한국축산식품학회지 (Food Science of Animal Resources)

  • 제38권1호
  • /
  • Pages.143-151
  • /
  • 2018
  • /
  • 2636-0772(pISSN)
  • /
  • 2636-0780(eISSN)
한국축산식품학회 (Korean Society for Food Science of Animal Resources)
권호 표지
DOI QR코드

DOI QR Code

Effect of Proteolytic Enzymes and Ginger Extract on Tenderization of M. pectoralis profundus from Holstein Steer

  • 투고 : 2017.11.15
  • 심사 : 2018.01.20
  • 발행 : 2018.02.28
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

The effects of proteolytic enzymes (bromelain and bromelain+papain) and a ginger extract were assessed on collagen content and solubility, thermal shrinkage temperature of connective tissue, pH, cooking loss, drip loss, and Warner-Bratzler shear force (WBSF) of M. pectoralis profundus isolated from the beef brisket cut. Both proteolytic enzymes and ginger extract led to a significant increase in cooking loss and collagen solubility compared with untreated controls. On the other hand, the peak ($T_p$) thermal shrinkage temperature markedly decreased in all treatments compared with those in controls. Samples treated with bromelain, bromelain + papain, and ginger extract showed a significant decrease in WBSF by 36%, 40%, and 37%, respectively, compared with untreated controls. Our findings suggest that ginger extract are useful for post-mortem tenderization of meat containing high levels of collagen, compared to control even though, bromelain and bromelain + papain treatments have higher collagen solubility than ginger extract.

키워드

참고문헌

  1. Aktas N, Kaya M. 2001. Influence of weak organic acids and salts on the denaturation characteristics of intramuscular connective tissue. A differential scanning calorimetry study. Meat Sci 58:413-419. https://doi.org/10.1016/S0309-1740(01)00044-4
  2. Allen Foegeding E, Larick DK. 1986. Tenderization of beef with bacterial collagenase. Meat Sci 18:201-214. https://doi.org/10.1016/0309-1740(86)90034-3
  3. Anandh MA. 2013. Effect of different tenderizers on tenderness and quality of buffalo tripe. Asian J Dairy & Food Res 32:144-148.
  4. Bailey AJ. 1972. The basis of meat texture. J Sci Food Agri 23:955-1007.
  5. Benito-Delgado J, Marriott NG, Claus JR, Wang H, Graham PP. 1994. Chuck longissimus and infraspinatus muscle characteristics as affected by rigor state, blade tenderization and calcium chloride injection. J Food Sci 59:295-299. https://doi.org/10.1111/j.1365-2621.1994.tb06951.x
  6. Bernholdt HF. 1975. Enzymes in food processing. 2nd ed. Reed G (ed). pp 473. Academic Press, New York, NY, USA.
  7. Boleman SJ, Boleman SL, Miller RK, Taylor JF, Cross HR, Wheeler TL, Koohmaraie M, Shackelford SD, Miller MF, West RL, Johnson DD, Savell JW. 1997. Consumer evaluation of beef of known categories of tenderness. J Anim Sci 75:1521-1524. https://doi.org/10.2527/1997.7561521x
  8. Dransfield E, Wakefield DK, Parkman ID. 1992. Modelling post-mortem tenderisation-I: texture of electrically stimulated and non-stimulated beef. Meat Sci 31:57-73. https://doi.org/10.1016/0309-1740(92)90072-C
  9. Fang SH, Nishimura T, Takahashi K. 1999. Relationship between development of intramuscular connective tissue and toughness of pork during growth of pigs. J Anim Sci 77:120-130. https://doi.org/10.2527/1999.771120x
  10. Garmyn AJ, Hilton GG, Mateescu RG, Morgan JB, Reecy JM, Tait RG Jr, Beitz DC, Duan Q, Schoonmaker JP, Mayes MS, Drewnoski ME, Liu Q, VanOverbeke DL. 2011. Estimation of relationships between mineral concentration and fatty acid composition of longissimus muscle and beef palatability traits. J Anim Sci 89:2849-2858. https://doi.org/10.2527/jas.2010-3497
  11. Goll DE, Bray RW, Hoekstra WG. 1963. Age-associated changes in muscle composition. The isolation and properties of a collagenous residue from bovine muscle. J Food Sci 28:503-509. https://doi.org/10.1111/j.1365-2621.1963.tb00234.x
  12. Herring HK, Cassens RG, Briskey EJ. 1965. Further studies on bovine muscle tenderness as influenced by carcass position, sarcomere length, and fiber diameter. J Food Sci 30:1049-1054. https://doi.org/10.1111/j.1365-2621.1965.tb01885.x
  13. Hertzman C, Olsson U, Tornberg E. 1993. The influence of high temperature, type of muscle and electrical stimulation on the course of rigor, ageing and tenderness of beef muscles. Meat Sci 35:119-141. https://doi.org/10.1016/0309-1740(93)90074-R
  14. Hill F. 1966. The solubility of intramuscular collagen in meat animals of various ages. J Food Sci 31:161-166. https://doi.org/10.1111/j.1365-2621.1966.tb00472.x
  15. Honikel KO, Hamm R. 1994. Measurement of water-holding capacity and juiciness. In: Pearson AM, Dutson TR, Editors, Quality attributes and their measurement in meat, poultry and fish products. Blackie Academic and Professional, Wester Cleddans, Bishopbriggs, Glasgow, UK. pp 125-161.
  16. Horgan DJ, King NL, Kurth LB, Kuypers R. 1990. Collagen crosslinks and their relationship to the thermal properties of calf tendons. Arch Biochem Biophys 281:21-26. https://doi.org/10.1016/0003-9861(90)90407-P
  17. Hwang IH, Devine CE, Hopkins DL. 2003. The biochemical and physical effects of electrical stimulation on beef and sheep meat tenderness. Meat Sci 65:677-691. https://doi.org/10.1016/S0309-1740(02)00271-1
  18. Judge MD, Aberle ED. 1982. Effects of chronological age and post-mortem aging on thermal shrinkage temperature of bovine intramuscular collagen. J Anim Sci 54:68-71. https://doi.org/10.2527/jas1982.54168x
  19. Kang CK, Rice EE. 1970. Degradation of various meat fractions by tenderizing enzymes. J Food Sci 35:563-577. https://doi.org/10.1111/j.1365-2621.1970.tb04809.x
  20. Ketnawa S, Rawdkuen S. 2011. Application of bromelain extract for muscle foods tenderization. Food Nutri Sci 2:393-401. https://doi.org/10.4236/fns.2011.25055
  21. Kolar K. 1990. Colorimetric determination of hydroxyproline as measure of collagen content in meat and meat products: NMKL collaborative study. J Assoc Off Anal Chem 73:54-57.
  22. Lee YB, Kim YS, Ashmore CR. 1986. Antioxidant property in ginger rhizome and its application to meat products. J Food Sci 51:20-23. https://doi.org/10.1111/j.1365-2621.1986.tb10826.x
  23. Light ND, Champion AE, Voyle C, Bailey AJ. 1985. The role of epimysial, perimysial and endomysial collagen in determining texture in six bovine muscles. Meat Sci 13:137-141. https://doi.org/10.1016/0309-1740(85)90054-3
  24. Ludwig CJ, Clans JR, Marriott NG, Johnson J, Wang H. 1997. Skeletal alternation to improve beef longissimus muscle tenderness. J Anim Sci 75:2404-2410. https://doi.org/10.2527/1997.7592404x
  25. Maher SC, Mullen AM, Moloney AP, Buckley DJ, Kerry JP. 2004. Quantifying the extent of variation in the eating quality traits of the M. longissimus dorsi and M. semimembranosus of conventionally processed Irish beef. Meat Sci 66:351-360. https://doi.org/10.1016/S0309-1740(03)00110-4
  26. Mentiratta SK, Anjaneyulu ASR, Lakshmanan V, Naveena BM, Bisht GS. 2000. Tenderizing and antioxidant effect of ginger extract on sheep meat. J Food Sci Technol 37:565-570.
  27. Miles CA, Avery NC, Rodin VV, Bailey AJ. 2005. The increase in denaturation temperature following cross-linking of collagen is caused by dehydration of the fibres. J Mol Biol 346:551-556. https://doi.org/10.1016/j.jmb.2004.12.001
  28. Miller AT, Karmas E, Fu Lu M. 1983. Age-related changes in the collagen of bovine corium: Studies on extractability, solubility and molecular size distribution. J Food Sci 48:681-685. https://doi.org/10.1111/j.1365-2621.1983.tb14875.x
  29. Morgan JB, Miller RK, Mendez FM, Hale DS, Savell JW. 1991a. Using calcium chloride injection to improve tenderness of beef from mature cows. J Anim Sci 69:4469-4476. https://doi.org/10.2527/1991.69114469x
  30. Morgan JB, Savell JW, Hale DS, Miller RK, Griffin DB, Cross HR, Shackelford SD. 1991b. National beef tenderness survey. J Anim Sci 69:3274-3283. https://doi.org/10.2527/1991.6983274x
  31. Asif-Ullah M, Kim KS, Yu YG. 2006. Purification and characterization of a serine protease from Cucumis trigonus Roxburghi. Phytochemistry 65:870-875.
  32. Naveena BM, Mendiratta SK. 2001. Tenderization of spent hen meat using ginger extract. Br Poult Sci 42:344-350. https://doi.org/10.1080/00071660120055313
  33. Naveena BM, Mendiratta SK, Anjaneyulu ASR. 2004. Tenderization of buffalo meat using plant proteases from Cucumis trigonus Roxb (Kachri) and Zingiber officinale roscoe (Ginger rhizome). Meat Sci 68:363-369. https://doi.org/10.1016/j.meatsci.2004.04.004
  34. Naveena BM, Mendiratta SK. 2004. The tenderization of buffalo meat using ginger extract. J Muscle Foods 15:235-244.
  35. Olsson U, Hertzman C, Tornberg E. 1994. The influence of low temperature, type of muscle and electrical stimulation on the course of rigor mortis, ageing and tenderness of beef muscles. Meat Sci 37:115-131. https://doi.org/10.1016/0309-1740(94)90149-X
  36. Pawar VD, Mule BD, Machewad GM. 2007. Effect of marination with ginger rhizome extract on properties of raw and cooked chevon. J Muscle Foods 18:349-369. https://doi.org/10.1111/j.1745-4573.2007.00091.x
  37. Rattrie NW, Regenstein JM. 1977. Action of crude papain on actin and myosin heavy chains isolated from chicken breast muscle. J Food Sci 42:1159-1163. https://doi.org/10.1111/j.1365-2621.1977.tb14450.x
  38. Rawdkuen S, Benjakul S. 2012. Biochemical and microstructural characteristics of meat samples treated with different plant proteases. Afr J Biotechnol 11:14088-14095.
  39. Savell JW, Shackelford SD. 1992. The significance of tenderness to the meat industry. In Proceedings of the 45th reciprocal meat conference. Chicago, Il: American Meat Science Association and National Live Stock and Meat Board, pp 43-46.
  40. Shackelford SD, Morgan JB, Cross HR, Savell JW. 1991. Identification of threshold levels for Warner Bratzler shear force in beef top loin steaks. J Muscle Foods 2:289-296. https://doi.org/10.1111/j.1745-4573.1991.tb00461.x
  41. Sullivan GA, Calkins CR. 2010. Application of exogenous enzymes to beef muscle of high and low-connective tissue. Meat Sci 85:730-734. https://doi.org/10.1016/j.meatsci.2010.03.033
  42. Syed Ziauddin K, Rao DN, Amla BL. 1995. Effect of lactic acid, ginger extract and sodium chloride on electrophoretic pattern of buffalo muscle proteins. J Food Sci Technol 32:224-226.
  43. Takagi H, Arafuka S, Inouye M, Yamasaki M. 1992. The effect of amino acid deletion in subtilisin E, based on structural comparison with a microbial alkaline elastase, on its substrate specificity and catalysis. J Biochem 111:584-588. https://doi.org/10.1093/oxfordjournals.jbchem.a123801
  44. Thompson EH, Wolf ID, Allen CE. 1973. Ginger rhizome: A new source of proteolytic enzyme. J Food Sci 38:652-655. https://doi.org/10.1111/j.1365-2621.1973.tb02836.x
  45. Thu DTN. 2006. Meat quality: understanding of meat tenderness and influence of fat content on meat flavour. Sci Technol Dev 9:65-70.
  46. Vasanthi C, Venkataramanujam V, Dushyanthan K. 2007. Effect of cooking temperature and time on the physico-chemical, histological and sensory properties of female carabeef buffalo meat. Meat Sci 76:274-280. https://doi.org/10.1016/j.meatsci.2006.11.018
  47. Voutila L, Mullen AM, Ruusunen M, Troy D, Puolanne E. 2007. Thermal stability of connective tissue from porcine muscles. Meat Sci 76:474-480. https://doi.org/10.1016/j.meatsci.2006.12.012
  48. Wang H, Weir CE, Birkner ML. Ginger B. 1958 Studies on enzymatic tenderisation of meat. III. Histological and panel analyses of enzyme preparations from three muscles distinct sources. J Food Sci 23:423-438. https://doi.org/10.1111/j.1365-2621.1958.tb17590.x
  49. Woessner JF Jr. 1961. The determination of hydroxyproline in tissue and protein samples containing small proportions of this imino acid. Arch Biochem Biophys 93:440-447. https://doi.org/10.1016/0003-9861(61)90291-0

피인용 문헌

  1. Enzyme preparations in the technology of whole muscle turkey products vol.677, pp.3, 2018, https://doi.org/10.1088/1755-1315/677/3/032084
  2. Sensory and Physical Characteristics of M. biceps femoris from Older Cows Using Ginger Powder (Zingibain) and Sous Vide Cooking vol.10, pp.8, 2018, https://doi.org/10.3390/foods10081936
  3. Degradation of myofibrillar and sarcoplasmic proteins as a function of marinating time and marinade type and their impact on textural quality and sensory attributes of m. semitendinosus beefsteak vol.45, pp.9, 2018, https://doi.org/10.1111/jfpp.15691
  4. Improving tenderness and quality of M. biceps femoris from older cows through concentrate feeding, zingibain protease and sous vide cooking vol.180, pp.None, 2018, https://doi.org/10.1016/j.meatsci.2021.108563