, Liu Q, Liu J (2009). Physicochemical change and protein oxidation in porcine longissimus dorsi as influenced by different freeze-thaw cycles. Meat Science 83: 239–245.

Zhou GH, Xu XL, Liu Y (2010). Preservation technologies for fresh meat–A review. Meat Science 86: 119–128.

Published

2024-01-20

How to Cite

Banerjee, R., Maheswarappa, N.B., Muthukumar , M., & Dasoju, S. (2024). Quality, Storage Stability, and Effect of Cryoprotectants onUltrastructure of Superchilled Chicken. Journal of Meat Science, 18(2), 37–46. https://doi.org/10.48165/jms.2023.18.02.06