Food Science of Animal Resources (한국축산식품학회지)

Korean Society for Food Science of Animal Resources (한국축산식품학회)
권호 표지
DOI QR코드

DOI QR Code

Effects of Sonication on the Water-solubilization of Myofibrillar Proteins from Breast Muscle of Spent Hen

초음파처리가 노계 가슴육 근원섬유단백질의 수용화에 미치는 영향

  • Published : 2007.12.30
Download PDF
⟨ Previous Next ⟩

Abstract

Effects of sonication on water-solubilization of myofibril from breast muscle of spent hen effects investigated in this study. To evaluate effect of salt concentration and pH, salt concentration was varied with range from 0.1 to 0.8 M, and pH was varied with range from 6.0 to 8.0. Solubility, SDS-PAGE, viscosity and ATPase activity of sonicated myofibril were measured. Solubility of myofibrillar protein containing 0.1 M NaCl at pH 8.0 after sonication was above 90%. Main components of soluble protein by SDS-PAGE were myosin heavy chain and actin. That is, it indicated breaking of myofibril structure by sonication. Also, viscosity of soluble protein increased, but Ca- and Mg-ATPase activities decreased by increasing sonication time. From these results, we concluded that most of myofibrillar proteins were denatured by sonication.

본 연구에서는 노계 가슴육의 단백질 식품 소재로서 활용도를 높이기 위하여 초음파를 이용한 근원섬유 단백질의 수용화에 대하여 검토하였다. 근원섬유에 0.1-0.8 M NaCl, pH 6.0-8.0이 되도록 조절한 후 20 kHz에서 초음파 처리를 하였다. 그런 다음 이들의 용해도, SDS-PAGE, 점도, Ca- 및 Mg-ATPase 활성을 측정하였다. 각각의 처리 조건에서 용해도를 검토한 결과 초음파에 의해서 용해도는 증가하였으며 0.1 M NaCl, pH 8.0에서 약 90%를 나타내었다. 용해된 성분을 SDS-PAGE를 이용하여 검토한 결과 대부분 myosin heavy chain 및 actin에 상당하는 성분이 검출되었으며, 초음파에 의한 단백질의 분리는 근원 섬유 구조의 붕괴에 의한 것으로 사료되었다. 한편, 초음파에 의한 점도의 변화는 용해도가 높을수록 점도도 증가하였다. 그러나, Ca- 및 Mg-ATPase 활성은 초음파에 의해서 급격히 저하하였으며, 초음파에 의해서 분리되는 단백질은 대부분 변성이 진행된 상태인 것으로 사료되었다.

Keywords

References

  1. Acton, J. C., Ziegler, G. R., Carpenter, Z. I., and Dill, C. W. (1983) Functionality of muscle constituents in the processing of comminuted meat products. Food Sci. Nutr. 18, 99-121
  2. Alberts, B., Bray, D., Lewis, J., Raff, M., Roberts K., and Watson, J. D. (1983) Cytoskeleton. In: Molecular Biology of the Cell, Garland Publishing, Inc, New York & London, pp 549
  3. Antonomanolaki, R. E., Vareltzis, K. P., Georgakis, S. A., and Kaldrymidou, E. (1999) Thermal gelatin properties of surimi-like material made from sheep meat. Meat Sci. 52, 429-435 https://doi.org/10.1016/S0309-1740(99)00026-1
  4. Cho, D. H. and Yu, Y. H. (2000) Effect of ultrasonic treatment on the isolation of the Chlamydospore of Cylindrocarpon destructans causing root rot of Panax ginseng. J. Ginseng Res. 24, 53-57
  5. Chung, K., Kim, W. I., Hong, I. K., and Park, K. A. (2000) Ultrasonic energy effects on squalene extraction from amaranth seed. Appl, Chem. 4, 149-152
  6. Gornall, A. G., Bardawill, C. J., and David, M. M. (1949) Determination of serum proteins by means of the biuret reaction. J. BioI. Chem. 177, 751-766
  7. Hamm, R. (1986) Functional properties of the myofibrillar system and their measurements. In Muscle as Food. Bechtel, P. J. (ed.), Academic Press, New York, pp. 135-199
  8. Huxely, H. E. (1963) Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle. J Mol. Biol. 7, 281-308 https://doi.org/10.1016/S0022-2836(63)80008-X
  9. Kandos, N. and Luche, J. L. (2001) Sonochemistry of carbohydrate compounds. Carbohyd. Res. 332, 115-131 https://doi.org/10.1016/S0008-6215(01)00081-7
  10. Kim, H. S., Kim, C. H., Kwon, M. C. and Song, Y. K. (2006) Anticancer activity of ultrasonicfied extracts from seawaterbased culture of the microalgae Spirulina platensis. J. Korean Fish. Soc. 39, 318-325 https://doi.org/10.5657/kfas.2006.39.4.318
  11. Kim, J. H., Kim, D. H., You, J. H., Kim, C. H., Kwon, M. C., and Seong, N. S. (2005) Immuno-regulatory activities ofvarious fractions from Ehpedrae Sinica STAPE, Rubus Coreanus Miq. and Angelica gigas Nakai extracts with ultasonication. J. Med. Crop Sci. 13, 161-170
  12. Kim, S. M., Park, S. M., Choi, H. M., and Lee, K. T. (1999) Optimal Processing parameters of low molecular weight carrageenan by ultrasound. J. Korean Fish. Soc. 32, 495-500
  13. 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
  14. Lawrie, R. A. (1985) Developments Meat Science-3. Elsevier Applied Science Publishers Ltd., London, pp. 25
  15. Lee, B. S., Ko, M. S., Kim, H. J., Kwak, I. S., Kim, D. H., and Chung, B. W. (2006) Separation of 6-gingerol from ginger and antioxidative activity. Korean J. Biotechnol. Bioeng. 21, 484-488
  16. McClements, D. (1995) Advantages in the application of ultrasound in food analysis and processing. Trends Food Sci. Technol. 6, 293-299 https://doi.org/10.1016/S0924-2244(00)89139-6
  17. Moson, T. and Cordmas, E. (1996) Ultrasound intensification of chemical processing and related operations - a review. Trans Instit, Chem, Engineers 74(A), 511-516
  18. Nowsad, A. A. K. N., Kanoh, S., and Niwa, E. (2000) Thermal gelation characteristics of breast and thigh muscles of spent and broiler and their surimi. Meat Sci. 54, 169-175 https://doi.org/10.1016/S0309-1740(99)00091-1
  19. Richardson, R. I. and Jones, J. M. (1987) The effects of salt concentration and pH upon water-binding, Water-holding and protein extractabilityof turkey meat. Int. J. Food Sci. Tech. 22, 683-692 https://doi.org/10.1111/j.1365-2621.1987.tb00537.x
  20. Shin, H. J. and Lee, D. C. (2003) Study on the process to decrease the molecular weight of ${\beta}-1.6-branched\;{\beta}-1.3-D-glucans$. Korean J. Biotechnol. Bioeng. 18, 352-355
  21. Smyth, A. B. and ONiel, E. (1997) Heat-induced gelation properties of surimi from mechanically separated chicken. J. Food Sci. 62, 326-330 https://doi.org/10.1111/j.1365-2621.1997.tb03994.x
  22. Srinivasan, S., Xiong, Y. L., and Decker, E. A. (1996) Inhibition of protein and oxidation in beef heat surimi -like material by antioxidants and combinations of pH, NaCl, and buffer type in the washing media. J. Agric. Food Chem. 44, 119-125 https://doi.org/10.1021/jf950385i
  23. Xiong, Y. L., Cantor, A. H., Pescatore, A. J., Blanchard, S. P., and Straw, M. L. (1993) Variations in muscle chemical composition, pH and protein extractability among eight different broiler crosses. Poultry Sci. 72, 583-588 https://doi.org/10.3382/ps.0720583
  24. Yang, R., Shin, W. C., Oh, D. W., Jhin, H. S., and Kim, K. T. (1986) Comparison of biochemical characteristics of myofibrillar proteins from red muscle and white muscle. J. Kor. Food Sci. Technol. 3, 173-180

Cited by

  1. Quality Evaluation of Spent Hen and Broiler with Pulsed Electric Field and Super Heated Steam Treatment vol.29, pp.5, 2016, https://doi.org/10.9799/ksfan.2016.29.5.753
  2. Solubilisation of muscle proteins from chicken breast muscle by ultrasonic radiations in physiological ionic medium vol.1, pp.1, 2015, https://doi.org/10.1080/23311932.2015.1046716
  3. Solubilization of myofibrillar proteins in water or low ionic strength media: Classical techniques, basic principles, and novel functionalities vol.57, pp.15, 2017, https://doi.org/10.1080/10408398.2015.1110111
  4. Study on the Quality Characteristics of Pork By-product on the Different Pretreatment Process vol.32, pp.6, 2016, https://doi.org/10.9724/kfcs.2016.32.6.716
  5. Physico-Chemical Characteristics Evaluation of Spent Hen and Broiler vol.28, pp.4, 2015, https://doi.org/10.9799/ksfan.2015.28.4.527