Animal Bioscience

  • 제35권3호
  • /
  • Pages.494-502
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  • 2022
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  • 2765-0189(pISSN)
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  • 2765-0235(eISSN)
아세아태평양축산학회 (Asian Australasian Association of Animal Production Societies)
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Physicochemical properties of reduced-salt cured pork loin as affected by different freezing temperature and storage periods

  • Kim, Haeun (Department of Animal Science, Chonnam National University) ;
  • Chin, Koo Bok (Department of Animal Science, Chonnam National University)
  • 투고 : 2021.07.16
  • 심사 : 2021.08.20
  • 발행 : 2022.03.01
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초록

Objective: The objective of this study was to evaluate functional properties of reduced-salt pork meat products made of pre-rigor pork loin treated by different freezing temperatures (-30℃ and -70℃) during storage. Methods: Pre-rigor cured pork loin with 1.0% added salt was compared to post-rigor muscle added with 1.5% salt for pH, color (L*, a*, b*), cooking loss (CL), expressible moisture, warner-Bratzler shear value, thiobarbituric acid reactive substances (TBARS), and volatile basic nitrogen (VBN). Results: Pre-rigor cured pork loins had higher pH and temperature than post-rigor ones as raw meat (p<0.05). pH values were higher for pre-rigor pork loins than those of post-rigor pork loins (p<0.05). Color values did not different among treatments (p>0.05). No color differences were observed during storage period after cooking (p>0.05). The CL (%) of pre-rigor cured pork loins was the lowest when frozen at -70℃. The TBARS and VBN increased from 8 weeks of storage (p<0.05), but no further changed thereafter (p>0.05). Pre-rigor cured pork loins added with 1.0% salt showed similar characteristics to post-rigor pork loins added with 1.5% salt. Conclusion: Cured pork loins could be produced using pre-rigor muscle added with 1/3 of the original salt level (1.5%) and could be stored for up to 4 wks of frozen storage, regardless of a frozen temperature of -30℃ or -70℃ without detrimental effects.

키워드

과제정보

This study was supported by a project (PJ013809022019) funded by the Rural Development Administration, Republic of Korea.

참고문헌

  1. Bhat ZF, Morton JD, Mason SL, Bekhit AEDA. The application of pulsed electric field as a sodium reducing strategy for meat products. Food Chem 2020;306:125622. https://doi.org/10.1016/j.foodchem.2019.125622
  2. Desmond E. Reducing salt: A challenge for the meat industry. Meat Sci 2006;74:188-96. https://doi.org/10.1016/j.meatsci.2006.04.014
  3. Choi JS, Chin KB. Evaluation of physicochemical and textural properties of chicken breast sausages containing various combinations of salt and sodium tripolyphosphate. J Anim Sci Technol 2020;62:577-86. https://doi.org/10.5187/jast.2020.62.4.577
  4. Song DH, Ham YK, Ha JH, Kim YR, Chin KB, Kim HW. Impacts of pre-rigor salting with KCl on technological properties of ground chicken breast. Poult Sci J 2020;99:597-603. https://doi.org/10.3382/ps/pez527
  5. Claus JR, Sorheim O. Preserving pre-rigor meat functionality for beef patty production. Meat Sci 2006;73:287-94. https://doi.org/10.1016/j.meatsci.2005.12.004
  6. Puolanne EJ, Terrell RN. Effects of Salt Levels in Prerigor Blends and Cooked Sausages on Water Binding, Released Fat and pH. J Food Sci 1983;48:1022-4. https://doi.org/10.1111/j.1365-2621.1983.tb09152.x
  7. Alonso V, Muela E, Tenas J, Calanche JB, Roncales P, Beltran JA. Changes in physicochemical properties and fatty acid composition of pork following long-term frozen storage. Eur Food Res Technol 2016;242:2119-27. https://doi.org/10.1007/s00217-016-2708-y
  8. Jauregui CA, Regenstein JM, Baker RC. A simple centrifugal method for measuring expressible moisture, a water-binding property of muscle foods. J Food Sci 1981;46:1271. https://doi.org/10.1111/j.1365-2621.1981.tb03038.x
  9. Wheeler TL, Shackelford SD, Koohmarrie M. Variation in proteolysis, sarcomere length, collagen content, and tenderness among major pork muscles. J Anim Sci 2000;78:958-65. https://doi.org/10.2527/2000.784958x
  10. Miwa K, Iida H. Studies on ethylalcohol determination in "Shiokara" by the microfiltration method. Fish Sci 1973;39:1189-94.
  11. Sinnhuber RO, Yu TC. The 2-thiobarbituric acid reaction, an objective measure of the oxidative deterioration occurring in fats and oils. J JOCS 1977;26:259-67. https://doi.org/10.5650/jos1956.26.259
  12. Liu J, Ruusunen M, Puolanne E, Ertbjerg P. Effect of pre-rigor temperature incubation on sarcoplasmic protein solubility, calpain activity and meat properties in porcine muscle. LWT-Food Sci Technol 2014;55:483-9. https://doi.org/10.1016/j.lwt.2013.10.001
  13. Judge MD, Aberle ED. Effect of prerigor processing on the oxidative rancidity of ground light and dark porcine muscles. J Food Sci 1980;45:1736-9. https://doi.org/10.1111/j.1365-2621.1980.tb07600.x
  14. Teuteberg V, Kluth IK, Ploetz M, Krischek C. Effects of duration and temperature of frozen storage on the quality and food safety characteristics of pork after thawing and after storage under modified atmosphere. Meat Sci 2021;174:108419. https://doi.org/10.1016/j.meatsci.2020.108419
  15. Medic H, Kusec ID, Pleadin J, et al. The impact of frozen storage duration on physical, chemical and microbiological properties of pork. Meat Sci 2018;140:119-27. https://doi.org/10.1016/j.meatsci.2018.03.006
  16. Xia X, Kong B, Liu J, Diao X, Liu Q. Influence of different thawing methods on physicochemical changes and protein oxidation of porcine longissimus muscle. LWT-Food Sci Technol 2012;46:280-6. https://doi.org/10.1016/j.lwt.2011.09.018
  17. Drerup DL, Judge MD, Aberle ED. sensory properties and lipid oxidation in prerigor processed fresh pork sausage. J Food Sci 1981;46:1659-61. https://doi.org/10.1111/j.1365-2621.1981.tb04456.x
  18. Thomas R, Anjaneyulu AS. R, Kondaiah N. Effect of hot-boned pork on the quality of hurdle treated pork sausages during ambient temperature (37±1℃) storage. Food Chem 2008;107:804-12. https://doi.org/10.1016/j.foodchem.2007.08.079
  19. Kim GD, Jeong JY, Hur SJ, Yang HS, Jeon JT, Joo ST. The relationship between meat color (CIE L* and a*), myoglobin content, and their influence on muscle fiber characteristics and pork quality. Korean J Food Sci An 2010;30:626-33. https://doi.org/10.5851/kosfa.2010. 30.4.626
  20. Karakaya M, Saricoban C, Yilmaz MT. The effect of various types of poultry pre- and post-rigor meats on emulsification capacity, water-holding capacity and cooking loss. Eur Food Res Technol 2005;220:283-6. https://doi.org/10.1007/s00217-004-1068-1
  21. Mortensen M, Andersen HJ, Engelsen SB, Bertram HC. Effect of freezing temperature, thawing and cooking rate on water distribution in two pork qualities. Meat Sci 2006;72:34-42. https://doi.org/10.1016/j.meatsci.2005.05.027
  22. Bertram HC, Andersen RH, Andersen HJ. Development in myofibrillar water distribution of two pork qualities during 10-month freezer storage. Meat Sci 2007;75:128-33. https://doi.org/10.1016/j.meatsci.2006.06.020
  23. Choi EJ, Park HW, Chung YB, Park SH, Kim JS, Chun HH. Effect of tempering methods on quality changes of pork loin frozen by cryogenic immersion. Meat Sci 2017;124:69-76. https://doi.org/10.1016/j.meatsci.2016.11.003
  24. Utrera M. Morcuende D, Estevez M. Temperature of frozen storage affects the nature and consequences of protein oxidation in beef patties. Meat Sci 2014;96:1250-7. https://doi.org/10.1016/j.meatsci.2013.10.032
  25. Vieira C, Diaz MT, Martinez B, Garcia-Cachan MD. Effect of frozen storage conditions (temperature and length of storage) on microbiological and sensory quality of rustic crossbred beef at different states of ageing. Meat Sci 2009;83:398-404. https://doi.org/10.1016/j.meatsci.2009.06.013
  26. Kim GD, Jung EY, Lim HJ, Yang HS, Joo ST, Jeong JY. Influence of meat exudates on the quality characteristics of fresh and freeze-thawed pork. Meat Sci 2013;95:323-9. https://doi.org/10.1016/j.meatsci.2013.05.007
  27. Sakata R, Oshida T, Morita H, Nagata Y. Physico-chemical and processing quality of porcine M. longissimus dorsi frozen at different temperatures. Meat Sci 1995;39:277-84. https://doi.org/10.1016/0309-1740(94)P1828-J
  28. Zhang Y, Ertbjerg P. On the origin of thaw loss: Relationship between freezing rate and protein denaturation. Food Chem 2019;299:125104. https://doi.org/10.1016/j.foodchem.2019.125104
  29. Jiang Q, Jia R, Nakazawa N, Hu Y, Osako K, Okazaki E. Changes in protein properties and tissue histology of tuna meat as affected by salting and subsequent freezing. Food Chem 2019;271:550-60. https://doi.org/10.1016/j.foodchem.2018.07.219
  30. Koohmaraie M, Doumit ME, Wheeler TL. Meat toughening does not occur when rigor shortening is prevented. J Anim Sci 1996;74:2935-42. https://doi.org/10.2527/1996.74122935x
  31. Grujic R, Petrovic LJ, Pikula B, Amidzic L. Definition of the optimum freezing rate-1. Investigation of structure and ultrastructure of beef M. longissimus dorsi frozen at different freezing rates. Meat Sci 1993;33:301-18. https://doi.org/10.1016/0309-1740(93)90003-Z
  32. Sabikun N, Bakhsh A, Ismail I, Hwang YH, Rahman MS, Joo ST. Changes in physicochemical characteristics and oxidative stability of pre- and post-rigor frozen chicken muscles during cold storage. J Food Sci Technol 2019;56:4809-16. https://doi.org/10.1007/s13197-019-03941-0
  33. Kim HW, Hwang KE, Song DH, et al. Effect of pre-rigor salting levels on physicochemical and textural properties of chicken breast muscles. Korean J Food Sci An 2015;35: 577-84. https://doi.org/10.5851/kosfa.2015.35.5.577
  34. APFQIA: Animal, Plant and Fisheries Quarantine and Inspection Agency. Standard for Processing & Ingredient Specifications of Livestock Product [Internet]. Gimcheon, Korea: Animal and Plant Quarantine Agency [cited 2020 Nov 24]. Available from: https://www.qia.go.kr/english/html/indexqiaEngNoticeWebAction.do
  35. Georgantelis D, Ambrosiadis I, Katikou P, Blekas G, Georgakis SA. Effect of rosemary extract, chitosan and α-tocopherol on microbiological parameters and lipid oxidation of fresh pork sausages stored at 4℃. Meat Sci 2007;76:172-81. https://doi.org/10.1016/j.meatsci.2006.10.026