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Microbial Transglutaminase Improves the Property of Meat Protein and Sausage Texture Manufactured with Low-quality Pork Loins

  • Katayama, K. ;
  • Chin, K.B. ;
  • Yoshihara, S. ;
  • Muguruma, M.
  • Received : 2004.11.15
  • Accepted : 2005.06.23
  • Published : 2006.01.01

Abstract

Microbial transglutaminase (MTGase) was investigated to determine whether it was an effective binding agent for the processing of low-quality pork loins. MTGase especially promoted the coagulation of myosin heavy chain (MHC). However, the effect of MTGase on MHC from low-quality meat was less than that from the normal meat when the reaction time was not enough. The breaking strength of the heat-induced gel made of myosin B from low-quality meat with MTGase was lower than that of normal meat. Sausage made with low-quality meat with MTGase did not exhibit improved hardness, as compared to that made with normal meat. Results of this study indicated that use of low-quality meat in the manufacture of sausage was feasible to get textural property equal to that of normal meat sausage, when a half or more of the raw material was normal meat and MTGase was used in the sausage.

Keywords

Microbial Transglutaminase;Low-quality Pork Loin;Sausage Texture

References

  1. Chin, K. B. and B. K. Chung. 2003. Utilization of transglutaminase for the development of low-fat, low-salt sausages and restructured meat products manufactured with pork ham and loins. Asian-Aust. J. Anim. Sci. 16:261-265 https://doi.org/10.5713/ajas.2003.261
  2. Gornall, A. G., C. J. Bardawill and M. M. David. 1949. Determination of serum protein by means of the biuret reaction. J. Biol. Chem. 177:751-766
  3. Ishioroshi, M. 1996. Shokuniku Seibun no Kako Tokusei. (Ed. A. Okitani). Niku no Kagaku, pp. 131-137. Tokyo, Japan: Asakura shoten (in Japanese)
  4. Kuraishi, C., J. Sakamoto, K. Yamazaki, Y. Susa, C. Kuhara and T. Soeda. 1997. Production of restructured meat using microbial transglutaminase without salt or cooking. J. Food Sci. 62:488- 490, 515 https://doi.org/10.1111/j.1365-2621.1997.tb04412.x
  5. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227:680- 685 https://doi.org/10.1038/227680a0
  6. Park, K. H., M. Muguruma, T. Fukazawa and T. Ito. 1975. Relationship between superprecipitating activity and constituents of myosin B prepared from normal and PSE porcine muscle. Agric. Biol. Chem. 39:1363-1370 https://doi.org/10.1271/bbb1961.39.1363
  7. Okitani, A. 1996. Shokuniku no Oishisa to Jukusei. (Ed. A. Okitani). Niku no Kagaku, pp. 85. Tokyo, Japan: Asakura shoten (in Japanese)
  8. Macdougall, D. B. 1994. Color of Meat. In: (Ed. A. M. Pearson, and T. R. Dutson), Quality attributes and their measurement in meat, poultry and fish products. Adv. Meat Res., 9. Blackie Academic & Professional an imprint of Chapman & Hall Glasgow, UK
  9. Yasui, T., T. Gotoh and J. Morita. 1973. Influence of pH and temperature on properties of myosin A in glycerol-treated fiber bundles. J. Agric. Food Chem. 21:241-246 https://doi.org/10.1021/jf60186a019
  10. Motoki, M. and K. Seguro. 1998. Transglutaminase and its use in food processing. Trends in Food Science and Technology, 9:204-210 https://doi.org/10.1016/S0924-2244(98)00038-7
  11. Nakai, H., F. Saito, T. Ikeda, S. Ando and A. Komatsu. 1975. Standard models of pork colour. In: Bulletin of the National Institute of Animal Industry, 29:69-74
  12. Szent-Györgyi, A. 1951. Chemistry of muscle contraction, 2nd ED, pp. 151-152. New York: Academic Press
  13. Ando, H., M. Adachi, K. Umeda, A. Matsuura, M. Nonaka, R. Uchio, H. Tanaka and M. Motoki. 1989. Purification and characteristics of a novel transglutaminase derived from microorganisms. Agric. Biol. Chem. 53:2613-2617 https://doi.org/10.1271/bbb1961.53.2613
  14. Erwanto, Y., M. Muguruma, S. Kawahara, T. Tsutsumi, K. Katayama, K. Yamauchi, T. Morishita, Y. Kai and S. Watanabe. 2002. Effect of heating on polymerization of pig skin collagen using microbial transglutaminase. Asian-Aust. J. Anim. Sci. 15:1204-1209 https://doi.org/10.5713/ajas.2002.1204
  15. Penny, R. W. 1967. The effect of post-mortem conditions on the extractability and adenosine triphosphatase activity of myofivrillar proteins of rabbit muscle. J. Food Technol. 2:325- 338 https://doi.org/10.1111/j.1365-2621.1967.tb01356.x
  16. Numata, M., H. Yamada, T. Nakamura and M. Muguruma. 1989. The effect of transglutaminase on heat-induced gelation and water holding capacity of myosin B. Nippon Shokuhin Kogyo Gakkaishi, 36:832-838 (in Japanese) https://doi.org/10.3136/nskkk1962.36.10_832
  17. Bourne, M. C. 1978. Texture profile analysis. Food Technol. July. 62-66
  18. Sakamoto, H., Y. Kumazawa and M. Motoki. 1994. Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions. J. Food Sci. 59:866-871 https://doi.org/10.1111/j.1365-2621.1994.tb08146.x
  19. Muguruma, M., K. Tsuruoka, K. Katayama, Y. Erwanto, S. Kawahara, K. Yamauchi, S. K. Sathe and T. Soeda. 2003. Soybean and milk proteins modified by transglutaminase improves chicken sausage texture even at reduced level of phosphate. Meat Sci. 63:191-197 https://doi.org/10.1016/S0309-1740(02)00070-0
  20. Tseng, T. F., M. T. Chen and D. C. Liu. 2002. Purification of transglutaminase and its effects on myosin heavy chain and actin of spent hens. Meat Sci. 60:267-270 https://doi.org/10.1016/S0309-1740(01)00132-2
  21. Margossian, S. S. and S. Lowey. 1982. Preparation of myosin and its subfragments from rabbit skeletal muscle. (Ed. D. W. Frederiksen and L. W. Cunningham). Methods Enzymol., Vol. 85, pp. 55-59. New York: Academic Press https://doi.org/10.1016/0076-6879(82)85009-X
  22. Yasui, A. and Y. Aoyagi. 2000. Measurement of Food Components. (Ed. T. Sugahara and A. Maekawa). Handbook of Food Analysis, pp. 15-32. Tokyo, Japan: Kenpakusha (in Japanese)

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