Browse > Article
http://dx.doi.org/10.5851/kosfa.2009.29.3.317

Application of a Kiwifruit (Actinidia chinensis) to Improve the Textural Quality on Beef Bulgogi Treated with Hydrostatic Pressure  

Lee, Eun-Jung (Food Safety Research Center, Korea Food Research Institute)
Oh, Se-Wook (Food Safety Research Center, Korea Food Research Institute)
Lee, Nam-Hyouck (Food Processing Research Center, Korea Food Research Institute)
Kim, Young-Ho (Food Processing Research Center, Korea Food Research Institute)
Lee, Dong-Un (Department of Food Science and Technology, Chung-Ang University)
Yamamoto, Katsuhiro (Department of Food Science, Rakuno Gakuen University)
Kim, Yun-Ji (Food Safety Research Center, Korea Food Research Institute)
Publication Information
Food Science of Animal Resources / v.29, no.3, 2009 , pp. 317-324 More about this Journal
Abstract
In order to reduce the increased hardness of beef bulgogi due to hydrostatic pressure (HP), kiwifruit (Actinidia chinensis) was applied. To understand the changes of shear force in beef bulgogi with kiwifruit induced by HP, changes in chemical properties of myofibril (Mf) with 10% kiwifruit induced by HP were investigated. From the SDS-PAGE patterns of Mf with 10% kiwifruit, there was an observed increase in the degradation of myosin heavy chain (MHC) by HP (300-500 MPa) to that by 0.1 MPa. This result indicates that HP may enhance enzyme action from a kiwifruit for the degradation of MHC, and the similar phenomenon occurred in the beef bulgogi with kiwifruit induced by HP. The shear force of beef bulgogi without a kiwifruit induced by 400 and 500 MPa significantly increased compared to that by 0.1 MPa (p<0.05). However, in the beef bulgogi with 10% or 20% kiwifruit, the shear force induced by 400 or 500 MPa was similar or slightly lower than that by 0.1 MPa. Consequently, adding kiwifruit to bulgogi could reduce the hardness of HP-induced beef bulgogi due to the enzyme action in the kiwifruit accelerated by HP.
Keywords
hydrostatic pressure; kiwifruit (Actinidia chinensis); bovine myofibril; beef bulgogi;
Citations & Related Records
Times Cited By KSCI : 4  (Citation Analysis)
Times Cited By Web Of Science : 1  (Related Records In Web of Science)
Times Cited By SCOPUS : 1
연도 인용수 순위
1 Hong, G. -P., Shim, K. -B., Choi, M. -J., and Min, S. -G. (2008) Effects of thermal processing combined with high pressure on the characteristics of cooked pork. Korean J. Food Sci. Ani. Resour. 28, 415-421   과학기술학회마을   DOI   ScienceOn
2 Kamphuis, I. G., Drenth, J., and Baker, E. N. (1985) Thiol protease. J. Mol. Biol. 182, 317-329   DOI   PUBMED
3 Kato, A. and Nakai, S. (1980) Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochem. Biophys. Acta. 624, 13-20   DOI   PUBMED   ScienceOn
4 Margey, D. M., Patterson, M. F., and Moss, B. W. (1997) Effect of various temperature/pressure combinations on microbiological and quality attributes of poultry meat. In: High Pressure Research in the Biosciences and Biotechnology, Heremans, K. (eds), 307-310
5 Trespalacios, P. and Pla, R. (2007) Synergistic action of transglutaminase and high pressure on chicken meat and egg gels in absence of phosphates. Food Chem. 104, 1718-1727   DOI   ScienceOn
6 Yamamoto, K., Miura, T., and Yasui, T. (1990) Gelation of myosin filament under high hydrostatic pressure. Food Struct. 9, 269-277
7 Wada, M., Suzuki, T., Yaguti, Y., and Hasegawa, T. (2002) The effects of pressure treatments with kiwi fruit protease on adult cattle semitendinosus muscle. Food Chem. 78, 167-171   DOI   ScienceOn
8 Yamamoto K., Yoshida, Y., Morita, J., and Yasui, T. (1994) Morphological and physicochemical changes in the myosin molecules induced by hydrostatic pressure. J. Biochem. 116, 215-220   DOI
9 Ishioroshi, M., Samejima, M., Arie, Y., and Yasui, T. (1980) Effect of blocking the myosin-actin interaction in heatinduced gelation of myosin in the presence of actin. Agr. Biol. Chem. 44, 2185-2194   DOI
10 Yamamoto, K., Hayashi, S., and Yasui, T. (1993) Hydrostatic pressure-induced aggregation of myosin molecules in 0.5 M KCl at pH 6.0. Biosci. Biotechnol. Biochem. 57, 383-389   DOI
11 Iwasaki, T. and Yamamoto, K. (2002) Effect of high hydrostatic pressure on chicken myosin subfragment-1. Int. Biol. Macromol. 30, 227-232   DOI   ScienceOn
12 Lee, E. -J., Kim, Y. -J., Lee, N. -H., Hong, S. -I., and Yamamoto, K. (2007) Differences in properties of myofibrillar proteins from bovine semitendinosus muscle after hydrostatic pressure or heat treatment. J. Sci. Food Agri. 87, 40-46   DOI   ScienceOn
13 Neuhoff, V., Arold, N., Taube, D., and Ehrhardt, N. (1988) Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G250 and R-250. Electrophoresis 9, 255-262   DOI   ScienceOn
14 Jung, S., Ghoul, M., and Lamballerie-Anton, M. (2000) Changes in lysosomal enzyme activities and shear values of high pressure treated meat during ageing. Meat Sci. 56, 239- 246   DOI   ScienceOn
15 Visschers, R. W. and Harmen de Jongha, H. J. (2005) Disulphide bond formation in food protein aggregation and gelation. Biotechnol. Advances. 23, 75-80   DOI   ScienceOn
16 Ellman, G. L. (1959) Tissue sulfhydryl groups. Archives of Biochem. Biophy. 82, 70-77   DOI   PUBMED   ScienceOn
17 McDowall, M. A. (1970) Anionic proteinase from Actinidia chinensis preparation and properties of the crystalline enzyme. Eur. J. Biochem. 14, 214-221   DOI   ScienceOn
18 Sompongse, E., Itoh, Y., and Obataka, A. (1996) Effect of cryoprotectants and reducing reagent on the stability of actomyosin during ice storage. Fishery Sci. 62, 110-113   DOI
19 Hsu, K. -C., Hwang, J. -S., Yu, C. -C., and Jao, C. -L. (2007) Changes in conformation and in sulfhydryl groups of actomyosin of tilapia (Orechromis niloticus) on hydrostatic pressure treatment. Food Chem., 103, 560-564   DOI   ScienceOn
20 Kim, Y. -J., Lee, E. -J., Lee, N. -H., Kim, Y. -H., and Yamamoto, K. (2007) Effects of hydrostatic pressure treatment on the physicochemical, morphological, and textural properties of bovine semitendinosus muscle. Food Sci. Biotechnol. 16, 49-54   과학기술학회마을
21 Pla, R. and Trespalacios, P. (2007) Simultaneous application of transglutaminase and high pressure to improve functional properties of chicken gels. Food Chem. 100, 264-272   DOI   ScienceOn
22 Lee, E. -J., Kim, Y. -J., Lee, N. -H., Kim, Y. -H., Seo, E. -J., and Yamamoto, K. (2004) Effects of hydrostatic pressure on biochemical characteristics of myofibrillar protein extracted from bovine semitendinosus muscle. Food Sci. Biotechnol. 13, 632-635   과학기술학회마을
23 Lewis, D. A. and Luh, B. S. (1988) Application of actinidin from kiwifruit to meat tenderization and characterization of beef muscle protein hydrolysis. J. Food Biochem. 12, 147-158   DOI
24 Shigehisa, T., Ohmori, T., Saito, A., Taji, .S., and Hayashi, R. (1991) Effects of high hydrostatic pressure on characteristics of pork slurries and inactivation of microorganisms associated with meat and meat products. International Journal of Food Microbiol. 412, 207–216
25 Mohamed, S. A., Fahmy, A. S., Mohamed, T. M., and Hamdy, S. M. (2005) Proteases in egg, miracidium and adult of Fasciola gigantica characterization of serine and cysteine proteases from adult. Comp. Biochem. Physiol. Part B. Biochem. Mol. Biol. 142, 192-200   DOI   ScienceOn
26 Kim, E. -M., Choe, I. -S., and Hwang, S. -G. (2003) Effects of singular manner or mixed type treatment of proteases isolated from pear, pineapple and kiwifruit on actomyosin degradation. Korean J. Food Sci. Ani. Resour. 23, 193-199   과학기술학회마을
27 Lawmmli, V. K. (1970). Cleavage of structural proteins during the head of bacteriophage T4. Nature 227, 680-685   DOI   PUBMED   ScienceOn
28 Li-Chen, E. (1983) Heat-induced changes in the proteins of whey protein concentrate. J. Food Sci. 48, 47-56   DOI
29 Iwasaki, T. and Yamamoto, K. (2003) Changes in rabbit skeletal myosin and its subfragments under high hydrostatic pressure. Int. Biol. Macromol. 33, 215-220   DOI   ScienceOn