Food Science and Biotechnology

Korean Society of Food Science and Technology (한국식품과학회)
권호 표지

Free Amino Acids, Collagen Solubility, and Meat Quality in Pork (Longissimus Muscle of Yorkshire) as a Function of Chiller Temperature and Aging

  • Park, Beom-Young (Division of Animal Products, National Livestock Research Institute, RDA) ;
  • Park, Kyoung-Mi (Institute of Rare Earth for Biological Application, Chonbuk National University) ;
  • Kim, Jin-Hyung (Division of Animal Products, National Livestock Research Institute, RDA) ;
  • Cho, Soo-Hyun (Division of Animal Products, National Livestock Research Institute, RDA) ;
  • Kim, Nam-Kuk (Department of Applied Biochemistry, College of Biomedical and Health Science, Konkuk University) ;
  • Song, Min-Jin (Department of Applied Biochemistry, College of Biomedical and Health Science, Konkuk University) ;
  • Lee, Chang-Soo (Department of Applied Biochemistry, College of Biomedical and Health Science, Konkuk University) ;
  • Cho, In-Kyung (Department of Food and Nutrition, Nambu University) ;
  • Choe, Ho-Sung (Institute of Rare Earth for Biological Application, Chonbuk National University) ;
  • Ryu, Kyeong-Seon (Institute of Rare Earth for Biological Application, Chonbuk National University) ;
  • Hwang, In-Ho (Institute of Rare Earth for Biological Application, Chonbuk National University)
  • Published : 2008.02.29
Download PDF
⟨ Previous Next ⟩

Abstract

This study was conducted to identify the effect of chilling temperature (-3 and $6^{\circ}C$) and aging (1- and 7-day) on objective meat quality, collagen solubility, and free amino acids in pork (longissimus muscle of Yorkshire). Warner-Bratzler (WB)-shear force indicated that variation in chilling temperature had no detectable effect on meat tenderness and tenderization during the 7-day aging period. Among the 13 detected free amino acids, only 3 amino acids (histidine, valine, leucine) were significantly affected by the temperature treatment (p<0.05). Collagen solubility was significantly increased at $6^{\circ}C$ treatment (p<0.05). There was a significant linear relationship (r=0.67, p<0.05) between changes in free amino acids and WB-shear force during the 7-day aging period. These results confirmed that chilling conditions had significantly affected collagen solubility, and meat tenderization occurred in direct proportion to an increase in free amino acids.

Keywords

References

  1. Offer G, Cousins T. The mechanism of drip production: Formation of two compartments of extracellular space in muscle post mortem. J. Sci. Food Agr. 58: 107-116 (1992) https://doi.org/10.1002/jsfa.2740580118
  2. Bertram HC, Schafer A, Rosenvold K, Anderson HJ. Physical changes of signficance of early post mortem water distribution in porcine m. longissimus. Meat Sci. 66: 915-924 (2004) https://doi.org/10.1016/S0309-1740(03)00188-8
  3. Tarrant PV. The effects of handling, transport, slaughter, and chilling on meat quality and yield in pigs. pp. 1-25. In: Manipulating Pig Production II. Proceeding of Biennial Conference of the Australian Pig Science Association. August 10-15th. Warribee, Victoria, Australia. Australian Pig Science Association, Melbourne, Australia (1989)
  4. Grandin T. Methods to reduce PSE and blood splash. pp. 206-209. In: Proceeding of Allen D. Leman Swine Conference. University of MN, USA. Swine Association, Minniapolis, MN, USA (1994)
  5. Park BY, Kim NK, Lee CS, Hwang IH. Effect of fiber type on postmortem proteolysis in longissimus muscle of Landrace and Korean native black pigs. Meat Sci. 77: 482-491 (2007) https://doi.org/10.1016/j.meatsci.2007.04.022
  6. van Laack RLJM, Smulders FJM. The effect of rapid chilling on pork quality in the Netherlands. pp. 510-511. In: Congress Proceedings of the 42nd ICoMST. August 21-26, ICoMST, Helsinki, Finland (1996)
  7. Offer G. Modelling of the formation of pale, soft, and exudative meat: Effects of chilling regime and rate and extent of glycolysis. Meat Sci. 30: 157-184 (1991) https://doi.org/10.1016/0309-1740(91)90005-B
  8. Toldra F, Flores M. The use of muscle enzymes as predictors of pork meat quality. Food Chem. 69: 387-395 (2000) https://doi.org/10.1016/S0308-8146(00)00052-2
  9. Moya VJ, Flores M, Aristoy MC, Foldra F. Pork meat quality affects peptide and amino acid profiles during the ageing process. Meat Sci. 58: 197-206 (2001) https://doi.org/10.1016/S0309-1740(00)00152-2
  10. Cornet M, Bousset J. Free amino acid and dipeptides in porcine muscles: Differences between 'red' and 'white' muscles. Meat Sci. 51: 215-219 (1999) https://doi.org/10.1016/S0309-1740(98)00104-1
  11. Nishimura T, Kato H. Taste of free amino acids and peptides. Food Rev. Int. 4: 175-194 (1988) https://doi.org/10.1080/87559128809540828
  12. Hernandez-Jover T, Izquierdo-Pulido M, Veciana-Nogues T, Vidal- Carou MC. Biogenic amine sources in cooked cured shoulder pork. J. Agr. Chem. 44: 3097-3101 (1996) https://doi.org/10.1021/jf960250s
  13. Wheeler TL, Shackelford SD, Koohmaraie M. Relationship of beef longissimus tenderness classes to tenderness of gluteus medius, semimembranosus, and biceps femoris. J. Anim. Sci. 78: 2856-2861 (2000)
  14. Cross HR, West RL, Dutson TR. Comparison of methods for measuring sarcomere length in beef semitendinosus muscle. Meat Sci. 5: 261-266 (1981) https://doi.org/10.1016/0309-1740(81)90016-4
  15. Picard B, Leger J, Robelin J. Quantitative determination of type I myosin heavy chain in bovine muscle with anti myosin monoclonal antibodies. Meat Sci. 36: 333-343 (1994) https://doi.org/10.1016/0309-1740(94)90130-9
  16. Bar A, Pette D. Three fast myosin heavy chains in adult rat skeletal muscle. FEBS Lett. 235: 153-155 (1998) https://doi.org/10.1016/0014-5793(88)81253-5
  17. Bradford MM. A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254 (1976) https://doi.org/10.1016/0003-2697(76)90527-3
  18. Kolar K. Colorimetric determination of hydroxyproline as measure of collagen content in meat and meat products: NMKL collaborative study. J. Assoc. Off. Ana. Chem. 73: 54-57 (1990)
  19. Hill F. The solubility of intramuscular collagen in meat animals of various ages. J. Food Sci. 31: 161-166 (1966) https://doi.org/10.1111/j.1365-2621.1966.tb00472.x
  20. Hwang IH, Thompson JM. The interaction between pH and temperature decline early postmortem on the calpain system and objective tenderness in electrically stimulated beef longissimus dorsi muscle. Meat Sci. 58: 167-174 (2001) https://doi.org/10.1016/S0309-1740(00)00147-9
  21. SAS Institute Inc. SAS User's Guide. Statistical Analysis Systems Institute, Cary, NC, USA (2001)
  22. Pearson AM, Dutson TR. Scientific basis for electrical stimulation. Vol. 1, pp. 185-218. In: Advances in Meat Research-Electrical Stimulation. Pearson DH, Dutson TR (eds). West-Port CT: AVI Publishing Co., New York, NY, USA (1985)
  23. Hwang IH, Park BY, Cho SH, Kim MJ, Lee JM. Effects of preslaughter fasting and chiller ageing on objective meat quality in longissimus dorsi, biceps femoris, and triceps brachii muscles of Korean native black pigs. J. Anim. Sci. Technol. 46: 405-414 (2004) https://doi.org/10.5187/JAST.2004.46.3.405
  24. Geesink GH, Koohmaraie M. Ionic strength-induced inactivation of ${\mu}$-calpain in postmortem muscle. J. Anim. Sci. 78: 2336-2343 (2000)
  25. Locker RH, Hagyard CJ. A cold shortening effect in beef muscles. J. Sci. Food Agr. 14: 787-793 (1963) https://doi.org/10.1002/jsfa.2740141103
  26. Hwang IH, Devine CE, Hopkins DL. The biochemical and physical effects of electrical stimulation on beef and sheep meat tenderness- A review. Meat Sci. 65: 677-691 (2003) https://doi.org/10.1016/S0309-1740(02)00271-1
  27. Wheeler TD, Koomaraie M. The extent of proteolysis is independent of sarcomere length in lamb longissimus and psoas major. J. Anim. Sci. 77: 2444-2451 (1999) https://doi.org/10.2527/1999.7792444x
  28. Park BY, Kim JH, Cho SH, Ha KH, Lee SH, Chio CH, Kim DH, Lee JM, Kim YK, Ahn JN, Hwang IH. Evidence of significant effects of stunning and chilling methods on PSE incidences. A. Austral. J. Anim. 20: 257-262 (2007)
  29. Armero E, Baselga M, Aristoy MC, Toldra F. Effects of sire type and sex on pork muscle exopeptidase activity, natural dipeptides, and free amino acids. J. Sci. Food Agr. 79: 1280-1284 (1999) https://doi.org/10.1002/(SICI)1097-0010(19990715)79:10<1280::AID-JSFA359>3.0.CO;2-7
  30. Choi YM, Ruy YC, Lee SH, Kim BC. Relationships between myosin light chain isoforms, muscle fiber characteristics, and meat quality traits in porcine longissimus muscle. Food Sci. Biotechnol. 14: 639-644 (2005)
  31. Rhee MS, Ryu YC, Kim BC. Effects of packaging methods on the shelf life of selenium-supplemented chicken meat during refrigerated storage. Food Sci. Biotechnol. 15: 431-436 (2006)