Food Science of Animal Resources (한국축산식품학회지)

Korean Society for Food Science of Animal Resources (한국축산식품학회)
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Meat Quality of Pork Muscles from Low-fat Cuts

돼지 저지방 부의 근육들의 육질 특성

  • 성필남 (농촌진흥청 국립축산과학원) ;
  • 조수현 (농촌진흥청 국립축산과학원) ;
  • 김진형 (농촌진흥청 국립축산과학원) ;
  • 하경희 (농촌진흥청 국립축산과학원) ;
  • 박범영 (농촌진흥청 국립축산과학원) ;
  • 이종문 (농촌진흥청 국립축산과학원) ;
  • 김동훈 (농촌진흥청 국립축산과학원)
  • Published : 2009.06.30
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Abstract

This study was conducted to provide fundamental information in developing muscle-specific strategies to improve the quality and value of low-fat pork cuts upon evaluating meat qualitative parameters of twenty one (21) muscle samples selected from ten (10) market-weighted crossbred pigs. The following observations were made. The pH was highest for subscpularis and lowest for gluteus superrificialis (p<0.05); the subscpularis can hold water the most (p<0.05), biceps femoris loses the most content upon cooking, while subscpularis loses the least content (p<0.05); gluteus superrificialis (p<0.05) has the most purge loss contents, and infraspanatus and gastrocneminus contained the most collagen, while adductor had the least collagen (p<0.05); biceps femoris has the most WB-shear force values while subscpularis (p<0.05) has the least; pectoralis profundi-fan was the most protein soluble; semitendinosus has the most gel strength (p<0.05). In the properties of meat color, tensor fasciae latae shows the highest CIE $L^*$ (lightness) values (p<0.05) and supraspinatus, brachiocephalicus and infraspanatus have the highest CIE $a^*$ (redness, p<0.05) values; vastus intermedius has the most myoglobin content while longissimus dorsi (p<0.05) has the least; infraspanatus is the most tender (one of the sensory properties) while biceps femoris was the most tough among all tested muscles (p<0.05); the pectoralis profundi-fan was the most flavorful pork while vastus intermedius was the least (p<0.05); supraspinatus, infraspanatus, semitendinosus, and vastus intermedius were juiciest while longissimus dorsi was the driest (p<0.05). In overall likeness, the semitendinosus and infraspanatus were most liked while biceps femoris and longissimus dorsi were the least (p<0.05). This study presents the results of several parameters in selected pork muscle samples which are useful information for developing new muscle-specific strategies to improve the quality of consuming meat and meat products.

돼지고기 저지방 부위 근육들의 특성에 맞는 이용법을 구명하는데 필요한 기초 자료를 제시하고자 삼원교잡종 돼지도체 10두(거세돼지 5두, 암퇘지 5두)에서 분리한 21개 근육의 육질 특성을 조사하였다. 돼지 저지방 부위를 구성하고 있는 주요 21개 근육의 육질특성을 조사한 결과, subscpularis 근육의 pH가 가장 높았고, gluteus superrificialis 근육이 가장 낮았다(p<0.05). 보수력은 subscpularis 근육이 가장 높았으며(p<0.05), 가열감량은 biceps femoris 근육이 가장 많았고, subscpularis 근육이 적었다(p<0.05). 포장감량은 bluteus superrificialis 근육이 가장 많았고(p<0.05) 콜라겐 함량은 infraspinatus와 gastrocnemius 근육이 가장 많았던 반면에 adductor 근육이 가장 적었다(p<0.05). 전단력은 biceps femoris 근육이 가장 높았고, subscpularis 근육이 가장 낮았다(p<0.05). 단백질 용해성은 pectoralis profundi(fan) 근육이 가장 높았고(p<0.05), 겔 강도는 semitendinosus 근육이 가장 높았다(p<0.05). 육색특성에서 명도 값은 tensor fasciae latae 근육이 가장 높았고(p<0.05), 적색도는 superaspinatus, brachiocephalicus, infraspinatus 근육들이 높았으며, 미오글로빈 함량은 vastus intermedius 근육이 가장 높았고, longissimus dorsi 근육이 가장 낮았다(p<0.05). 관능적 특성 중 연도는 infraspinatus 근육이 가장 연하였던 반면에 biceps femoris 근육이 가장 질겼다(p<0.05). 풍미에서는 pectoralis profundi(fan) 근육이 가장 높은 평가를 받았고, vastus intermedius 근육이 가장 낮은 평가를 받았다(p<0.05). 다즙성에서는 supraspinatus, infraspinatus, semitendinosus, vastus intermedius 근육들이 가장 다즙했던 반면에 longissimus dorsi 근육이 가장 건조했다(p<0.05). 전체기호도는 semitendino년와 infraspinatus 근육이 가장 높은 평가를 받았고, biceps femoris와 longissimus dorsi 근육이 가장 낯은 평가를 받았다(p<0.05). 이상의 결과를 종합하면 돼지 저지방 부위를 구성하는 21개 근육들은 육질적인 측면에서 서로 다른 특성들을 나타내는 것으로 조사되었으며, 이러한 결과는 각 근육들의 특성에 적합한 이용방법 개발에 필요한 기초 자료로 유용할 것으로 사료된다.

Keywords

References

  1. Aaslyng, M. D., Bejerholm, C., Ertbjerg, P., Bertram, H. C., and Andersen, H. J. (2003) Cooking loss and juiciness of pork in relation to raw meat quality and cooking procedure, Food Qual. and Perfer. 14, 277-288 https://doi.org/10.1016/S0950-3293(02)00086-1
  2. AOAC (2000) 'Official Methods of Analysis'. Ch 39.1.27. Hydroxy- proline in meat and meat products. Association of Official Analytical Chemists. Gaithersburg, MD. p 13-15
  3. Bader, R. (1982) Enzymhistochemische und histometrische untersuchungen an skelettmuskeln von ausgemastenten, gesunde sweinen der deutschen landrasse. Zbl. Vet. Med. A. 29, 443-450
  4. Barton-Gade, P. (1981) The measurement of meat quality in pigs post mortem. In: Porcine Stress and Meat Quality - Causes and Possible Solutions to the Problems. Froysten, T., Slinde, E., Standal, N. (Eds.). Agricultural Food Research Society. ${\AA}$s. Norway. p. 359
  5. Barton-Gade, P. and Olsen, E. V. (1987) Evaluation and Control of Meat Quality in Pigs. Tarrant, P. V., Eikelenboom, G., and Monin, G. (eds). Martinus Nijhoff. Dordrecht. p. 117
  6. Bee, G., Anderson, A. L., Lonergan, S. M., and Huff-Lonergan, E. (2007) Rate and extent of pH decline affect proteolysis of cytoskeletal prteins and water-holding capacity in pork. Meat Sci. 76, 359-365 https://doi.org/10.1016/j.meatsci.2006.12.004
  7. Beecher, G. R., Cassens, R. G., Hoekstra, W. G., and Briskey, E. J. (1965) Red and White fiber content and associated postmortem properties of seven porcine muscles. J. Food Sci. 30, 969-976 https://doi.org/10.1111/j.1365-2621.1965.tb01872.x
  8. Bendall, J. R. (1978) Variability in rates of pH fall and of lactate production in the muscles on cooling beef carcasses. Meat Sci. 2, 91-104 https://doi.org/10.1016/0309-1740(78)90010-4
  9. Brewer, M. S., Zhu, L. G., Bidner, B., Meisinger, D. J., and McKeith, F. K. (2001) Measuring pork color: effects of bloom time, muscle, pH and relationship to instrumental parameters. Meat Sci. 57, 169-176 https://doi.org/10.1016/S0309-1740(00)00089-9
  10. Briskey, E. J., Hoekstra, W. G., Bray, R. W., and Grummer, R. H. (1960) A comparison of certain physical and chemical characteristics of eight pork muscles. J. Anim. Sci. 19, 214-225 https://doi.org/10.2527/jas1960.191214x
  11. Camou, J. P. and Sebranek, J. G. (1991) Gelation characteristics of muscle proteins from pale, soft, exudative (PSE) pork. Meat Sci. 30, 207-220 https://doi.org/10.1016/0309-1740(91)90067-Z
  12. Carmack, C. F., Kastner, C. L., Dikeman, M. E., Schwenke, J. R., and García Zepeda, C. M. (1995) Sensory evaluation of beef-flavor-intensity, tenderness, and juiciness among major muscles. Meat Sci. 39, 143-147 https://doi.org/10.1016/0309-1740(95)80016-6
  13. Cross, H. R., Carpenter, Z. L., and Smith, G. C. (1973) Effects of intramuscular collagen and elastin on bovine muscle tenderness. J. Food Sci. 38, 998-1003 https://doi.org/10.1111/j.1365-2621.1973.tb02133.x
  14. DeVol, D. L., McKeith, F. K., Bechtel, P. J., Novakofski, J., Shanks, R. D., and Carr, T. R. (1988) Variation in composition and palatability traits and relationships between muscle characteristics and palatability in a random sample of pork carcasses. J. Anim. Sci. 66, 385-395 https://doi.org/10.2527/jas1988.662385x
  15. Deymer, D. I. and Vandekerckhove, P. (1979) Compounds determining pH in dry sausage. Meat Sci. 34, 351-362 https://doi.org/10.1016/0309-1740(93)90083-T
  16. Essen-Gustavsson, B. and Fjelkner-Modig, S. (1985) Skeletal muscle characteristics in different breeds of pigs in relation to sensory properties of meat. Meat Sci. 13, 33-47 https://doi.org/10.1016/S0309-1740(85)80003-6
  17. Forrest, J. C., Aberle, E. D., Hedrick, H. B., Judge, M. D., and Merkel, R. A. (1975) Principles of Meat Science. W. H. Freeman & Co. San Francisco. pp. 178-185
  18. Gee, A. and Plkinghorne, R. (2002) Design and protocol for Korean BBQ taste test sensory trials. Meat Standard Australia, Sydney. Australia
  19. Harris, P. V. and Shorthose, W. R. (1988) Meat texture. In R. Lawrie (Ed.), Developments in meat science (pp. 245-290). London and New York: Elsevier Applied Science
  20. Johnson, R. C., Chen, C. M., Muller, T. S., Costello, W. J., Romans, J. R., and Jones, K. W. (1988) Characterization of the muscles within the beef forequarter. J. Food Sci. 53, 1247-1250 https://doi.org/10.1111/j.1365-2621.1988.tb09249.x
  21. Jones, S. T. and Burson, D. E. (2000) Porcine myology. University of Nebraska, Institute of Agriculture and Natural Resources. Animal Science Department. Lincoln. NE 68583-0908
  22. Kallweit, E. (1987) Evaluation and Control of Meat Quality in Pigs. Tarrant, P. V., Eikelenboom, G., and Monin, G. (eds). Martinus Nijhoff. Dordrecht. pp. 107
  23. Karlsson, A. H., Klont, R. E., and Fernandez, X. (1999) Skeletal muscle fibres as factors for pork quality. Livestock Production Science 60, 255-269 https://doi.org/10.1016/S0301-6226(99)00098-6
  24. Karlsson, A., Enfalt, a. Ch., Essen-Gustavson, B., Lundstrom, K., Hansson, I., Rydhamer, L. and Stern, S. (1991) Proceedings 37th International Congress of Meat Science and Technology Kulmbach, Germany. pp. 131
  25. Kiessling, K. H. and Hansson, I. (1983) Fiber composition and enzyme activities in pig muscles. Swedish J. Agric. Res. 13, 257-261
  26. Ko, M. S. and Yang, J. B. (2001) Effects of wrap and vacuum packaging on shelf life of chilled pork. Kor. J. Food and Nutr. 14, 255-262
  27. Laakkonen, E., Wellington, G. H., and Skerbon, J. W. (1970) Low temperature longtime heating of bovine. I. Changes in tenderness, water binding capacity, pH and amount of watersoluble component. J. Food. Sci. 35, 175-177 https://doi.org/10.1111/j.1365-2621.1970.tb12131.x
  28. Lan, Y. H., Novakofski, J., McCusker, R. H., Brewer, S. B., Carr, T. R., and McKeith, F. K. (1995) Thermal gelation of myofibrils from pork, beef, fish, chicken and turkey. J. Food Sci. 60, 941-945 https://doi.org/10.1111/j.1365-2621.1995.tb06266.x
  29. Lin, R. R., Carpenter, J. A., and Reagan, J. O. (1983) Chemical, cooking and textural properties of semimembranosus, semitendinosus and biceps femoris muscles of pork. J. Food Quality 7, 277-282 https://doi.org/10.1111/j.1745-4557.1985.tb01059.x
  30. McKeith, F. K., DeVol, D. L., Miles, R. S., Bechtel, P. J., and Carr, T. R. (1985) Chemical and sensory properties of thirteen major beef muscles. J. Food Sci. 50, 869-872 https://doi.org/10.1111/j.1365-2621.1985.tb12968.x
  31. Monin, G., Mejenes-Quijano, A., Talmant, A., and Sellier, P. (1987) Influence of breed and muscle metabolic type on muscle glycolytic potential and meat pH in pigs. Meat Sci. 20, 149-158 https://doi.org/10.1016/0309-1740(87)90034-9
  32. Nold, R. A., Romans, J. R., Costello, W. J., Henson, J. A., and Libal, G. W. (1997) Sensory characteristics and carcass traits of boars, barrows, and gilts fed high- or adequate-protein diets and slaughtered at 100 or 110 kilograms. J. Anim. Sci. 75, 2641-2651 https://doi.org/10.2527/1997.75102641x
  33. Nold, R. A., Romans, J. R., Costello, W. J., and Libal, G. W. (1999) Characterization of muscles from boars, barrows, and gilts slaughtered at 100 or 110 kilograms: differences in fat, moisture, color, water-holding capacity, and collagen. J. Anim. Sci. 77, 1746-1754 https://doi.org/10.2527/1999.7771746x
  34. Oeckel, M. J., Warnants, N., and Boucque, Ch. V. (1999) Comparison of different methods for measuring water holding capacity and juiciness of pork versus on-line screening methods. Meat Sci. 51, 313-320 https://doi.org/10.1016/S0309-1740(98)00123-5
  35. Park, B. Y., Cho, S. H., Yoo, Y. M., Ko, J. J., Kim, J. H., Chae, H. S., Ahn, J. N., Lee, J. M., Kim, Y. K., and Yoon, S. K. (2001) Animal products and processing : Effect of carcass temperature at 3 h post-mortem on pork quality. J. Anim. Sci. Technol(Kor). 43, 949-954
  36. Pearson, A. M. and Young, R. B. (1989) Muscle and Meat Biochemistry. Academic Press. San Diego
  37. Ramsbottom, J. M., Strandine, E. J., and Koonz, C. H. (1945) Comparative tenderness of representative beef muscles. Food Res. 10, 497-509 https://doi.org/10.1111/j.1365-2621.1945.tb16198.x
  38. Ruusunen, M. (1989) Korrelationen mellan vattenh${\aa}$llande f$\"{u}$rm${\aa}$gaoch muskelfibersammans$\"{a}$ttning I olika typer av svinmuskler. In: Lundstrom, K., Malmfors, G. (Eds.), K$\"{}$tkvalitet hos V${\aa}$ra Slaktdjur, NJF - seminarium 183. Swedish University of Agricultural Sciences Department of Food Science. Uppsala. pp. 33-40
  39. Saffle, R. L. (1968) Meat emulsion. In: Advances in Food Research. Chichester, C. O., Mark, E. M. and Stewart, G. F. (eds.). Academic Press. New York. USA.
  40. Saffle, R. L. and Galbreath. J. W. (1964) Quantitative determination of salt soluble protein in various types of meat. Food Technol. 18, 119-120
  41. Samejima, K., Egelandal, B., and Fretheim, K. (1985) Heat gelation properties and protein extractability of beef myofibrills. J. Food Sci. 50, 1540-1543, 1555 https://doi.org/10.1111/j.1365-2621.1985.tb10528.x
  42. SAS, 1996, SAS/STAT user's guide
  43. Shackelford, S. D., Wheeler, T. L., and Koohmaraie, M. (1995) Relationship between shear force and trained sensory panel tenderness ratings of 10 major muscles from Bos indicus and Bos taurus cattle. J. Anim. Sci. 73, 3333-3340 https://doi.org/10.2527/1995.73113333x
  44. Siegel, D. G. and Schmidt, G. R. (1979) Crude myosin fraction as meat binders. J. Food Sci. 44, 1129-1132 https://doi.org/10.1111/j.1365-2621.1979.tb03463.x
  45. Stainsby, G. (1987) Gelatin gels, In: Advances in meat research. Volume 4, Collagen as a food. Pearson, A. M., Dutson, T. R. and Bailey, A. J. (eds). Van Nostrand Reinhold Company. NY. pp. 209-222
  46. Sutton, D. S., Ellis, M., Lan, Y., McKeith, F. K., and Wilson, E. R. (1997) Influence of slaughter weight and stress gene genotype on the water-holding capacity and protein gel characteristics of three porcine muscles. Meat Sci. 46, 173-180 https://doi.org/10.1016/S0309-1740(97)00006-5
  47. Topel, D. G., Merkel, R. A., Mackintosh, D. L., and Hall, J. L. (1966) Variation of some physical and biochemical properties within and among selected porcine muscles. J. Anim. Sci. 25, 277-282 https://doi.org/10.2527/jas1966.252277x
  48. Trout, G. R. (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. J. Food Sci. 54, 536-540 https://doi.org/10.1111/j.1365-2621.1989.tb04644.x
  49. Von Seggern, D. D., Calkins, C. R., Johnson, D. D., Brickler, J. E., and Gwartney, B. L. (2005) Muscle profiling: Characterizing the muscles of the beef chuck and round. Meat Sci. 71, 39-51 https://doi.org/10.1016/j.meatsci.2005.04.010
  50. Warner, R. D., Kauffman, R. G., and Russell, R. L. (1993) Quality attributes of major porcine muscles: A comparison with the Longissimus Lumborum. Meat Sci. 33, 359-372 https://doi.org/10.1016/0309-1740(93)90007-5
  51. Wheeler, T. L., Shackelford, S. D., and Koohmaraie, M. (2000) Variation in proteolysis, sarcomere length, collagen content, and tenderness among major pork muscles. J. Anim. Sci. 78, 958-965 https://doi.org/10.2527/2000.784958x
  52. Yeom, G. W., Andrieu, J., and Min, S. G. (2004) Effect of acid treatment process on the physicochemical properties of gelatin extracted from pork skin. Kor. J. Food Sci. 24, 266-272
  53. 박범영, 김진형, 조수현, 유영모, 황인호, 김동훈, 채현석, 안종남, 김용곤, 정명옥, 이종문 (2004) 소돼지 도체수율, 농촌진흥청 축산연구소. pp. 86-133
  54. 송재철, 박현정 (1995) 식품물성학. 울산대학교 출판사. pp.506-507

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